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FOOD SCIENCE AND TECHNOLOGY
FOOD CHEMISTRY
DONGFENG WANG
HONG LIN
JIANQIAN KAN
LINWEI LIU
XIAOXING ZENG
AND
SHENGRONG SHEN
EDITORS
New York
Copyright © 2012 by Nova Science Publishers, Inc.
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Additional color graphics may be available in the e-book version of this book.
Preface vii
Contributors ix
About the Editors xi
Chapter 1 Introduction 1
Dongfeng Wang
Chapter 2 Water 9
Jianqian Kan and Guoqing Huang
Chapter 3 Carbohydrates 35
Dongfeng Wang, Jipeng Sun, Guoqing Huang,
Xiaolin Zhou and Liping Sun
Chapter 4 Lipids 107
Shengrong Shen, Dongfeng Wang and Undurti N. Das
Chapter 5 Proteins 137
Hong Lin, Lisha Wu and Shuhui Wang
Chapter 6 Vitamins 191
Yibin Zhou, Dongfeng Wang and Ping Dong
Chapter 7 Minerals 223
Dongfeng Wang, Lina Yu, Haiyan Li, Bin Zhang,
Shuhui Wang and Xingguo Liang
Chapter 8 Food Flavors 247
Xiaoxiong Zeng and Guaoqing Huang
Chapter 9 Food Additives 273
Linwei Liu and Shiyuan Dong
Chapter 10 Toxicants in Foods 305
Wang Dongfeng, Guoqing Huang and Shuhui Wang
Index 353
PREFACE
Foods consist of a large quantity of compounds, of which, some are original from plant or
animal materials, some are new ones generated during processing or preservation, some are
intentionally added by manufacturers, and some are contaminants produced during
processing, preservation or packaging. These compounds undergo various changes during
processing and storage and it is hence necessary to understand the effects of processing or
storage on these compounds so as to enhance the nutrition, palatability and safety of foods.
The purpose of Food Chemistry is to elucidate the structure, physicochemical properties,
nutrition and safety of major food constituents and their changes occurred during processing
and storage. Due to the extreme importance, Food Chemistry has been accepted as a major
fundamental course for food-related majors.
Though food chemistry has a history of more than 200 years, it developed into a
relatively independent system in the late 1960‘s. Since then, the United States, Japan,
Germany and other countries published several authoritative food chemistry textbooks,
including Latest Food Chemistry edited by Hayashi Junzo and Kitamura Mitsuo (Japan),
Food Chemistry by Sakurai Yoshito (Japan), Food Chemistry by Owen R. Fennema (United
States), Food Chemistry by Belitz HD (Germany), Food Chemistry by Zhang Wang (China),
and Food Chemistry by Dongfeng Wang (China). Of the works, the publications edited by
Fennema and Belitz HD have been widely chosen by university students as textbook.
However, the two books contain too many contents and part of them overlaps with those
stated in Biochemistry and Organic Chemistry. Besides, the two books are too expensive for
readers in developing countries.
Hence, there is an urgent demand to publish a simplified Food Chemistry textbook that
most university students can afford, which is the case of this book. This book presents the
chemistry and properties of the six essential nutrients contained in foods, including water,
carbohydrates, lipids, proteins, vitamins and minerals, and their changes occurred during food
processing and storage. In addition, this book also deals with the chemistry and properties of
flavors, food additives and toxic substances in foods. This book is simplified and cheaper
than previously published books without reducing its academic level, and reflects the latest
advances in food chemistry. This work can be used as a textbook by university students and
especially suitable for students in developing countries and non-English speaking countries
for bilingual delivery.
The authors would like to thank the postgraduates of the Laboratory of Food Chemistry
and Nutrition of Ocean University of China, including Mei Ding, Yan Li, Lu Yu, Xingya Li,
viii Dongfeng Wang, Hong Lin, Jianqian Kan et al.
Xiang Gao, Wen Zhou, Zhe Xu, Min Wang, Mengqi Li, and Chunsheng Li, for assistance in
literature collection and typesetting, and Ocean University of China for funding the
publication.
CONTRIBUTORS
Undurti N Das
Jawaharlal Nehru Technological University, Kakinada-533 003, India
Liping Sun
College of Chemistry and Engineering, Kunming University of Science and Technology,
Yunnan Province, China
Jipeng Sun
Third Institute of Oceanography State Oceanic Administration, Xiamen, China
Lina Yu
Shandong Peanut Research Institute, Qingdao, China
Xiaoling Zhou
Medical College of Shantou University, Shantou, Guangdong Province, China
Bin Zhang
School of Food and Pharmacy & Medical School, Zhejiang Ocean University, Zhushang
City, Zhejiang Province, China
Haiyan Li
College of Food Science and Engineering, Ocean University of China, Qingdao, China
Banping Wang
College of Food Science and Engineering, Ocean University of China, Qingdao, China
Xingguo Liang
College of Food Science and Engineering, Ocean University of China, Qingdao, China
ABOUT THE EDITORS
Dongfeng Wang is a professor of the College of Food Science and Engineering at the
Ocean University of China. He has published many books related to food chemistry as editor-
in-chief, including Food Chemistry (2007), Advanced Food Chemistry (2009), Chemistry of
Toxic Substances in Foods (2005), Technology of Experiment & Study of Tea Biochemistry
(1997), Experiments on Food Quality & Food Safety (2004) and Technology of Experiments
on Food Science and Engineering (2007). He has published over 120 original papers that
reflect his research interests in food chemistry, tea biochemistry, carbohydrate chemistry, and
preservation. He has received many teaching & academic honors, including The Second Prize
for Advanced Science and Technology of China in 2010, The First Prize for Advanced
Science and Technology from Ministry of Education of the People‘s Republic of China in
2009, Distinguished Teacher Awards from Shandong Province of China in 2006, and Award
for Young Scientists from Anhui Province in 2000. Professor Wang received his BS degree of
agriculture in 1982 from Anhui Agricultural College (Anhui, China), the MS degree of tea
biochemistry in 1988 from Zhejiang Agricultural University (Zhejiang, China), and the PhD
degree of inorganic biochemistry of food in 1999 from University of Science and Technology
of China (Hefei, China).
Lingwei Liu is a professor of the College of Food Science & Engineering in Northwest
A&F University, Yangling, ShaanXi, China. He has done intensive researches related to food
chemistry, food analysis, nutrition and food safety. Professor Liu received the BS degree of
food science from Northwest Agriculture University (ShaanXi, China) in 1982 and the PhD
xii Dongfeng Wang, Hong Lin, Jianqian Kan et al.
degree of food science from Northwest Agriculture & Forest University (ShaanXi, China) in
1995.
Hong Lin received the BS degree in 1984, the MS degree in 1990, and the PhD degree
in 1998 in seafood science from the Ocean University of China. Professor Lin is a famous
expert in the seafood safety field and his research area covers novel marine organism-derived
chemical and biological hazard discovery, quality control during seafood processing, and fast
hazard detection method development. Professor Lin has been granted 4 invention patents,
published more than 100 original articles, and edited 4 academic books, including Seafood
Safety (2010), Aquatic Nutrition and Safety (2007), Effective Use of Aquatic Resources
(2007), and Fish Preservation Technologies (2000).
Xiaoxiong Zeng received the BS degree from Hunan Agricultural University in 1985,
the MS degree from Zhejiang Agricultural University in 1988, and the PhD degree from
Shizuoka University (Shizuoka, Japan) in 2000. Dr. Zeng is now a professor of the College of
Food Science and Technology, Nanjing Agricultural University, China. He is one of the
authors or corresponding author of over 100 original papers related to food chemistry, food
biotechnology and glycobiology.
Yibin Zhou is a professor of the Department of Food Science and Engineering at Anhui
Agricultural University, Anhui, China. He had edited Food Chemistry (in Chinese) as an
assistant, and is the author or corresponding author of over 40 original papers on
carbohydrates, food engineering, and biotechnology.
Guoqing Huang is a lecturer of the College of Food Science and Engineering, Qingdao
Agricultural University, Qingdao, China.
Shiyuan Dong is a lecturer of the College of Food Science and Engineering, Ocean
University of China, Qingdao, China.
Chapter 1
INTRODUCTION
Dongfeng Wang
College of Food Science and Engineering, Ocean University of China, Qingdao, China
ABSTRACT
Food Chemistry is a fundamental discipline for students, engineers, and
professionals engaged in the food industry. This chapter provides an overview of this
discipline, including its definition, purpose, development, and its role in food science and
engineering.
food. The purpose of Food Chemistry is to elucidate the structure, physical and chemical
properties, nutritional value as well as safety of these components, their changes undergone
during storage and processing, and the effects of these changes on food nutrition and
palatability. The knowledge is of great importance in improving food quality, developing new
food resources, evolving food processing and storage technologies, upgrading food packaging
materials, and increasing food safety and quality.
Water
Carbohydrates
Proteins
Lipids
Minerals
Natural
Vitamins
Pigments
Hormones
Flavor components
Toxic substances
Food components
Natural additives
Food Addtives
Synthetic additives
Unnatural
From processing
Contaminants
From environmental pollution
Figure 1-1. Composition of foods.
As the trading of foods between regions and countries increased, both consumers and
manufacturers had urgent needs on the information of water contents and the presence non-
food components in foods. Meanwhile, driven by the rapid development of analysis measures,
the desire to understand the natural characteristic of foods also grew. In 1860, German
scholars Hanneberg W. and Stohman F. invented a method for the simultaneous
determination of water, crude fat, ash, and nitrogen contents. Several years later, diets
containing solely proteins, lipids, and carbohydrates were found insufficient for maintaining
life.
In 1900s, with the advancement of analytical techniques and the biochemistry subject and
the rapid development of the food industry, requirements on new food processing
technologies and prolonged storage life emerged, which drove the quick development of food
chemistry. During this period, a growing number of researches papers were published and the
quantity of related journals increased significantly as well, including Archives of Biochemistry
and Biophysics (initiated in 1942), Journal of Agricultural and Food Chemistry (initiated in
1953) and Food Chemistry (initiated in 1966). Due to the emergency of increasing deep and
systematic publications, Food Chemistry gradually developed into an independent subject.
Chinese scholars Yanbin Xia and Ruijin Yang divide the history of Food Chemistry into
four stages.
Stage one: Many natural components were separated from plants and animals and were
identified, including lactic acid, citric acid, malic acid, and tartaric acid. The knowledge was
not systematic yet and was reported mainly by chemists.
Stage two: In the early 1900s (1820 ~ 1850), food chemistry developed quickly along
with the development of agricultural chemistry and gained much importance in Europe.
Specialized food chemistry laboratories were established and many professional journals
related to food chemistry were issued. Meanwhile, adulteration became a serious issue and
the need for impurity determination propelled the development of food chemistry. In this
stage, Justus von Liebig invented an optimized method for quantitative analysis of organic
substances and published Researches on the Chemistry of Food in 1847.
Stage three: In the middle 1900s century, the British scientist Arthur Hill Hassall reported
the microscopic images of pure and adulterated foods and food chemistry came into the
microanalysis time. In 1871, Jean Baptis M.D.M. proposed that diets containing only
proteins, carbohydrates and lipids were insufficient to sustain human‘s life. The interests on
the nutritional requirements further accelerated the development of food chemistry. Until the
first half of the 20th century, the majority of components in foods were identified and the
number of literatures related to chemistry food increased markedly. Food chemistry then
turned to be a mature and independent subject in mid-20th century.
Stage four: Food chemistry is now in the fourth stage. With the rapid development of
society, economy, science and technology, and the improvement of living standards,
consumers raise higher requirements on food security, nutrition, palatability, and
convenience. Meanwhile, to realize the transformation from traditional to scaled,
standardized, and modernized processing of foods, more and more new technologies,
materials, and equipment are used, which markedly drive the rapid development of food
chemistry. Besides, the advancement of basic chemistry, biochemistry, instrumental analysis
and other related subjects guarantee the rapid development of food chemistry. Food chemistry
has become a most important subject for food scientists [1, 2].
4 Dongfeng Wang
Due to the rapid development of food chemistry, some important reactions, including the
Millard reaction, caramelization, lipid auto-oxidation, starch gelatinization and aging,
polysaccharide hydrolysis and modification, protein hydrolysis and denaturation, pigment
discoloration, vitamin degradation, metal-catalyzed reactions, enzyme-catalyzed reactions, fat
hydrolysis and transesterification, lipid thermo-oxidative decomposition and polymerization,
flavor compound changes, action mechanisms of food additives, generation of harmful
ingredients as well as postharvest physiology, are identified in foods. The knowledge on these
reactions greatly enhances the development of the food industry.
chemistry should not only ensure the healthcare and enjoyment attributes of food
components, but also guide consumers on rational diet selection. The concept of nutrition has
evolved significantly due to social development and the change of the healthy status of
consumers. How to reduce the incidences of diet-related diseases, such as cardio-
cerebrovascular diseases, cancers, and diabetes, has turned to be a new major task of food
industry. In addition to the healthcare attribute, foods should also provide desirable flavors so
that consumers enjoy the eating process. The emergence of biotechnologies and new food
processing technologies guarantees the safety of foods.
Contamination of foods by pollutants is currently a worldwide concern due to global
environmental deterioration. The analysis and identification of trace and ultramicro
substances are of vital importance to the nutrition value and the control of toxicants of foods.
The development of food chemistry has been associated with the healthy status and
civilization level of human.
Each type of food contains a large number of components and is thereby a much complex
system. Hence, the research methods of food chemistry are quite different from those of
common chemistry subjects. In food chemistry, the knowledge on the chemical composition,
physicochemical properties, and changes of food components must be associated with the
nutrition, enjoyment, and safety of foods. The experimental design of food chemistry should
reveal the complex composition of food systems and the changes of the nutrition value,
enjoyment, and safety of foods during processing and storage. The interactions between food
components and their changes occurred during storage and processing (such as ultra-high
pressure, high temperature, freezing, presence or absence of oxygen) are extremely complex.
Hence, many researches are carried out in simplified and stimulated models, which must be
then verified in real food systems.
The experiments of food chemistry include mainly physicochemical experiments and
sensory evaluation experiments. Physicochemical experiments reveal the composition of
foods and the structures of the components, including nutrients, toxicants, and flavors; while
sensory experiments evaluate the texture, flavor, and color changes of foods through visual
inspection.
Foods or food materials undergo a series of changes during storage, transport, processing,
and sales. The changes include: enzymatic and chemical reactions in raw and fresh materials;
changes caused by water activity variance; component decomposition, polymerization, and
denaturation under violent conditions (high temperature, high pressure, mechanical actions);
oxidation induced by oxygen or other oxidants; photochemical reactions; and migration of
packaging materials to foods. Of the changes, non-enzymatic browning, lipid oxidation and
hydrolysis, protein hydrolysis and denaturation, protein cross-linking, oligosaccharide and
polysaccharide hydrolysis, and change of the presence form of natural pigments and their
degradation, are the most important reactions for the food industry. Of the reactions, some are
desired, but some are unexpected and must be avoided during processing (Table 1-2). The
mechanisms and control of these reactions constitute the key contents of food chemistry.
Introduction 7
Table 1-2. Part reactions occurred during food processing and storage and their
influences on foods [3, 4]
The research fruits and methods of food chemistry have been widely absorbed by the
food industry and greatly promote the development of the food industry. In the last decades,
some new subjects and research areas, such as structural chemistry, free radical chemistry,
membrane separation, edible package, microencapsulation, extrusion, superfine comminution,
bioactive packaging, supercritical extraction, molecular distillation, membrane catalysis, bio-
reactor, toxicant chemistry of foods, molecular nutrition, and nutria-genomics, have been
established. These new technologies and subjects will undoubtedly facilitate the rapid
development of the food industry, which in turn benefits the improvement of the food
chemistry subject.
REFERENCES
[1] Wang, DF. Food Chemistry.1st edition. Beijing: Chemistry Industry Press; 2007
[2] Damodaran, S; Parkin, KL; Fennema, OR. Fennema’s Food Chemistry. 4th edition.
New York: CRC Press; 2007.
[3] Kan, JQ. Food Chemistry. 1st edition. Beijing: China Agricultural University Press;
2002.
[4] Wang, Z. Food Chemistry. 1st edition. Beijing: China Light Industry Press; 2005.
In: Food Chemistry ISBN: 978-1-61942-125-7
Editors: D.Wang, H. Lin, J. Kan et al. © 2012 Nova Science Publishers, Inc.
Chapter 2
WATER
ABSTRACT
Water is an important component in many foods. Its content and occurrence status
significantly affect the flavor, texture, and stability of foods. This chapter deals with the
various physical and chemical properties of water and ice and the interactions with other
components in foods. Water occurs in multiple states due to interactions with solutes and
the interactions significantly affect the bioavailability of water to chemical reactions and
microorganisms.
To distinguish the differences between water content and its bioavailability, the term
water activity (aw) is proposed and its application in food stability predication are
detailed. The relationship between water content and aw can be presented by moisture
sorption isotherm (MSI), which is very useful in designing the concentration and
dehydration processes of foods.
In addition to aw, molecular mobility (Mm) has also been proposed to predict food
stability. Its definition and its effect on food stability are also a concern of this chapter.
Water is a predominant constituent in many foods (Table 1). Water in proper amount,
location, and orientation profoundly influences the structure, appearance, and taste of
foods and their susceptibility to spoilage.
Because medium water supports chemical reactions and water is a reactant in
hydrolytic processes, the removal of water from foods retards many reactions and inhibits
the growth of microorganisms, thus improving the shelf lives of a number of foods.
Through physical interaction with proteins, polysaccharides, lipids and salts, water
contributes significantly to food texture.
Water is essential to life: as an important governor of body temperature, as a solvent,
as a carrier of nutrients and waste products, as a reactant and reaction medium, as a
lubricant and plasticizer, as a stabilizer of biopolymer conformation, as a likely facilitator
of the dynamic behavior of macromolecules, including their catalytic (enzymatic)
properties, and in other ways yet unknown.
10 Jianqian Kan and Guoqing Huang
Figure 1. Schematic model of a single HOH molecule: (a) sp3 configuration, and (b) van der Waals radii
for a HOH molecule in the vapor state [1].
Water 11
In the vapor state, the bond angle of an isolated water molecule is 104.5°. The O-H
internuclear distance is 0.96 Å and the van der Waals radii for oxygen and hydrogen are 1.40
and 1.2 Å respectively.
Figure 2 Hydrogen bonding of water molecules in a tetrahedral configuration. Open circles are oxygen
atoms and closed circles are hydrogen atoms. Hydrogen bonds are represented by dashed lines [1].
Table 2. Coordination number and distance between two water molecules [2]
Table 3. Comparisons of the melting and boiling points of methanol, dimethyl ether, and
water
Figure 4. Unit cell of ordinary ice at 0°C. Circles represent oxygen atoms of water molecules. Nearest-
neighbor internuclear O-O distance is 2.76 Å; θ is 109° [3].
Mixing of solutes and water results in altered properties of both water and solutes.
Hydrophilic solutes change the structure and mobility of adjacent water, and water causes
changes in the reactivity, and sometimes structure, of hydrophilic solutes. Hydrophobic
groups of added solutes interact only weakly with adjacent water. Interactions between water
and specific classes of solutes are considered below.
14 Jianqian Kan and Guoqing Huang
Figure 5. Likely arrangement of water molecules adjacent to sodium chloride. Only water molecules in
plane of paper are shown [3].
Water 15
Figure 8. Hydrogen bonding (dotted lines) of water to two kinds of functional groups occurring in
proteins [3].
Figure 9. Examples of a three-molecule water bridge in papain; 23, 24, and 25 are water molecules [4].
16 Jianqian Kan and Guoqing Huang
Figure 10. Schematic depiction of a globular protein undergoing hydrophobic interaction. Open circles
are hydrophobic groups, ―L-shaped‖ entities around circles are water molecules oriented in accordance
with a hydrophobic surface, and dots represent water molecules associated with polar groups [2].
Water 17
Foods are composed of proteins, polysaccharides, minerals, pigments, and many other
constituents in addition to water. These constituents interact with water and significantly
affect the properties and status of water. Generally, the water in foods can be classed as ―bulk
water‖ and ―bound water‖.
1. Bound water associates with nonaqueous constituents more tightly and its vapor
pressure is much lower than bulk water. More energy is required for removing bound
water than bulk water and the removal of bound water might irreversibly degrade the
flavor, texture, and other properties of foods.
2. Bound water freezes in much lower temperature than bulk water. This explains why
plant seeds and microbial spores can survive low temperatures. In contrast, juicy
fruits and vegetables have much higher water contents and their tissues are
susceptible to damage by ice crystals in low temperatures.
3. Bound water cannot dissolve solutes.
4. Bulk water can be utilized by microorganisms, while bound water cannot.
3. WATER ACTIVITY
Intensive researches have indicated that no relationship can be established between the
water content of a food with its physiochemical properties or stability. It has also been
Water 19
observed that various types of foods with the same water content differ significantly in
perishability. Thus, water content alone is not a reliable indicator of perishability. This
situation is attributable, in part, to differences in the intensity with which water associates
with nonaqueous constituents. The term ―water activity‖ (aw) was developed to account for
the intensity with which water associates with various nonaqueous constituents. Experience
shows that food stability, safety, and other properties can be predicted far more reliably from
aw than from water content.
P ERH
aw RVP
P0 100 (1)
where, RVP is the relative vapor pressure; P is the partial vapor pressure of food moisture at
temperature T; P0 is the saturation vapor pressure of pure water at temperature T, and ERH is
the equilibrium relative humidity at temperature T.
Equation (1) applies only to ideal solutions and thermodynamically equilibrium systems
and the values obtained are only approximate for food systems. The RVP of a food can be
determined by placing it in a closed chamber for a time sufficient to achieve apparent
equilibrium (constant weight) and then measuring either pressure or relative humidity in the
chamber. The vapor pressures of the aqueous solution of solutes are generally lower than that
of pure water and aw hence falls in the range 0~1.
d ln aw H
d (1/ T ) R (3)
where, T is the absolute temperature, R is the gas constant, and ⊿H is the isosteric net heat of
sorption at the water content of the sample.
By rearrangement, equation (2-4) can be obtained:
H 1
Inaw k
R T (4)
where, R and T have the same meaning as those in Equation (2-3), ⊿H is the latent heat of
vaporization of pure water (40.5372kJ/mol), and k is calculated from the following formula:
20 Jianqian Kan and Guoqing Huang
Absolute temperature of the sample - Absolute temperature of pure water in vapor pressure p
k
Absolute temperature of pure water in vapor pressure p
Plots of Inaw versus 1/T are not always linear over broad temperature ranges, and they
generally exhibit sharp breaks with the onset of ice formation. Figure 11. is a plot of logaw
versus 1/T, illustrating that (a) the relationship is linear at subfreezing temperatures, (b) the
influence of temperature on RVP is typically far greater at subfreezing temperatures than at
above-freezing temperatures, and (c) a sharp break occurs in the plot at the freezing point of
the sample. Below freezing temperatures, the water activity (aw) can be calculated as follow:
p ff pice
aw
p0 ( SCW ) p0 ( SCW )
(5)
where, pff is the partial pressure of water in partially frozen food, p0(SCW) is the vapor pressure
of pure supercooled water, and pice is the vapor pressure of pure ice.
Two important distinctions should be noted when comparing aw values at above- and
below-freezing temperatures. First, at above-freezing temperatures, aw is a function of sample
composition and temperature, with the former factor predominating. At subfreezing
temperatures, aw becomes independent of sample composition and depends solely on
temperature; that is, in the presence of an ice phase aw values are not influenced by the kind
or ratio of solutes present. Hence, the knowledge of aw at a subfreezing temperature cannot be
used to predict aw at an above-freezing temperature. Second, as the temperature is changed
sufficiently to form or melt ice, the meaning of aw, in terms of food stability, also changes.
For example, in a product at -15°C (aw =0.86), microorganisms will not grow and chemical
reactions will occur slowly. However, at 20°C and aw 0.86, some chemical reactions will
occur rapidly and some microorganisms will grow at moderate rates.
Figure 11. Relationship between relative vapor pressure and temperature for a complex food above and
below freezing [5].
Water 21
A plot of water content (expressed as mass of water per unit mass of dry material) of a
food versus aw at constant temperature is known as a moisture sorption isotherm (MSI). The
MSI of a food system is of great importance for the following reasons:
Shown in Figure 12. is a schematic MSI for a high-moisture food plotted to include the
full range of water content from normal to dry. Omission of the high-moisture region and
expansion of the low-moisture region, as is usually done, yields an MSI that is much more
useful (Figure 13).
Several substances that have MSIs of markedly different shapes are shown in Figure 14.
Isotherms with an S shape are characteristic of most foods. Foods such as fruits, confections,
and coffee extract that contain large amounts of sugar and other small soluble molecules, and
are not rich in polymeric materials exhibit a J-type isotherm shown as curve 1 in Figure 14.
Figure 12. Schematic moisture sorption isotherm encompassing a broad range of moisture contents [3].
22 Jianqian Kan and Guoqing Huang
Figure 13. Generalized moisture sorption isotherm for the low-moisture segment of a food (20°C) [3].
Figure 14. Resorption isotherms for various foods and biological substances. Temperature 20°C, except
for number 1, which is 40°C: (1) confection (main component powdered sucrose), (2) spray-dried
chicory extract, (3) roasted Columbian coffee, (4) pig pancreas extract powder, (5) native rice starch
[6].
The MSI can be prepared in two ways. For high-moisture foods, the desorption isotherm
can be obtained by plotting the water content versus aw during dehydration. For low-moisture
foods, the resorption isotherm can be determined by plotting water content versus aw during
addition of water to the foods. The shape and position of the isotherm are determined by
several factors including sample composition, physical structure of the sample (e.g.,
crystalline or amorphous), sample pretreatments, temperature, and methodology
To deeply understanding the meaning and usefulness of sorption isotherms it is
sometimes appropriate to divide them into three zones as indicated in Figure 13.
Water 23
(1) Water present in Zone I of the isotherm is most strongly absorbed and least mobile.
This water associates with accessible polar sites by water-ion or water-dipole
interactions, is unfreezable at -40°C, has no ability to dissolve solutes, and is not
present in sufficient amount to have a plasticizing effect on the solid. It behaves
simply as part of the solid. The high-moisture end of Zone I (boundary of Zones I
and II) corresponds to the ―Brunauer-Emmett-Teller (BET) monolayer‖ moisture
content of the food. Zone I water constitutes a tiny fraction of the total water in a
high-moisture food material.
(2) Water added in Zone II occupies first-layer sites that are still available. This water
associates with neighboring water molecules and solute molecules primarily by
hydrogen bonding, is slightly less mobile than bulk water, and most of it is
unfreezable at -40°C, it exerts a significant plasticizing action on solutes, lowers their
glass transition temperatures, and causes incipient swelling of the solid matrix, leads
to acceleration in the rate of most reactions. Water in Zones I and Zone II usually
constitutes less than 5% of the water in a high-moisture food material.
(3) Further addition of water (Zone III) causes a glass-rubber transition in samples
containing glassy regions, a very large decrease in viscosity, a very large increase in
molecular mobility, and commensurate increases in the rates of many reactions. This
water is freezable, available as a solvent, and readily supports the growth of
microorganism. Zone III water is referred to as bulk-phase water. The bulk-phase
water of Zone III, either entrapped or free, usually constitutes more than 95% of the
total water in a high-moisture food.
An MSI prepared by addition of water (resorption) to a dry sample will not necessarily be
superimposable on an isotherm prepared by desorption. This lack of superimposability is
referred to as ―hysteresis,‖ and a schematic example is shown in Figure 15. Typically, at any
given p/p0, the water content of the sample will be greater during desorption than during
resorption. MSIs of polymers, glasses of low molecular-weight compounds, and many foods
exhibit hysteresis. The following explanations have been proposed for the occurrence of
hysteresis:
1. Some moisture cannot be released during desorption due to the interaction with
nonaqueous components.
2. Different vapor pressures are needed for evacuating or filling the moisture entrapped
by capillaries.
3. The tissues of foods are changed during desorption. As a result, moisture cannot bind
the same tightly to the tissues during resorption and higher aw is resulted in the same
water content.
4. The magnitude of hysteresis, the shape of the curves, and the inception and
termination points of the hysteresis loop can vary considerably depending on factors
such as nature of the food, the physical changes it undergoes when water is removed
or added, temperature, the rate of desorption, and the degree of water removal during
desorption.
24 Jianqian Kan and Guoqing Huang
Range
Inhibited Microorganisms Foods generally within this range
of aw
Highly perishable (fresh) foods and canned
Pseudomonas, Escherichia
fruits, vegetables, meat, fish, and milk;
Proteus, Shigella, Klebsiella,
1.00–0.95 cooked sausages and breads; foods
Bacillus, Clostridium
containing up to approximately 40% (w/w)
perfringens, some yeasts
sucrose or 7% sodium chloride
Salmonella, Vibrio Some cheeses (Cheddar, Swiss, Muenster,
parahaemolyticus, C. Provolone),cured meat (ham), some fruit
0.95–0.91 botulinum, Serratia, juice concentrates; foods containing up to
Lactobacillus, some molds, 55% (w/w) sucrose or 12% sodium
yeasts (Rhodotorula, Pichia) chloride
Fermented sausage (salami), sponge cakes,
Many yeasts (Candida,
dry cheeses, margarine; foods containing
0.91–0.87 Torulopsis, Hansenula,
up to 65% (w/w)sucrose (saturated) or
Micrococcus)
15% sodium chloride
Most fruit juice concentrates, sweetened
Most molds (mycotoxigenic condensed milk, chocolate syrup, maple
penicillia), Staphylococcus and fruit syrups; flour, rice, pulses
0.87–0.80
aureus, most Saccharomyces containing 15–17% moisture; fruit cake;
(bailii) spp., Debaryomyces country-style ham, fondants, high-ratio
cakes
Most halophilic bacteria, Jam, marmalade, marzipan, glacé fruits,
0.80–0.75
mycotoxigenic aspergilli some marshmallows
Xerophilic molds (Aspergillus Rolled oats containing approximately 10%
chevalieri, A. candidus, moisture; grained nougats, fudge,
0.75–0.65
Wallemia marshmallows, jelly, molasses, raw cane
sebi),Saccharomyces bisporus sugar, some dried fruits, nuts
Osmophilic yeasts
(Saccharomyces
Dried fruits containing 15–20% moisture;
0.65–0.60 rouxii), few molds
some toffees and caramels; honey
(Aspergillus echinulatus,
Monascus bisporus)
Pasta containing approximately 12%
0.50 No microbial proliferation moisture; spices containing approximately
10% moisture
Whole egg powder containing
0.40 No microbial proliferation
approximately 5% moisture
Cookies, crackers, bread crusts, etc.
0.30 No microbial proliferation
containing 3–5% moisture
Whole milk powder containing 2–3%
moisture; dried vegetables containing
0.20 No microbial proliferation approximately 5% moisture; corn flakes
containing approximately 5% moisture;
country style cookies, crackers
Water 25
Figure 16. Relationships among relative water vapor pressure, food stability and sorption isotherms. (A)
Microbial growth versus p/p0. (B) Enzymatic hydrolysis versus p/p0. (C) Oxidation (nonenzymatic)
versus p/p0. (D) Maillard browning versus p/p0. (E) Miscellaneous reaction rates versus p/p0. (F) Water
content versus p/p0. All ordinates are ―relative rate‖ except for F [3].
26 Jianqian Kan and Guoqing Huang
Shown in Table 6. are various common microorganisms and the range of aw permitting
their growth. Most bacterial growth is affected above water activity 0.90 and most yeast and
molds, however, can grow above water activity 0.80. No microorganisms survive in water
activity lower than 0.5.
5.2. Water Activity (aw) and Chemical and Enzymatic Reactions in Foods
The relationship between water activity and the rates of chemical and enzymatic reactions
is very complex. First, water is a reactant of many chemical and enzymatic reactions and its
content significantly influences the balance of the reactions. Second, water can bind to polar
or ionic groups through hydration and significantly affects their contact with other reactants.
Third, many biomolecules swell in the presence of water and more reaction sites are exposed,
leading to accelerated reaction. However, high water contents dilute solutes and retard the
proceeding of reactions.
As shown in Figure 16, all chemical and enzymatic reactions, except oxidation reactions,
have the lowest reaction rates at the boundary of Zone I and Zone II, corresponding aw
0.2~0.3.
Figure 6.(c) indicates the relationship between lipid oxidation rate and aw. Within a
specific aw range, the rate of lipid oxidation decreases with the increase of aw. When aw
further increases to the boundary of Zone II and Zone III, the lipid oxidation rate starts to rise.
Generally, the lowest lipid oxidation rate is found in aw 0.35.
The moisture in food might either enhance or suppress lipid oxidation. When aw is lower
than 0.35, lipid oxidation is suppressed for the following reasons. Firstly, water covers the
oxidizable sites and prevents their contact with oxygen. Secondly, water hydrates ions and
eliminates the oxidation reactions initiated by ions. Thirdly, water hydrogen bonds with
hydroperoxides and retards the oxidation induced by them. Finally, water facilitates the
binding between free radicals and disrupts the chain reactions involving the free radicals.
When aw is greater than 0.35, water enhances lipid oxidation though two ways. Water
dissolves solutes and facilities their movement. Meanwhile, biomolecules swell in high water
content and more accessible sites are exposed.
Water 27
Figure 16(c) illustrates the influence of aw on Maillard reaction. It could be seen that
Maillard reaction occurs mainly in aw range 0.3~0.7. In low aw, the water-solute hydrogen
bonding and the association of water with neighboring molecules retard the movement of
solutes and subsequently suppress the Maillard reaction. As the aw increases gradually,
reactants and products move more easily and the rate of Maillard reaction increase as a result.
When aw exceeds a specific value, solutes are diluted and the Maillard reaction is
consequently retarded.
As shown in Figure 16, all the chemical enzymatic reactions, except oxidation, occur the
slowest in the boundary of Zone I and Zone II (corresponding to aw 0.2~0.3) and further
decrease of the water content does not change the minimum rates. The water content at the
first-encountered rate minimum is the ―BET monolayer‖ water content. The BET theory is a
theory proposed by Brunauer, Emett, and Teller in 1938 and the theory was named after them.
The BET monolayer value of a food provides a good first estimate of the water content
providing maximum stability of a dry product. One can use the BET equation to compute the
monolayer value:
aw 1 c 1
m(1 - aw ) m1c m1c (10)
where, aw is water activity, m is water content (in g H2O/g dry matter), m1 is the BET
monolayer value, and c is a constant.
From this equation, it is apparent that a plot of versus aw, known as a BET plot, should
yield a straight line. An example for native potato starch, with aw replaced by p/p0, is shown
in Figure 17. The linear relationship, as is generally acknowledged, begins to deteriorate at
p/p0 values greater than about 0.35.
The BET monolayer value can be calculated as follows:
1
Monolyaer value (m1 ) (11)
(y intercept) (slope)
From Figure 17, the y intercept is 0.6. Calculation of the slope from Figure 17 yields a
value of 10.7. Thus,
1
m1 0.088g H2O/g dry matter
0.6 10.7
In this particular instance, the BET monolayer value corresponds to a aw, of 0.2.
28 Jianqian Kan and Guoqing Huang
Figure 17. BET plot for native potato starch (resorption data, 20°C) [8].
(1) All water converted to ice increases 9% in volume. Consequently, ice crystals formed
in a disperse system can cause locally increased pressures, which can in turn cause
mechanical damage. Hence water will leave the cells, which will shrink
considerably; enzymes will release into solution, whereby they become active; this
may result in a product of poor quality.
(2) Nonaqueous constituents become concentrated in the unfrozen phase, the unfrozen
phase changes significantly in properties such as pH, titratable acidity, ionic strength,
viscosity, freezing point (and all other colligative properties), surface and interfacial
tension, and oxidation reduction potential. In addition, solutes sometimes crystallize,
supersaturated oxygen and carbon dioxide may be expelled from solution, water
structure and water-solute interactions may be drastically altered, and
macromolecules will be forced closer together, making interactions more probable.
These changes in concentration-related properties often favor increases in reaction
rates. Thus, freezing can have two opposing effects on reaction rate: lowering
temperature, as such, will always decrease reaction rates, and freeze-concentration,
as such, will sometimes increase reaction rates.
In addition to water activity, molecular mobility (Mm) has also been used to predicate
and control the stability of foods. Molecular mobility involves all the movements of food
Water 29
components during storage that are related to the stability and processability and includes:
molecular movement or deformation caused by liquid movement or mechanical stretch;
Brownian movements or atomic rotation caused by molecular diffusion; relative movement of
materials in containers or pipelines. Some properties and behavioral characteristics of food
that are dependent on Mm are shown in Table 7. Mm is mainly influenced by hydration and
temperature. The water content and the interaction between water and nonaqueous
components determine the fluidity of the liquid phase. As temperature is increased, the
translational and rotational motion (Mm) becomes easier, while upon cooling to Tg,
translational motion of polymer segments stop.
It is necessary to introduce the concept of state diagram before the discussion of the
relationship between Mm and the stability of dried, partially dried, or frozen foods, State
diagrams are supplemented phase diagrams, and contain equilibrium information as well as
information on conditions of nonequilibrium and metastable equilibrium ―states‖, and are
appropriate because foods that are dried, partially dried, or frozen do not exist in a state of
thermodynamic equilibrium. A simplified temperature-composition state diagram for a binary
system is shown in Figure 19.
Table 7. Some properties and behavioral characteristics of foods that are governed by
molecular mobility (diffusion-limited changes in products containing amorphous
regions) [9]
Figure 19. State diagram of a binary system. Assumptions: maximal freeze concentration, no solute
crystallization, constant pressure, no time dependence. Tml is the melting point curve, TE is the eutectic
point, Tms is the solubility curve, Tg is the glass transition curve, and Tg‘is the solute-specific glass
transition temperature of a maximally freeze concentrated solution. Heavy dashed lines represent
conditions of metastable equilibrium. All other lines represent conditions of equilibrium [1].
Most foods are so complex that they cannot be accurately or easily represented on a state
diagram. Differential scanning calorimetry (DSC) can successfully determine the glass
transition temperature (Tg) of simple polymer systems, but is inapplicable to complex food
systems. The Tg of complex food systems is often determined by using dynamic mechanical
analysis (DMA) or dynamic mechanical thermal analysis (DMTA).
Glass transition temperature (Tg) is the temperature at which a supersaturated solution
(amorphous liquid) converts to a glass, and is dependent on solute type and water content. Tg‘
is a special Tg that applies only to samples containing ice, and only when ice has been formed
so maximum freeze-concentration occurs (very slow cooling). Below Tg or Tg‘ of a complex
sample, all but small molecules lose their translational mobility while retaining limited
rotational and vibrational mobility.
In the glassy state, the food will have greater stability (shelf life). As long as the
temperature remain below Tg‘, the composition of the system is virtually fixed. This implies
physical stability: crystallization, for instance, will not occur. But some chemical reactions
may still proceed, albeit very slowly because of the high viscosity and the low temperature.
approach is of questionable value or is clearly unsuitable. Some examples are (1) chemical
reactions whose rates are not strongly influenced by diffusion, (2) desirable or undesirable
effects achieved through the action of specific chemicals (e.g., alteration of pH or oxygen
tension), (3) situations in which sample Mm is estimated on the basis of a polymeric
component (Tg of polymer) and where Mm of small molecules that can penetrate the polymer
matrix is a primary determinant of the product attribute of interest, and (4) growth of
vegetative cells of microorganisms (p/p0 is a more reliable estimator than Mm). Examples of
diffusion-limited reactions are proton transfer reactions, radical recombination reactions,
acid-base reactions involving transport of H+ and OH-, many enzyme-catalyzed reactions,
protein folding reactions, polymer chain growth, and oxygenation/deoxygenation of
hemoglobin and myoglobin. At constant temperature and pressure, three primary factors
govern the rate at which a chemical reaction will occur: a diffusion factor, D (to sustain a
reaction, reactants must first encounter each other), a frequency-of-collision factor, A
(number of collisions per unit time following an encounter), and a chemical activation-energy
factor, Ea (once a collision occurs between properly oriented reactants the energy available
must be sufficient to cause a reaction, that is, the activation energy for the reaction must be
exceeded). For a reaction to be diffusion-limited, it is clear that factors A and Ea must not be
rate-limiting. Diffusion-limited reactions typically have low activation energies (8–25
kJ/mol). When a food is cooled and/or reduced in moisture content so that all or part of it is
converted to a glassy state, Mm is greatly reduced and diffusion-limited properties become
stable.
It should be noted that the plasticizing effect is valid only when water gets entrapped in
the amorphous region of the components. In the absence of environmental effects, moisture
content is the predominant factor that affects Tg, especially in low-moisture foods.
Table 8. Relationship between the Tg and moisture content of pre-gelatinized starch and
wheat starch
For example, the Tg of the anhydrous mixture of 50% starch and 50% sucrose is about
60°C; when the moisture content increases to 2%, the Tg decreases to 20°C; when the
moisture content further increases to 6%, Tg falls to as low as 10°C. Table 8. lists the
relationships between the Tg and moisture content of native wheat starch and pre-gelatinized
starch. It could be seen that the Tg of both the materials increases along the decrease of
moisture content.
Figure 25. Relationship between average molecular weight and dextrose equivalent (DE) of commercial
starch hydrolysis products with Tg‘ [10].
ice-free foods. Because aw can be measured conveniently and quickly, it is still the major
indicator for judging food stability.
REFERENCES
[1] Fennema, OR. Food Chemistry. 3rd edition. New York: Marcel Dekker; 1996.
[2] Damodaran, S; Parkin, KL; Fennema, OR. Fennema’s Food Chemistry. 4th edition.
New York: CRC Press; 2007.
[3] Belitz, HD; Gorsch, W. Food Chemistry. 2nd edition. Berlin: Springer-Verlag, 1999.
[4] Berendsen, HJC. Specific interactions of water with biopolymers. In: Franks, F. Water -
A Comprehensive Treatise. New York: Plenum Press, 1975; 293-349.
[5] Fennema, OR. Enzyme kinetics at low temperature and reduced water activity. In:
Crowe, JH; Clegg, JS. Dry Biological Systems. New York: Academic Press, 1978; 297-
322.
[6] Ferry, JD. The evaluation of water activity in aqueous solutions from freezing point
depression. International Journal of Food Technology, 1980, 16, 21-30.
[7] Beuchat, LR. Microbial stability as affected by water activity. Cereal Foods World,
1981, 26, 345-349.
[8] Van den Berg, C. Vapour Sorption Equilibria and Other Water-Starch Interactions; A
Physico-Chemical Approach, PhD thesis, Wageningen: Wageningen Agricultural
University, 1981.
[9] Slade, L; Levine, H. Beyond water activity: Recent advances based on an alternate
approach to the assessment of food quality and safety. Critical Reviews in Food Science
and Nutrition. 1991, 30, 115–360.
[10] Levine, H., and L. Slade (1986). A polymer physico-chemical approach to the study of
commercial starch hydrolysis products (SHPs). Carbohydrate Polymers, 6, 213–244.
In: Food Chemistry ISBN: 978-1-61942-125-7
Editors: D.Wang, H. Lin, J. Kan et al. © 2012 Nova Science Publishers, Inc.
Chapter 3
CARBOHYDRATES
ABSTRACT
Carbohydrates account for 3/4 of the dry weight of terrestrial plants and algae and
can be found in all the plants, animals and microorganisms that human can eat.
Carbohydrates are one of the major components in foods. The compounds not only
provide human beings with energy, but also impart foods with desired textures and tastes.
Carbohydrates undergo various changes during food processing and storage and yield
substantial compounds that affect the flavor, quality and safety of foods. This chapter
deals with the classification of carbohydrates and their most important functional
properties, in which, special attention is paid to the non-enzymatic browning reaction, its
influences on food quality, and its control. The structures, proportions, and applications
of most important polysaccharides and oligosaccharides in foods are then detailed one by
one. Dietary fiber as an important healthy diet component is also introduced at the end of
this chapter.
36 Dongfeng Wang, Jipeng Sun, Guoqing Huang et al.
INTRODUCTION
Carbohydrates Classification
Carbohydrates are natural organic compounds converted from carbon dioxide and water
through photosynthesis of plants. According to the number of monosaccharide units,
carbohydrates are divided into monosaccharides, oligosaccharides and polysaccharides.
Monosaccharides are the simplest sugars in structure and can no longer be hydrolyzed. A
monosaccharide often contains three, four, five, or six carbon atoms and its functional group
might be the aldehyde or keto group. An oligosaccharide generally consists of 2 to 20
monosaccharide units and can be hydrolyzed to simple sugars. Oligosaccharides are often
found in glycoproteins or lipopolysaccharides. According to monosaccharide composition,
oligosaccharides are further divided into homo-oligosaccharides and hetero-oligosaccharides.
A homo-oligosaccharide is composed of only one type of monosaccharide, such as maltose
and dextrin with degree of polymerization less than 20. In contrast, a hetero-oligosaccharide
consists of two or more types of monosaccharide units. Polysaccharides, with degree of
polymerization greater than 20, are formed by dehydration of multiple monosaccharide units
and consist of homo-polysaccharides, such as cellulose and starch, and hetero-polysaccharide
such as seaweed and tea polysaccharides. Polysaccharides can also be classified into plant,
animal and microbial polysaccharides according to their origins or storage and functional
polysaccharides according to their biological functions.
Polysaccharides contain multiple hydroxyl groups and can covalently attach to the side
chains of proteins or peptides to form glycoproteins or protein polysaccharides.
Polysaccharides also react with carboxyl-containing molecules to form esters such as
lipopolysaccharide (LPS) and sulfate polysaccharides. Besides, polysaccharides can complex
with transition metals due to the presence of hydroxyl groups. These polysaccharide
derivatives are generally referred to as polysaccharide complexes.
Carbohydrates in Foods
Starch is one of the most abundant carbohydrates in plant-derived foods and is the most
abundant in seeds, roots and tubers. Glycogen is found in animal-derived foods especially in
muscle and liver, and it is structurally similar to amylopectin. Starch is insoluble in aqueous
solutions and does not contribute to the sweetness of foods, unless it was hydrolyzed into
oligosaccharides or glucose.
The majority of plant-derived foods contain only a small amount of free sugars and most
sugars are present as starch. For example, maize contains only 0.2%~0.5% D-glucose,
0.1%~0.4% D-fructose and 1%~2% sucrose. Free sugars not only provide the sweet taste for
foods, but also participate in flavor and color formation during thermal processing. An
increase in free sugar content during processing improves food quality. For example, to
increase the sweetness of sweet corn, sweet corn must be harvested before sugars are
converted to starch.
Many fruits are often harvested before they are fully mature for two reasons. Firstly, the
high rigidity of immature fruits facilitates their transport and storage. Secondly, starch is
Carbohydrates 37
converted to sucrose or other sweet sugars during transport and storage. This change makes
the fruits sweet and soft. The post-harvest ripening is the reverse of the starch synthesis
process in the grain, tuber and root of plants.
The contents of water-soluble sugars in processed foods are generally higher than the
corresponding materials, because sugars are intentionally added by manufacturers to meet the
requirements of consumers on flavor and color.
Carbohydrates are the main constitutes in foods and are closely related to the nutrition,
color, taste, texture and functionality of foods. Carbohydrates are essential nutrients for
human body and 70% of the energy needed by human body is provided by carbohydrates.
Reducing sugars with free aldehyde or ketone contribute to the formation of colors and
flavors in food thermal processing and thus affects food quality. Besides, many free sugars
are sweet and positively affect the mouth feel of foods. Some carbohydrates, such as guar
gum and carrageenan, have special viscoelastic properties and can give pleasant textures for
foods. Cellulose, pectin, and many other macromolecules can provide desired food texture
and adjust the intestine flora as dietary fibers. In addition, some polysaccharides or
oligosaccharides, such as lentinan and tea polysaccharides, have specific physiological
functions and can be directly added to foods as functional ingredients.
Carbohydrate Structure
Monosaccharide
Monosaccharide generally contains 5 or 6 carbon atoms with the general formula
Cn(H2O)n. Monosaccharides are asymmetric and optically active. Taking glyceraldehyde as an
example, the C atom in position 2 is chiral and glyceraldehyde therefore has two enantiomers.
D-glyceraldehyde is dextrorotatory and is distinguished by the prefix ―+‖ or ―d‖ and L-
glyceraldehyde is levorotatory and is labeled with prefix ―-‖ or ―l‖. Monosaccharides derived
from D-glyceraldehyde are termed D-ketones and those from L-glyceraldehyde are termed L-
ketones.
The carboxyl group of a monosaccharide ring can react with a free hydroxyl group in the
same molecule to yield more stable 5- or 6-membered hemiacetal or hemiketal, called lactol.
Lactol formation provides a new chiral center. Thus, there are two additional diastereomers
for each pyranose or furanose. These isomers are called anomers and are denoted as α- or β-
forms. Most naturally occurring simple sugars are present in the D form. Hence, it is
sometimes unnecessary to indicate the configuration of these sugars.
Monosaccharides can produce various biologically important derivatives after chemical
modification. Monosaccharide derivates that have been identified in foods include
38 Dongfeng Wang, Jipeng Sun, Guoqing Huang et al.
Sugar alcohols have lower calorific values and are sweeter than their monosaccharide
precursors. Sugar alcohols do not undergo the typical reactions of sugars and are stable
against heating and pH variations. Sugar alcohols share the same chemical properties as
common alcohols and are not involved in the Maillard reaction.
Inositol is a cyclic hexatomic alcohol and has 9 stereoisomers (Table 3-1), of which, 7 are
mesomeric and 2 are optically active. Among the isomers, only the myo isomer is biologically
active. Inositol is often present as free form in the muscle, heart, liver, and lung of animals.
The hydroxyl groups in inositol can react with phosphate acid to produce phosphoinositides.
In higher plants, all the six hydroxyl groups in inositol are phosphated to inositol
hexaphosphate. Phosphoinositides can complex with Ca2+ and Mg2+, forming calcium and
magnesium salts of phytic acid.
Glycosides are the condensation products of monosaccharides and non-saccharide ligand
through the hemiacetal hydroxyl of monosaccharide. The bond between sugar and ligand is
referred to as the glycosidic linkage.
Glycosides contain one furanose or pyranose ring and the new chiral center might be
present in the alpha or beta form. Most glycosides occur in the beta form in nature.
Oligosaccharides
Oligosaccharides are water-soluble and occur widely in nature. Generally, naturally
occurring oligosaccharides contain less than six monosaccharide units, of which, most are
disaccharides and trisaccharides. For example, sucrose and maltose are disaccharides, and
affinose is a trisaccharide.
Some high-molecular weight oligosaccharides, such as cyclodextrins (or schardinger
dextrin), have gained wide applications in the food industry. Cyclodextrins consist of 6~8 D-
glucopyranose units, corresponding to α-, β-, and γ- cyclodextrins respectively. In addition to
molecular weight, the three cyclodextrins differ in their water solubility and cavity size, as
shown in Table 3-2. X-ray diffraction reveals that α-cyclodextrin is a highly symmetric
cylinder. Six C6 hydroxyl groups are located in the bottom of the cylinder and 12 C2 and C3
hydroxyl groups are arranged on the cylinder top. The inner wall of the cylinder is covered
with C-H groups and hence more hydrophobic than the external surface. Cyclodextrins are
used to stabilize hydrophobic substances by entrapping them in the cavity during food
processing.
Polysaccharides
Structure
The degrees of polymerization (DP) of polysaccharides range from 21 to several
thousands. Polysaccharides consist of one type of structural unit (homoglycans) or multiple
types of structure units (heteroglycans) and the structural units can be linked in a linear (such
as cellulose and amylose) or branched pattern (such as amylopectin and glycogen). The
monosaccharide units generally occur periodically in polysaccharides and each periodic
repeat contains one or more alternative structural units. An example of the exceptions is the
carbohydrate components in glycoproteins, in which the monosaccharide compositions are
nonperiodic all along the chain.
The DPs of polysaccharides are heterogeneous, that is, polysaccharides have no fixed
molecular weight (MW) and display the Gauss distribution. The heterogeneity of
polysaccharide molecular weight is associated with the metabolic status of organisms. For
example, the MW of glycogen is closely dependent on the blood glucose level of animals.
When the blood glucose level is low, the liver glycogen is hydrolyzed and glycogen is
cleaved to small segments. In contrast, when the blood glucose level increases, glycogen is
synthesized in the liver and the glycogen MW is increased. In addition, many polysaccharides
are present as complexes, such as glycoproteins, glycopeptides and glycolipids. In this case,
the MWs of polysaccharides are determined by much more factors than polysaccharide alone.
Conformation
Polysaccharides are either straight or branched molecules, but they have much more
complex conformations. Some typical conformations are elucidated in the following by taking
glucans and some other polysaccharides as examples.
This conformation is typical for 1,4-linked β-D-glucopyranosyl residues (Figure 3-1), for
instance that in cellulose fibers. This formula shows that the stretched chain conformation is
due to the zigzag geometry of monomer linkages involving oxygen bridging. The chain may
be shortened or compressed to enable formation of H-bonds between adjacent resides and
thus contribute to conformational stabilization. In this type of conformation, if the number of
monomers in turn is denoted as n and the pitch (advancement) in the axial direction per
monomer unit is denoted as h, n ranges from 2 to ±4 and h equals the length of a monomer
unit. Thus, the chain given in Figure 3-2(a) has n value of -2.55 and h value of 5.13 Å.
A strongly plated ribbon-type conformation might also occur, as shown by a segment of a
pectin chain (1,4-linked α-D-galactopyranosyl-uronate units) and an alginate chain (1,4-
linked α-L-gulopyranosyluronate units), as shown in Figure 3-3.
Since alginate contains multiple oxygen atoms, it can complex with many transition
metals. As shown in Figure 3-3(b), Ca2+ stabilizes the conformation of alginate. In this case,
two alginate chains are assembled in a conformation which resembles an egg box, which is
referred as the egg box type of conformation (Figure 3-4).
This conformation is typical for 1,3-linked β-D-glucopyranose units and occurs in the
polysaccharide lichenin, for example, as shown in Figure 3-5 (a). The formula shows that the
helical conformation of the chain is imposed by a U-form geometry of the monomer linkages.
Amylose (1,4-linked α-D-glucopyranosyl residues) also has such a geometry, and hence a
helical conformation (Figure 3-5 (b)).
a b c
Figure 3-6. Stabilization of helical conformations. a, clathrate compounds; b, coiled double or triple
helices; c, nesting.
The number(n) of monomers per turn and the pitch in the axial direction per residue (h)
might differ significantly in this conformation.
The value of n varies from 2 to ±10, while h can be near its limit value of 0. The
conformation of a β(1-3)-glucan, with n value of 5.64 and h value of 3.16 Å, is shown in
Figure 3-2(b).
The helical conformation can be stabilized in various ways. When the helix diameter is
large, inclusion (clathrate) compounds can be formed (Figure 3-6(a)). More extended or
stretched chains, with smaller helix diameter, can form double or triple stranded helices
(Figure 3.6(b)), while strongly-stretched chains, in order to stabilize the conformation, have a
zigzag, plated association and not stranded (Figure 3-6(c)).
Crumpled-type conformation
Loosely-jointed conformation
This is typical for glycans with 1,6-linked β-D-glucopyranosyl units, because they exhibit
a particularly great variability in conformation. The great flexibility of this glycan-type
conformation is based on the nature of the connecting bridge between the monomers. The
bridge has three free rotational bonds and, furthermore, the sugar residues are further apart.
Carbohydrates 43
Conformations of heteroglycans
The examples considered so far have demonstrated that a prediction is possible for a
homoglycan conformation based on the geometry of the bonds of the monomer units which
maintain the oxygen bridges. It is more difficult to predict the conformation of a heteroglycan
with a periodic sequence of several monomers, which implies different types of
conformations. Such a case is shown by ι-carrageenan, in which the β-D-galactopyranosy l-4-
sulfate units have a U-form geometry, while the 3,6-anhydro-α-Dgalactopyranosyl-2-sulfate
residues have a zigzag geometry (Figure 3-7).
Calculations have shown that conformational possibilities vary from a shortened,
compressed ribbon band type to a stretched helix type. X-ray diffraction analyses have proved
that a stretched helix exists, but as a double stranded helix in order to stabilize the
conformation.
Interchain interactions
Physiochemical Properties
Solubility
Most monosaccharides, such as sugar alcohols, glycosides, and oligosaccharides, are
water soluble. At 20°C, up to 195 g of sucrose can dissolve in 100 g of water. The solubility
of sugar alcohols varies significantly with species. For example, sorbitol has a higher
solubility than sucrose and reaches up 220 g per 100g water, while that of mannitol, erythritol
and isomaltitolto is only 17, 50, and 100 g per 100g water, respectively. Sugar alcohols
absorb much more heat than sugars when dissolution and thus produce cooling sensation in
the mouth. Sugar alcohols are added to candies and chewing gums to provide the cooling
sensation.
The solubility of glycosides is closely correlated with their ligands. Generally, glycosides
are more water soluble than corresponding ligands. For example, flavonoids are usually
insoluble, but the corresponding glycosides are soluble. Flavonoids provide foods with
different colors and tastes in the soluble glucoside form.
Each sugar unit in polysaccharides contains an average of three hydroxyl groups and each
hydroxyl group can hydrogen bond with one or more water molecules. In addition, the
oxygen atoms in the sugar ring and glycosidic bond can also form hydrogen bonds with
water. Therefore, monosaccharide units in polysaccharides can be completely solvated and
most polysaccharides have strong water-holding capabilities and are highly hydrophilic.
Polysaccharides in foods affect the movement of water and significantly influence the
functional properties of foods.
The presence of polysaccharides does not increase the penetrability or significantly
reduce the freezing point of water, although polysaccharides can be solvated by water.
Therefore, polysaccharides are good frozen stabilizers. Taking starch solution as an example,
when a starch solution is frozen, a two-phase system is formed, of which, one phase is
composed of crystal water and another phase is in the glass state consisting of 70% starch and
30% unfrozen water. Due to the extremely high polysaccharide concentration in the glass-
state phase, the viscosity is high and the movement of unfrozen water in the glass-state phase
is restricted. In addition, polysaccharides are concentrated in low temperatures. In this case,
46 Dongfeng Wang, Jipeng Sun, Guoqing Huang et al.
the mobility of water is further restricted and water molecules can no longer adsorb to crystal
nucleus or the active sites for crystal growth. Both high and low molecular weight
polysaccharides can effectively protect food texture and structure from being damaged during
frozen storage.
Some polysaccharides occur in a highly ordered form. In these molecules, the chains are
tightly bound to form crystals. Because the number of exposed hydroxyl groups is
significantly reduced, these polysaccharides are insoluble in water unless the inter-chain
hydrogen bonds are broken. Taking cellulose as an example, the structural unit β-D-
glucopyranosyl residues are arranged orderly and linearly along the chain and form inter-
chain hydrogen bonds with parallel chains. The crystal regions of cellulose are not water
soluble and are very stable.
The majority of carbohydrates is not present as crystals and readily dissolves or swells in
water. Water-soluble polysaccharides and their derivates used in the food industry are often
termed gums or hydrophilic colloids. The solutions of most macromolecular polysaccharides
are viscous and the viscosity depends on the molecular size, shape, net charge and
conformation in solution. The thickening and gelling properties of polysaccharides
significantly affect the quality of foods.
Hydrolysis
Hydrolysis of Glycosides
Though glycosides occur in low contents in foods, they impart important physiological
effects and functionality to foods. For example, nature saponins are strong foaming agent and
stabilizer, flavonoids produce bitterness and color for foods. In addition to a small amount of
sweet glycosides such as stevioside and osladin, most glycosides taste bitter or astringent,
particularly when the ligand is larger than methyl. When glycosides are hydrolyzed, their
solubility is reduced and the bitterness or astringency is alleviated.
O-glycoside bonds are stable in neutral and weak alkaline solutions, but easily
hydrolyzed in acidic conditions. Most glycosides in foods (except for strong acidic foods) are
stable.
In the enzymatic hydrolysis of glycosides, the sugar component is transformed to highly
active half-chair conformation and the glycosidic bond is weakened. Then, a proton is
transferred from the enzyme to an oxygen atom in glycoside. When the oxygen atom is
separated from the carbon atom, a positively-charged carbon ion is generated. This carbon ion
then reacts with the negatively-charged -COO- group in the enzyme and is temporarily
stabilized until it is completely hydrolyzed by reacting with the -OH- group in solvent.
N-glycosidic bond is not as stable as O-glycosidic bonds and is susceptible to hydrolysis
in water. For example, glycosylamines are unstable in water and can be hydrolyzed to colored
products through a series of reactions. These reactions are the main reason of Maillard
reaction initiation (to be discussed in Section 3.2.4).
Thioglycosides, which contain S-glycosidic bonds, occur naturally in mustard and
horseradish and are very stable and water-soluble. Thioglycosides can be hydrolyzed by thio-
glucosidase to produce isothiocyanates, as shown in Figure 3-11.
Cyanogenic glycosides are another category of glycosides that significantly affect food
safety. Cyanogenic glycosides are widely present in apricot, cassava, sorghum, bamboo, and
lima beans and can yield toxic hydrocyanic acid upon hydrolysis. Amygdalin and
Carbohydrates 47
mandelonitrile are the most important cyanogenic glycosides. The complete hydrolysis of
amygdalin generates D-glucose, benzaldehyde, and hydrocyanic acid (Figure 3-12).
Table 3-3 lists the main thio-glycosides and their hydrolysates. Excessive intake of
cyanogenic glycosides leads to cyanide poisoning.
In addition to enzyme activity and environmental acidity, the hydrolysis of glycosides is
also affected by glycodic bond conformation, substitution of the sugar ring, and sugar ring
size. Generally, glycosides with β glycodic bond are hydrolyzed faster than those with α
glycodic bond. Substitution on the sugar ring reduces the hydrolysis rate and furanosides are
hydrolyzed faster than corresponding pyranosides (Table 3-4). The hydrolysis rate of
glycosides increases rapidly with elevated temperature, as shown in Table 3-4.
Similar to glycosides, oligosaccharides are hydrolyzed easily by acid and enzymes and
are stable in alkaline solutions. Sucrose can be hydrolyzed by acid to yield equamolar mixture
of glucose and fructose that is called invert sugar.
Oxidation
Carbohydrates with reducing free aldehydes or ketoses that can be converted to aldehyde
groups can be oxidized into aldonic acid in the presence of weak oxidants in alkaline
conditions. When strong oxidants are present, both the aldehyde and primary hydroxyl of
aldoses are oxidized to carboxyl and aldaric acids are produced as a result [3, 18].
Some enzymes catalyze the oxidation of aldoses. For example, dehydrogenases oxidize
the primary hydroxyl of some aldoses to produce uronic acids. D-glucuronic acid, D-
galacturonic acid, and D-manuronic acid are the components of many heteropolysaccharides.
D-glucose can be oxidized to D-gluconic acid by glucose oxidase. Figure 3-13 illustrates
the preparation of D-gluconic acid and gluconolactones. D-gluconic acid-δ-lactone can be
transformed to γ-lactone and both can be hydrolyzed into D-gluconic acid at room
Carbohydrates 49
Reduction
The carbonyl groups of monosaccharides can be reduced to the hydroxyl group.
Reduction of a ketose yields to two sugar alcohols isomers due to the formation of a new
chiral carbon atom. Figure 3-14 shows sugar alcohols produced by the reduction of glucose
and fructose.
Figure 3-15. Esterification of glucose and fructose by phosphorus acid (left: D-glucose; right: D-
fructose).
Sugars can also be etherified, but naturally occurring sugar ethers are not as diverse as
sugar esters. Etherification of polysaccharides can significantly improve their functional
properties. Carboxymethyl cellulose (CMC) is an important ester of cellulose and is soluble
in water. CMC has been widely used in the food industry as thickening agent or emulsion
stabilizer.
50 Dongfeng Wang, Jipeng Sun, Guoqing Huang et al.
Properties of Carbohydrates
Hydroscopicity
Carbohydrates contain abundant hydrophilic hydroxyls and can bind water through
hydrogen bonding. For example, when monosaccharides or oligosaccharides are placed in
environments of different relative humidity (RH), the compounds can absorb moisture from
air (Table 3-5).
Figure 3-16. Hydroscopicity and water holding capacity of tea polysaccharide in different RHs (left:
RH=81%; middle: RH=43%; right: RH=43%).
All sugar alcohols, except mannitol and isomaltulose, exhibit hygroscopicity especially in
high RH environments. The hygroscopicity of sugar alcohols varies with their purity and low-
purity compounds have relatively higher hygroscopicity. Sugar alcohols are used as
moisturizing agent in cream foods and soft pastries. Polysaccharides also absorb moisture
from air and hence have good water holding capacity (Figure 3-16).
The hydroscopicity of carbohydrates, which is often referred to as moisture retention
capacity, is the most important attribute and determines their applications in foods. For
example, to overcome the sticky problem of icing sugar powders after packaging, sugars with
low hydroscopicity, such as lactose and maltose, are preferred in such products.
Carbohydrates 51
Definition of Viscosity
Viscosity is a measure of the resistance of a fluid which is being deformed by either shear
stress or tensile stress. Viscosity can be measured with various types of viscometers and
rheometers, such as capillary viscometer, rotational viscometer, falling ball viscometer and
vibration-type viscometer.
The aqueous solutions of monosaccharides, sugar alcohols, oligosaccharides and soluble
macromolecular polysaccharides are viscous. Many factors affect the viscosity of
carbohydrates. Internal factors include the average molecular weight size and shape of
molecular chains and external factors are carbohydrates concentration, environmental
temperature, etc.
Figure 3-18. Effective volume of straight-chain and branched-chain polysaccharides with equal
molecular weights in solution.
Branched polysaccharides (amylopectin, glycogen) are more soluble in water than their
perfectly linear counterparts since the chain–chain interaction is less pronounced and there is
a greater extent of solvation of the molecules. This is especially the case for highly branched
polysaccharides, because they have much less effective volumes than their linear
counterparts, as shown in Figure 3-18.
In addition to the DP, unfolding degree, and rigidity, the viscosity of polysaccharides is
also affected by the shape and flexibility of polysaccharides after solvaiton.
The charge carried by solvated polysaccharides significantly influences the viscosity of
the solution. For example, straight-chain polysaccharides containing carboxyl, sulfate hemi-
ester or phosphate groups are often negatively charged. The electrostatic repulsion between
the molecules unfolds the molecules and increases their effective volume, leading to
increased viscosity. Hence, pH has significant impact on the viscosity of polysaccharide
solutions, since it is closely related to the charge statues of the molecules.
The viscosity of polysaccharide solutions decreases with the increase of temperature,
except xanthan solution, whose viscosity remains nearly unchanged in the temperature range
0~100°C. Besides, the viscosity of xanthan gum solutions decreases with shear rate increase.
Hence, xanthan gum solutions are pseudoplastic. A practical use would be in salad dressing:
xanthan gum makes it thick enough at rest in the bottle to keep the mixture fairly
homogeneous, but the shear forces generated by shaking and pouring thins it, so it can be
easily poured. When it exits the bottle, the shear forces are removed and it thickens back and
clings to the salad.
Gelation
Gelation is another important property of polysaccharides. In food processing,
polysaccharides or proteins and other macromolecules can form a sponge-like three-
dimensional network gel structure through hydrogen bonding, hydrophobic interaction, Van
der Waals attraction, ionic cross bridges, entanglement or covalent bonding (Figure 3-19).
Liquids containing small-sized solutes and polymers fill the holes of the gel network.
Carbohydrates 53
Gels possess the properties of both solids and liquids. They are not as flowable as
continuous liquids or rigid as orderly organized solids. Instead, gels are viscoelastic semi-
solids and can retain their shape even in the presence of external stresses. Polysaccharide gels
generally contain only about 1% polymer—that is, they may contain as much as 99% water.
Examples of polysaccharide gels are dessert gels, aspics, structured fruit pieces, structured
onion rings, meat-analog pet foods, and icings.
The firmness of a gel depends on the extent of junction zone formation. If the conjunction
zone area is not long enough, polysaccharide chains cannot bind tightly. In this case, the
chains can be separated by pressure or high temperature due to increased mobility of the
chains. Such gels are easily damaged and are heat-labile. If the conjunction area contains long
chain segments, the interaction between chains is strong enough to withstand applied pressure
or thermal stimulation. Gels of this type are hard and stable. Therefore, gels of different
hardness and strength are available by controlling the length of the conjunction zone.
Branched-chain polysaccharides or heteropolysaccharides cannot bind to each other well
as linear molecules and large enough conjunction areas cannot be formed between these
molecules. Hence, gels cannot be formed by branched-chain or hetero- polysaccharides. This
is also the case for charged molecules, such as those containing carboxyl groups, because the
Coulomb repulsion between chains hinders the formation of conjunction zone.
Figure 3-19. A diagrammatic representation of the type of three-dimensional network structure found in
gels.
Flavor Retention
Aroma release from food matrix and the subsequent delivery of flavor to the olfactory
and gustatory receptors is greatly dependent on the type of food ingredients and on the
physicochemical properties of the aroma compound. It has been shown that macromolecules,
such as polysaccharides, are involved in the retention of volatile compounds. Polysaccharides
influence the volatility of aroma compounds and their partitioning between different phases
[1].
54 Dongfeng Wang, Jipeng Sun, Guoqing Huang et al.
The use of carbohydrates may induce a significant decrease in flavor perception and/or
release. Some factors affecting the retention and release of volatile flavor compounds by
carbohydrates are depending on physicochemical properties of flavor compounds, type of
carbohydrates and their concentrations. Firstly, high molecular weight flavor compounds tend
to retain in carbohydrate than low molecular weight flavor compounds. Additionally, long
linear chain length molecules will be retained in polysaccharide matrix higher than short
chain molecules or aromatic one. Among the volatile flavor compounds such as alcohol,
aldehyde, ester and ketone, alcohol are usually the best retained in carbohydrates. The
retention of polar (hydrophilic) volatiles flavor compounds is expected to be very low in
carbohydrates complex. The second factor is depending on type of carbohydrates. Each type
of carbohydrate resents different structure that influence on the interaction between flavor
compounds and its structure and also the retention and release. Thirdly, the concentration of
carbohydrates generally shows that an increase in the concentration of sugar is proportional of
the release of flavor compounds due to the salting out effect. On the other hand, an increase in
polysaccharide concentration leads to a decrease the release of flavor compounds due to
complexation and viscosity effect of that polysaccharide themselves. This knowledge can be
used to optimize product quality in term of flavour retention during preparation or processing
and its release during eating [2].
Table 3-6. Relative sweetness of sugars and sugar alcohols to sucrose in 10% aqueous
solution
Galactitol 41 D-Mannose 59
D-Fructose 114 Raffinose 22
D-Galactose 63 D-Rhamnose 33
D-Glucose 69 D-Sorbitol 51
Invert sugar 95 Xylitol 102
Lactose 39 D-Xylose 67
Maltose 46
Carbohydrates 55
Sweetness
Sweetness is a value relative to that of sucrose under the same conditions, which is often
referred to as 100. All sugars, sugar alcohols and oligosaccharides are sweet (Table 3-6) with
varying intensity of sweetness and some glycosides and polysaccharide complexes are
excellent sweeteners. For example, the sweetness of honey and most fruits is contributed by
sucrose, D-fructose or D-glucose. The sweetness perceived by consumers varies with the
composition, conformation, and physical aspects of sugars.
The intensities of sweetness of sugar alcohols differ markedly from those of
corresponding sugars. For example, sorbitol is sweeter than glucose and that of xylitol is
greater than xylose. Generally, all sugar alcohols, except xylitol, are less sweet than sucrose.
Sugar alcohols are usually incompletely absorbed into the blood stream from the small
intestines which generally results in a smaller change in blood glucose than sucrose. This
property makes them popular sweeteners among diabetics and people on low-carbohydrate
diets. As an exception, erythritol is actually absorbed in the small intestine and excreted
unchanged through urine, so it has no side effects at typical levels of consumption.
Amadori products are degraded via various pathways in the intermediate stage, leading to
the formation of furfurals, reductones and fragmentation products (carbonyl and
hydroxycarbonyl compounds). Furfural or hydromethylfurfural (HMF) formation (Figure 3-
22) is favored under acidic conditions, while alkaline media favor the production of
reductones (Figure 3-23).
The products of 1-amino-1-deoxy-2-ketose fragmentation in alkaline media, such acetol,
diacetyl, pyruvaldehyde, etc, are able to react with amino acids via the Strecker degradation
(named after the German chemist Adolph Strecker, Figure 3-24) to give Strecker aldehydes of
the amino acids and aminoketones; the latter subsequently condense to form pyrazines.
Strecker aldehydes and pyrazines contribute to aroma formation in heated foods.
Carbohydrates 57
The majority of the compounds displaying color are formed in the final stage of the
Maillard reaction. Furfurals, reductones, aldehydes either undergo aldol condensation without
the intervention of amino compounds or react with amino compounds as other intermediates,
leading to the ultimate reaction products known as melanoidins. Hodge defined melanoidins
as ‗brown, nitrogenous polymers and copolymers‘. The structures of melanoidins remain
unknown till now. The pigment generated in the Maillard reaction is soluble in the early stage
of polymerization and exhibits no characteristic absorption pick in the visible range. Infrared
spectrum and chemical composition analysis indicate that melanoidins contain unsaturated
bonds, heterocycles, and complete amino acid residues.
The reaction mechanism of the Maillard reaction proposed by John Hodge is largely
unchanged after 60 years and is still widely cited. However, the hypothesis has some flaws.
Firstly, the mechanism presents only the general process of the Maillard reaction and the
details on the reaction are not described. Secondly, some new reactions have been identified
by other researchers. For example, the work of Japanese scientists Namiki and co-workers
found that the carbonyl fission products can also be formed directly from N-substituted
glycosylamine through a free radical-mediated pathway, which is known as the Namiki
pathway [4].
Mechanism of Caramelization
Heating of carbohydrates without the presence of nitrogen-containing compounds causes
a complex group of reactions termed caramelization. Unlike the Maillard reaction,
caramelization of carbohydrates is thermolysis as compared to the reaction with amino acids.
Mild heating or thermolysis in the early stage leads to anomeric shifts, ring size change,
glycosidic bond breakdown, and new glycosidic bond formation. Mostly, thermolysis causes
dehydration of the sugar molecule with introduction of double bonds or formation of anhydro
rings. Caramelization yields hundreds of flavor compounds and these compounds impart
foods with pleasant color and flavor. The caramels derived from different sugars have similar
compositions. Generally, the products of caramelization include caramel, which is the
polymerization product of sugar dehydration, and aldehydes, ketones, phenols, etc.
The caramelization process is divided into two stages.
Caramel formation
Figure 3-26 illustrates the formation of caramel by taking sucrose as the example. It can
be seen that caramelization is the removal of water from a sugar, proceeding to isomerization
and polymerization of the sugars into various high-molecular weight compounds.
Carbohydrates 59
The aqueous solutions of caramels are colloidal and the isoelectric points range from
3.0~9.0, with some exceptions with pI lower than 3. The presence of acids or certain salts
facilitates the reaction. The caramel prepared by heating sucrose solution in the presence of
acid or acidic ammonium salts has been widely used in food coloration.
The caramelization of sucrose consists of three steps:
Step 1: Caramelization of sucrose starts with the melting of the sugar at high
temperatures followed by foaming (boiling). At this stage sucrose decomposes into glucose
and fructose. This is followed by a condensation step, in which the individual sugars lose
water and react with each other to form the isosaccharosan (Figure 3-27). Isosaccharosan
loses the sweetness of sugar and tastes bitter instead.
Step 2: This step involves further dehydration reactions. Isosaccharosan dehydrates and
condensates to caramelan. Caramelan is one of the three main products of sucrose
caramelization. Caramelan are lightly brown and tastes bitter with formula of C24H36O18.
Caramelan melts at 138°C and is soluble in water and ethanol.
Step 3: This step includes both fragmentation reactions (flavor production) and
polymerization reactions (color production). With respect to color production, caramelan is
further dehydrated to form caramelen. If the mixture is further heated, polymerization
reaction occurs and the insoluble caramelin is generated. The caramelan melts at 154°C,
tastes bitter, and is soluble in water with formula of C36H50O25. Caramelin appears dark
brown and are not soluble in water with formula of C125H188O80.
60 Dongfeng Wang, Jipeng Sun, Guoqing Huang et al.
The presence of iron enhances the color of caramels. Phosphates, inorganic salts,
alkalines, citric acid, ammonia, and ammonium sulfate catalyze sugar caramelization.
Ammonia and ammonium sulfate increase the yield of caramel. However, the addition of
ammonia and ammonium sulfate cause the generation of 4-methylimidazole at high
temperatures, which is an anticonvulsants and can cause nervous system damage after long-
term consumption. Ammonia and ammonium sulfate have been prohibited in the production
of caramels.
Figure 3-28. Formation of aldehydes from sugars in acid media and thermal condition.
Carbohydrates 61
Structure of catechin
Catechin possesses two benzene rings (called the A- and B-rings) and a dihydropyran
heterocycle (the C-ring) with a hydroxyl group on carbon 3, as shown below:
Catechin contains multiple phenolic hydroxyl groups and is very susceptible to oxidation,
polymerization, and condensation. Catechin is white crystal and is oxidized to yellowish-
brown compounds in the air. Catechin is soluble in water, ethanol, methanol, acetone, and
acetic anhydride, partially soluble in ethyl acetate and acetic acid, and insoluble in chloroform
and anhydrous ether.
Carbohydrates 63
Mechanism of oxidation
The hydroxyl groups in catechin have different activities with respect to auto-oxidation.
Hydroxyl groups in adjacent and vicinal positions are oxidized easily, while the –OH in
carbon 3 on ring C cannot be oxidized.
The mechanism of the nonenzymatic auto-oxidation of catechin is very complex and not
well understood to the present. It is generally accepted that the process involves two
reactions. The first is the formation of quinine. Quinine is unstable and rapidly undergoes
condensation. The condensation product in the early stage is soluble, light yellow and tastes
bitter. As the reaction proceeds, the intermediates are further condensed to brown nitrogenous
polymer in the presence of amino compounds. The general process is illustrated in Figure 3-
31.
Effects on Color
The composition of nonenzymatic browning reaction products is very complex. Many
components affect the color of foods and their molecular weights range from several
hundreds to up to more than 100000 Dolton. Several coloring compounds have been isolated
from different model systems.
64 Dongfeng Wang, Jipeng Sun, Guoqing Huang et al.
A yellow compound is isolated from the Maillard reaction product of the xylose – Lys
model system and MS and NMR reveals that its possible structure is one of the following two
[5]:
(1)
Two red products are isolated and identified from the Maillard reaction product and their
structures are shown below [6]:
(2)
(3)
(4)
(5)
(6)
Figure 3-32. Part of possible melanoidin structure formed from 3-deoxyhexosulose involving amino
compounds [7].
Figure 3-34. pH changes of various sugar-amino acids solutions heated at 100°C. From up to down:
glucose, lactose, lactose + alanine, glucose +alanine, lactose + glycine, glucose + glycine, glucose +
lysine, lactose+ lysine.
Antioxidation
The antioxidant activity of Maillard reaction products (MRPs) was firstly reported by
Franzke and Iwainsky in 1954. The two researchers found that the thermal reaction product of
glycine and glucose improved the stability of margarine against oxidation [8]. However, this
research did not attract much attention until 1980s. The antioxidant components in various
MRPs are not identified yet and the antioxidant activity of MRPs is studied mainly by using
various model systems.
Carbohydrates 67
Elizalde et al. found that the volatile compounds of the MRP of the glucose-glycine
system showed a significant antioxidant activity and prolonged the induction period of
soybean oil thermoxidation by up to 3 times in relation to the control [9]. Bedinghaus and
Ockerman compared the lipid oxidation inhibitor activities of fifteen MRPs prepared by
heating one of three sugars (glucose, xylose, and dihydroxyacetone) with one of five amino
acids (arginine, histidine, leucine, lysine, and tryptophan) by using cooked ground pork
patties as the model food. It was found that the most effective MRPs were xylose-lysine,
xylose-tryptophan, dihydroxyacetone-histidine, and dihydroxy-acetone-tryptophan when
compared to controls [10]. Yamaguchi et al. obtained a fraction from the MRP of the xylose –
glycine system through multiple chromatographic steps and found that it is more effective in
preventing linoleic acid oxidation than BHA and propyl gallate [11]. Yoshimura et al.
investigated the MRP of the glucose-glycine system on the inhibition toward active oxygen
and fount that it inhibited more than ca. 90% of active oxygen species existing in the form of
hydroxyl radicals (•OH) [12].
Morales and Jiménez-Pérez investigated the DPPH· scavenging activities of MRPs
produced by heating glucose or lactose with lysine, alanine or glycine. It was found that all
the MRPs were effective DPPH· scavenging agents. Browning was not directly related to the
free radical scavenging properties of MRPs formed at prolonged heating conditions and
fluorescence measurement is more effective than browning to follow the formation of MRPs
with free radical scavenging activities, as shown in Figure 3-35.
Although the antioxidant effects of MRPs have been well recognized, their application as
effective antioxidants in foods is still limited due to insufficient knowledge on the structure
and antioxidant mechanism of MRPs. Early researches indicated that antioxidant capability of
MRPs is contributed by the intermediate reductones of the Maillard reaction and the metal
chelating ability of MRPs. Latest researches indicate that MRPs also have strong active
oxygen scavenging capabilities and can reduce peroxides.
Figure 3-35. Free radical scavenging activity in sugar/amino acid mixtures heated at 100°C up to 24 h
[13].
68 Dongfeng Wang, Jipeng Sun, Guoqing Huang et al.
Effects on Nutrition
One of the most obvious negative consequences of the Maillard reaction in food is the
loss of nutritive value of proteins due to decreased digestibility, destruction and/or biological
inactivation of amino acids, including essential amino acids like lysine and tryptophan,
inhibition of proteolytic and glycolitic enzymes, and interaction with metal ions.
Lysine is the most liable to loss in non-enzymatic browning, followed by alkaline amino
acids, including L-Arg and L-His. In addition to sugar-amino acid reactions, Strecker
degradation is also involved in amino acid loss. The formation of complex macromolecules
reduces the solubility of proteins and reduces their nutritional value. The effect of the
Maillard reaction on amino acid availability has been investigated by using rainbow trout
(Salmo gairdneri) as the model. It was found that arginine and lysine exhibited the greatest
losses in the mixture of fish protein isolate and glucose stored for 40 d at 37°C and the
apparent digestibility and absorption of individual amino acids, particularly lysine, was lower
in trout fed browned protein than in those fed the control protein [14].
Vitamin C is also involved in browning and therefore suffers loss during the process.
The products of non-enzymatic browning reduce the bioavailability of minerals.
Whitelaw et al. employed the dialysis procedure to determine the effect of the Maillard
reaction on apparent 65Zn availability. In the presence of 65ZnCl2, the amino acids glycine, D-
leucine, L-proline, L-lysine and L-glutamic acid were combined with D-glucose and
autoclaved (110°-120°C, 15 atm, 10 min) to produce high molecular weight 65Zn binding
compounds that were not dialyzable (6-8KD). Experiments in stimulated gastrointestinal
digestive conditions revealed that the Maillard reactions significantly reduced the
bioavailability of Zn [15].
Harmful Compounds
The safety of MRPs has attracted wide attentions in recent years. With the development
of new instrumental analysis measures, more and more harmful compounds have been
isolated and identified. For example, mutagenic compounds have been found in instant and
caffeine-free coffee and the compounds consist of dicarbonyl compounds, methylglyoxal,
diacetyl and glyoxal, among which the methylglyoxal presented highest mutagenic activity
[16]. Also in both fried and grilled meat and fish, mutagenic compounds were identified,
mainly stemming from heterocyclic amines [17]. The reaction mechanism seems to have a
major influence on the mutagenicity of the reaction products. For instance, ketose sugars
showed a higher mutagenic activity than the corresponding aldose sugars [18]. However, due
to the complexity of non-enzymatic browning reactions and the poor stability of
intermediates, only very few harmful compounds have been well elucidated, of which,
acrylamide is the most intensively studied.
Acrylamide is a well-known cancerogen and can cause neurologic damage. Acrylamide
has been detected in nearly all the foods, but fried and roasted foods that are processed at high
temperatures have much higher acrylamide contents, as presented in Table 3-7.
Carbohydrates 69
acrylamide formation is detected within 10 min and the content remains unchanged thereafter.
While in the glucose/methionine system, the formation of acrylamide keeps increasing in the
first 30 min and then remains unchanged in remaining time.
pH
Medium pH affects multiple reactions of non-enzymatic browning. Aqueous solutions of
sugar (xylose or glucose) and amino acid (glycine or lysine monohydrochloride), are heated
without pH control for up to 120 min and the total reaction products are analyzed by HPLC
and compared with those of the corresponding model systems maintained at pH 5 throughout
heating.
For xylose-lysine, seven of these peaks are common to the systems heated both with and
without pH control for 15 min, while no peak is common to both glucose-lysine systems
heated for 120min, indicating different products are formed under the conditions [19].
Generally, the browning rate between sugars and amino acids increases with pH when the
medium pH is greater than 3.5 and is reversely proportional to pH values in the range 2.0~3.5.
Hence, browning can be suppressed by reducing pH. This is why browning does not occur
readily in acidic foods such as pickled vegetables. Sulfites inhibit nonenzymatic browning by
reacting with carbonyl intermediates, thereby preventing their further reaction to form brown
pigments [20].
Figure 3-36. The time course of the browning develop in heated sugars -amines solutions at 100°CUp
to down: glucose+lysine, lactose +lysine, glucose+glycine, lactose+ glycine, glucose+alanine, lactose
+alanine, lactose, and glucose.
Carbohydrates 71
High Pressure
High pressure (100-1000 MPa), which is gaining increasing importance as a food-
processing technology particularly in combination with moderate temperatures (30-60 °C),
may influence the Maillard reaction and thereby affects the flavor, color, and nutritional value
of foods. It has been proposed that high pressure exerts its influence on non-enzymatic
browning by changing the medium pH. The effect of high pressure on Maillard reaction has
been investigated by using the glucose-lysine model system over a range of pH values (5-10)
at 60 °C either under atmospheric pressure or at 400 MPa. The results obtained showed that
high pressure affected in different ways the different stages of the Maillard reaction and that
such effects were strongly influenced by pressure-induced changes in the pH of the systems.
In unbuffered media, at an initial pH 8.0, the formation of Amadori rearrangement products
(ARP) was not considerably affected by pressure, whereas the intermediate and advanced
stages of the Maillard reaction were suppressed, suggesting a retardation of the degradation of
the ARP. In buffered media, at pH values 8.0, pressure slowed the Maillard reaction from the
initial stages. These effects are attributed to the pH drop caused by the pressure-induced
dissociation of the acid groups [22].
Sulfhydryl compounds
Antioxidants
prevent the formation of intermediates in the Maillard and related reactions, thus prevent the
formation of undesirable compounds during food processing.
Deglycation
Low temperature
Sulfurous acid
The condensation product of carbonyl group and sulfurous acid can react with R-NH2
and the resultant product cannot be transformed to Schiff‘s base. Hence, SO2 and sulfites
suppress non-enzymatic browning.
pH
Product concentration
Products with lower concentrations suffer lighter browning. For example, because lemon
juice is more susceptible to browning than orange juice, the concentration factor of lemon
juice is 4:1, which is lower than 6:1 of orange juice.
Insensitive sugar
Removal of sugar
Some foods contain only trace amount of sugars and these sugars can be removed to
prevent non-enzymatic browning. For example, glucose oxidase and catalase have been used
to remove the trace glucose in dried egg yolk and dehydrated meat.
Calcium salts
Calcium can complex with amino acids to form precipitates.
Carbohydrates 73
Oligosaccharides
Soybean oligosaccharide
Soybean oligosaccharide has once been regarded as an antinutritional factor and has been
reported to increase the incidence of diarrhea in rats. However, recent researches reveal that
soybean oligosaccharide has the potential as new functional ingredients in functional foods.
Soybean oligosaccharide has recently been found to be ―probiotic material‖ and have been
approved by the Food and Drug Administration as generally recognized as safe material in the
USA. Composition analysis indicates that soybean oligosaccharide was composed of
74 Dongfeng Wang, Jipeng Sun, Guoqing Huang et al.
galactose (65.3%), mannose (15.6%), fructose (7.8%) and glucose (8.7%) [24]. Intake of 3~5
g soybean oligosaccharide per day is sufficient to enhance the proliferation of bifidobacteria.
Fructo-oligosaccharide
Xylo-oligosaccharide
Chito-oligosaccharides
Other oligosaccharides
Starch
Starch is the major constituent of many foods and is the most important carbohydrate
source for human nutrition. Corn, wheat, potato, sweet potato, and rice are the most important
materials for starch production. Table 3-8 lists the contents of starch in some crops.
Starch can be divided into two fractions: amylose and amylopectin. Natural starches are
the mixture of amylose (10~20%) and amylopectin (80~90%). The percentages of amylose
and amylopectin in starches derived from different sources are shown in Table 3-9.
Gelatinization does not occur easily in starches with high amylose contents and the
gelatinization temperature can reach up to 100 °C. However, gelatinized amylose is unstable
and is prone to aging in contrast to the high stability of gelatinized amylopectin.
Due to the unique physicochemical properties and nutritional functions, starches are of
incomparable importance to human beings. Starch and its derivatives have been widely used
as thickening agent, bonding agent and stabilizing agent and as the materials of pudding,
soup, sauce, vermicelli, infant foods, pie, and mayonnaise.
Chemistry structure
Type B amylose shows the left-hand double helices structure, which are packed in a
parallel arrangement. Hydroxyl groups are located outside of the chains and the double helix
is stabilized by the hydrogen bridges between amylose molecules. The internal channel of the
helix is hydrophobic and hence can enclose only hydrophobic compounds, such as lipids. The
A-type is very similar to the B-type, except that the central channel is occupied by another
double helix, as shown in Figure 3-38.
Amylopectin is the highly branched polymer of glucose. The backbone chain is
composed of glucose units linked in a linear way with α(1→4) glycosidic bonds and
branching takes place through α(1→6) bonds. In amylopectin, α(1→6) bonds account for
4%~5% of total glycosidic bonds.
Figure 3-38. Unit cells and arrangement of double helices (cross section) in type-A amylose (left) and
type-B amylose (right) [29].
Due to the presence of multiple linear branches, amylopectin has multiple reducing ends
and are hydrolyzed by enzymes faster than amylose. The branches of amylopectin are
arranged in parallel or double helix, as shown in Figure 3-39.
Amylopectin contributes to the crystalline structure of starch granules. The molecular
weight of amylopectin ranges from 5×107~5×108. The ratio of amylopectin in starches
generally exceeds 75% and the value can reach up to 99% in some species, such as waxy corn
starch, as shown in Table 3-9. Starches derived from potato also contains a high phosphorus
content (0.06~0.1%). Hence, potato starches are slightly negatively charged and swell more
rapidly in warm water due to coulombic repulsion.
Gelatinization
Starch granule: Starches are present as granules in plant cells. Starch granules can be
round, oval, and polygonal and their sizes range from 0.001~0.15 mm, depending on the plant
78 Dongfeng Wang, Jipeng Sun, Guoqing Huang et al.
species, of which, potato starch granules have the largest size and cereal starch granules have
the smallest size, as shown in Figure 3-40. Polarization microscopy observation and X-ray
diffraction find double refraction and X-ray diffraction in starch granules, indicating the
presence of crystalline structure alternate layers of crystal region and amorphous region
(Figure 3-41 I). About 70% of the mass of a starch granule is regarded as amorphous and
about 30% as crystalline.
The amorphous regions contain mainly amylose and the crystalline regions consist
primarily of amylopectin. Amylose can enclose fatty acids and hydrocarbons due to the
presence of the hydrophobic internal channel and the complexes are termed inclusion
complexes. Amylose occur as double helices as in starch granules. Amylose and amylopectin
are arranged radially in starch granules, as shown in Figure 3-41 II.
Figure 3-39. Structural models (I, II) for amylopectin with parallel double helices. III is an enlarged
segment of I or II.
Carbohydrates 79
Figure 3-40. Shapes of starch grains in electron microscope (×1200).A, Green bean starch (mean grain
size: 0.016nm); B, Potato starch (mean grain size: 0.049nm; C, Common corn starch (mean grain size:
0.013nm); D, Sweet potato starch (mean grain size: 0.017nm).
Figure 3-41. Sketch of crystallization section and amorphous section of starches (I), and radial shape of
amylose and amylopectin in starches (I, II).
Gelatinization: Due to the inter-molecular hydrogen bonding, starch is not soluble in cold
water in spite of the abundance of hydroxyl groups. When the suspension is heated, the
vibration of starch molecules increases and the hydrogen bonding between molecules is
disrupted. As a result, more hydroxyl groups are exposed and starch-water hydrogen bonding
is formed instead. With the diffusion of water into starch granules, many long chains are
separated and the confusion degree increases markedly. Meanwhile, the number and size of
80 Dongfeng Wang, Jipeng Sun, Guoqing Huang et al.
crystal regions reduce significantly. When the suspension is further heated, the swelling
becomes reversible. In this case, random coils are observed in amylopectin due to hydration
and the ordered structure of starch is destroyed. This process is termed gelatinization and the
temperature at which irreversible changes occur is called the gelatinization temperature.
Starch gelatinization can be divided into three phases. In phase I, water diffuses into
granules and absorbs to the polar groups in amorphous regions below the gelatinization
temperature. The starch can restore to their original form if dehydrated. In phase II, when the
gelatinization temperature is reached, bulk water enters starch granules and the granules swell
significantly. Due to the increase of volume, the fraction between swollen starch increases
and the suspension becomes viscous, which can be followed by Brabender amylograph. In
this phase, water molecules enter the microcrystalline areas and the original arrangement is
disrupted. When the temperature further increases, the viscosity of the suspension increases
accordingly. In phase III, the swollen starch granules are disintegrated and the suspension
viscosity drops sharply, as shown in Figure 3-42. It could be seen that the shape of the curve
varies greatly for different starches.
The gelatinization of starch is affected by the following factors:
Water activity: Gelatinization occurs readily in medium with high water activity. The
presence of high concentration of sugars significantly suppresses gelatinization, because the
molecules can compete for water with starch.
6ISCOSITY "RABENDER UNITS X
4IME MIN
Helix amylose
Fatty acid
Retrogradation
When a hot starch paste is cooled down, the suspension generally transforms to a
viscoelastic gel and starch becomes insoluble. The process of soluble starch becoming
insoluble is called retrogradation. The presence of conjunction zones in the gel indicates that
retrogradation is actually the recrystallization of starch molecules. The qualities of many
foods are deteriorated during retrogradation. For example, the staling of breads and the loss of
viscosity of soups and sauces are partially caused by starch retrogradation.
The retrogradation of starch is influenced by the following factors:
Amylose to amylopectin ratio: Amylose is more susceptible to retrogradation due to its
linear structure, of which, amylose with DP of 100~200 is the most resistant to retrogradation.
Starch concentration: Retrogradation occurs readily in high starch concentrations due to
frequent molecular collision, but water content of less than 10% hinders the process. The
highest retrogradation rate is generally found in the water content of 30~60%.
Presence of inorganic salts: Inorganic salts hinder the repositioning of starch molecules.
The hindering effects of some common ions are SCN-, PO43-, CO3-, I-, NO1-, Br-, CI-, Ba2+,
Ca2+, K+, and Na+ in the decreasing order.
82 Dongfeng Wang, Jipeng Sun, Guoqing Huang et al.
Medium pH: Starch undergoes retrogradation readily in the pH range 5~7 and the process
is inhibited in alkaline or acidic solutions due to charge repulsion.
Temperature: The optimum temperature for starch retrogradation is 2°C~4°C and
retrogradation does not occur in temperatures above 60°C or below -20°C.
Cooling speed: When starch paste is cooled slowly, starch molecules have sufficient time
to align and retrogradation occurs readily. If the paste is cooled rapidly, the water in the paste
crystallizes quickly, which prevents the approaching of starch molecules. Hence,
retrogradation occurs slowly in rapid cooling.
Presence of other ingredients: Lipids and emulsifying agents prevent retrogradation.
Compounds such as glyceryl monopalmitate (GMP), other monoglycerides and their
derivatives, and sodium stearoyl 2-lactylate (SSL) are often added into doughs of bread and
other baked goods to prevent starch retrogradation and increase shelf life.
Hydrolysis of starch
Starches can be randomly hydrolyzed by acids and enzymes. Under mild conditions,
starch is only partially hydrolyzed by acids. This process is called thinning and the products
are termed acid-modified or thin-boiling starch. Acid-modified starch has increased gel
transparency and strength and is less susceptible to retrogradation. Acid-modified starch has
wide applications and can be used as film forming agent and adhesive agent in products such
as pan-coated roasted nuts and candy. Besides, they are also used as encapsulating agents and
flavor carriers.
Enzymatic hydrolysis has been used in the production of commercially important syrups.
In the production of high-fructose corn syrup, corn is firstly hydrolyzed by α-amylase and
glucoamylase to obtain high purity D-glucose. D-glucose isomerase is then added and D-
glucose is converted to D-fructose. The final product is the mixture of 58% D-glucose and
42% D-fructose. High-fructose corn syrup is commonly used as sweetener in soft drinks.
The degree of hydrolysis of starch is measured by dextrose equivalency (DE), which is
defined as the percentage of reducing sugar in the syrup. DE is related to the degree of
polymerization and is calculated in the following equation:
(1)
Glucose polymers with DE less than 20 are defined as maltodextrins and those with DE
in the range 20~60 are termed corn syrup. Table 3-14 lists the functional properties of some
hydrolysis products of starch.
Modified starch
Physical, chemical and biochemical modifications have been implemented to enhance the
functional properties of starches and modified starches have gained wide applications in the
food, pharmaceuticals, and chemical industry. Important modified starches that are widely
used in the food industry are described below.
Low viscosity starch: Starch of this type is also termed acid-modified starch. When starch
is exposed to acid below the gelatinization temperature, hydrolysis occurs only in the
Carbohydrates 83
amorphous region and the crystal region nearly remains intact. The modified starch produced
under such conditions is not soluble in cold water but is readily soluble in boiling water.
Compared with native starch, low viscosity starch has decreased viscosity and gel strength of
hot paste and elevated gelatinization temperature. Low viscosity starch can be used as
thickening and film forming agents.
Pre-gelatinized starch: This product is obtained by heating starch suspension above the
gelatinization temperature and then dried with drum drying, spray drying or extrusion. Pre-
gelatinized starch can dissolve and form gel in cold water. Pre-gelatinized starch can be used
in elder and infant foods, surimi products, ham, sausage, and bakery foods. Besides, pre-
gelatinized starch has gained applications in cooking-free instant foods due to its solubility in
cold water.
Etherified starch: All the three free hydroxyl groups in each D-glucopyranose unit can be
etherified. Hydroxyethyl starches of low degree of substitution (DS) have reduced
gelatinization temperature, increased swelling rate, and lowered tendency of pastes and gels
to retrogradation. Hydroxyalkyl starches, such as hydroxypropyl starch, can be used in salad
dressings, pie fillings, and other foods as thickening agent.
Esterified Starch: Starch can be esterified by acidic orthophosphates, acid
pyrophosphates, and tripolyphosphates to produce various starch esters. Compared with
native starch, monostarch phosphates gelatinize in lower temperatures and those with DS
greater than 0.07 can swell in cold water and have increased paste viscosity and transparency,
and decreased retrogradation. These properties are quite similar to those of potato starch,
which has high phosphorus content.
Because monostarch phosphates have good freezing-thawing stability, they are preferred
in frozen foods, such as frozen broth and frozen cream pie, as thickening agent to unmodified
starch.
Starch can also be esterified by various organic acids, such as acetic acid, long-chain fatty
acids (C6~C26), succinic acid, adipic acid, and citric acid. These esters are superior in
thickening and paste transparency and stability to native starch and can be used in bakery
products, soup powder, sauce, pudding and frozen foods as thickening agent and stabilizer, as
well as in dehydrated fruit as protective agent and in flavor processing as encapsulating
material.
Crosslinked starch: Starch can react with sodium trimetaphosphate, phosphorus
oxychloride, epichlorohydrin, and acid anhydride to yield crosslinked derivates. Crosslinking
84 Dongfeng Wang, Jipeng Sun, Guoqing Huang et al.
prevents starch granule swelling and increases the stability against heating. Crosslinking by
phosphorus increases the stability of swollen starch granules, but the paste of distarch
phosphates is opaque in contrast to that of monostarch phosphate.
Starches with high degree of crosslinking are very stable against high temperature, low
pH and mechanical vibration and their gelatinization temperature is proportional to the degree
of crosslinking. Some starches with high degree of crosslinking do not swell even in boiling
water.
Crosslinked starches are mainly used in infant foods, salad dressing, fruit pie filling and
cream-style corn as thickeners and stabilizers. They also provide resistance to gelling and
retrogradation, show good freeze-thaw stability, and do not undergo syneresis or weep on
standing.
Oxidized starch: Starch is hydrolyzed and oxidized when its aqueous suspension is
incubated with sodium hypochlorite below the gelatinization temperature and the carboxyl
group occurs once every 25 to 50 glucose residues in the resulting oxidation products.
Oxidized starch has relative low viscosity even in high concentrations and is used as
thickening agent in salad dressing and mayonnaise. Compared with low viscosity starch,
oxidized starch is less susceptible to retrogradation or forming opaque gel.
Table 3-15 lists the nature of a variety of starch before and after modification.
Glycogen
Glycogen is also called animal starch and is the major storage carbohydrate in muscle and
liver tissue of animals. Because glycogen accounts for only 0.02%~0.1% of fresh animal
Carbohydrates 85
tissues, it is less important for the food industry than starch. Glycogen is much branched than
starch and is similar to amylopectin in structure.
Cellulose
Cellulose is the major component of plant cell walls and often associates with
hemicellulose, pectin, and lignin. The mode and degree of their association significantly
affect the texture of plant-derived foods. Cellulose cannot be digested by the enzymes in
human digestive tract and hence is a good source of dietary fiber.
Cellulose is a linear homopolysaccharde consisting of D-glucopyranose units that are
connected through β-D-1,4-glycodic bonds. Native cellulose contains both crystal and
amorphous zones, of which, amorphous zone is more susceptible to solvent and chemical
reagent action. This difference has been used in the preparation of microcrystalline cellulose,
in which the amorphous zone is hydrolyzed by acids and the acid-resistance crystal zone is
remained. The molecular weight of microcrystalline cellulose ranges from 30~50kDal and its
tradename is avieol. Microcrystalline cellulose is insoluble in water and is often added to low-
calorie foods as fillings and rheology control agents.
The degree of polymerization (DP) of cellulose varies with the plant origin and ranges
from 1000~14000. Due to the large molecular weight and the presence of crystal structures,
cellulose is insoluble in water and its swelling power or the ability of absorb water is poor or
negligible.
CMC is the most widely used derivative of cellulose. It is obtained by treating alkaline
cellulose with chloroacetic acid. The DS of commercially important CMC ranges from
0.3~0.9 and DP from 500 to 2000.
CMC has long and rigid chains and carries positive charge. CMC solution is viscous and
stable due to the electrostatic impulsion. However, these properties depend on the DS and DP
of the product. Low-DS (≤ 0.3) CMC is insoluble in water but soluble in alkaline solutions,
while high-DS (> 0.4) are water soluble. Besides, the solubility and viscosity are also affected
by medium pH.
CMC with DS of 0.7~1.0 is used to increase the viscosity of foods. Their aqueous
solutions exhibit the characteristics of non-Newtonian fluid and the viscosity decreases with
temperature elevation. CMC solution is soluble in pH range 5~10 and is most stable in pH
7~9. Monovalent cations form soluble complex with CMC, divalent cations reduces CMC
solubility, whereas trivalent cations can cause gelling or precipitation of CMC.
CMC can be used to improve the solubility of such food proteins as gelatin, casein, and
soybean protein by complexing with these molecules. CMC can maintain the stability of the
dispersion system of proteins even in their isoelectric points.
Due to the excellent rheologic properties, safety, and indigestibility, CMC is added to
jellies, paste fillings, spreadable process cheeses, salad dressings, and cake fillings as binding
and thickening agent. Meanwhile, because CMC has strong water binding capacity, it is
86 Dongfeng Wang, Jipeng Sun, Guoqing Huang et al.
widely used in ice creams and other foods to prevent ice crystal formation. CMC also
increases the volume and elongate shelf life of cakes and other bakery foods, improves the
mouthfeel of sucrose and prevent CO2 escape from low-calorie carbonated beverage.
MC is the etherified derivative of cellulose and is prepared by treating alkaline CMC with
chloroform. The DS of commercially important MC lies in the range 1.1~2.2.
MC is characterized by its gelling properties. When a MC solution is heated, the initial
viscosity drops with rising temperature and then increases sharply. This can be explained by
the breakdown of hydration layer around MC molecules upon heating, which increases the
hydrophobic interactions between MC molecules. Electrolytes such as NaCl and
nonelectrolytes such as sucrose and sorbierite reduce the gelling temperature of MC by
competing for water molecules. MC cannot be digested by human body and is a calorie-free
polysaccharide.
HPMC is prepared by incubating cellulose with methyl chloride and cyclopropane in
alkaline solutions. The DS of commercial HPMC ranges from 0.002 to 0.3.
The initial viscosity of HPMC solution decreases with temperature elevation and the
formation of gel is reversible at specific temperature, which is similar to that of MC. The
gelling temperature and gel strength are related to the type of substation groups, DS and
concentration of the soluble gel. The hydroxypropyl group stabilizes the hydration layer of
HPMC and thereby increases the gelling temperature. Changing the proportion of methyl to
hydroxypropyl substituents can vary the jelling temperature within a wide range.
MC and HPMC increase the water retention and absorption capabilities of foods and
prevent excessive oil absorption in fried foods. MC can be added to functional foods as
fillings and dehydration and shrinkage inhibitors. The two derivatives are added to salad
dressings as thickening and stabilizing agents and to various foods as edible coatings and fat
substitutes.
Hemicellulose
Hemicelluloses occur along with cellulose in the cell walls of plant cells and consist of
multiple monomers in contrast to cellulose, such as xylose, mannose, galactose, rhamnose,
and arabinose in addition to glucose. The compositions of hemicelluloses vary with the plant
origin and tissue. For example, wheat and rye contain mainly arabinoxylans, while β-glucans
predominate in barley and oats.
In the food industry, hemicellulose is mainly added to bakery foods to increase the water
binding capability of flour, improve the kneading quality of dough by reducing the energy
required by kneading, and increase bread volume. Breads containing hemicellulose have
delayed hardening time compared with those without hemicellulose. Hemicellulose is an
important source of dietary fiber.
Carbohydrates 87
Pectin
gelation, the addition of 10%~20% sucrose markedly improves the texture of gels. LM gels
are less rigid or elastic than common pectin gels, but sugars or plasticizing agents improve the
properties. LM pectin, since it does not require sugar for gelation, is used to make dietetic
jams, jellies, and marmalades.
Agar
Table 3-16. Effects of degree of methyl esterification on the gelling properties of pectin
The hydroxyl groups on the chains are more or less esterified by methyl, sulfuric acid,
and pyruvic acid. Commercial agar is colorless or light yellow strips or powder. Agar is
insoluble in cold water, but dissolves slowly in hot water. The β-1,4-glycodic bonds can be
specifically hydrolyzed by the agarlytic enzymes derived from soil and marine organisms to
yield agar oligosaccharide. Figure 3-44 illustrates the structure of agarose.
Application
Agar is a most potent gelling agent in the food industry and is widely used in candies,
puddings, ice cream, gelly, and many other foods as gelling agent. Besides, agar is
indigestible and is a good source of dietary fiber. In the fermentation industry, agar has been
widely used to encapsulate enzymes and microbes.
Carrageenan
Carrageenans are mixtures of several related galactans having sulfate half-ester groups
attached to the sugar units and are extracted from the red seaweeds (Rhodophyceae).
Carrageenans are important commercial hydrophilic gels.
Carrageenans are linear chains of D-galactopyranosyl units joined with alternating (1,3)-
D- and (1,4)-D-glycosidic linkages, with most sugar units having one or two sulfate groups
esterified to a hydroxyl group at carbon atoms C-2 or C-6. The molecular weights (MWs) of
carrageenan range from (1~5)×105 and the average MW of food-grade carrageenans is 2×105.
According to the positions of sulfate half-ester groups, carrageenans are divided into κ-, ι-, λ-,
μ-, υ-, θ-, and δ- classes. Figure 3-45 presents the structures of the 7 carrageenan classes.
Alginate
Alginate, also termed algin or alginic acid, is an anionic polysaccharide obtained from
brown seaweeds. Commercial alginate is often available as sodium salt.
92 Dongfeng Wang, Jipeng Sun, Guoqing Huang et al.
Chitin is the second most abundant natural polysaccharide in the world and its annual
product is 1×1011 tones, which is only behind that of cellulose. It is also the most abundant
naturally occurring polysaccharide that contains amino sugars. Chitosan is the deacetylated
products of chitin and has improved solubility and functional properties. Their abundance,
combined with their specific properties and functions, impart them with wide applications in
the food industry.
Antibacterial agent
Chitosan and its derivates have strong antibacterial activities. Chitosan carries positive
charges and can adhere to negatively charged membranes of bacteria, leading to the leakage
of intracellular proteins and other components.
Fruit preservative
Chitosan can prevent the spoilage and decay of peach, kiwi fruit, cucumber, pepper, and
strawberry and markedly increase their shelf lives. This is because chitosan has strong film
forming capability. The film formed hinders the diffusion of oxygen to fruits and the escape
of CO2 generated by respiration, but allows the release of ethylene.
Antioxidants
It has been reported that the addition of chitosan at 1% resulted in a 70% decrease in the
2-thiobarbituric acid (TBA) values of meat after 3 days storage at 4 °C. The mechanism by
which this inhibition takes place is believed to be related to the chelation of free iron released
94 Dongfeng Wang, Jipeng Sun, Guoqing Huang et al.
from the hemoproteins of meat during heat processing or storage. This would in turn inhibit
the catalytic activity of iron ions [30].
Functional ingredients
After chitosan is absorbed, it can form indigestible complexes with triglycerides, fatty
acids, bile acid, and cholesterol. To complement for the bile acid that is associated with
chitosan, the liver increases the secretion of bile acid. Since bile acid is converted from
cholesterol in the liver, the content of cholesterol in liver and blood is deceased. Hence,
chitosan is an effective ingredient of functional foods.
Juice clarificant
Fruit juices become turbid after long-time storage due to the presence of negatively
charged pectin, cellulose, tannin, and pentosan. The positively charged chitosan can coagulate
these components by electrostatic attraction and hence is widely used in fruit juice
clarification. Chitosan has high affinity to polyphenolic compounds, such as catechin and
cinnamic acid. Chitosan has been added to grape wines to remove these components.
Chitosan-treated grape wines are dark golden yellow compared to the light yellow of
untreated products and hence have improved quality.
Water clarificant
Chitosan is more effective in removing polychlorobiphenyl (PCB) than active carbon.
Chitosan in combination with bentonite can effectively remove particles, color, and odor of
drinking water and that in combination with polysilicate, polyaluminosilicate, and ferric
chloride markedly reduces the COD and turbidity of water.
Micro-ecological regulator
COS is a Bifidobacterium proliferative factor and can selectively enhance the growth of
intestine probiotics and inhibit the proliferation of harmful bacteria and formation of spoilage
substances.
Functional sweetener
Chitobiose and chitotriose have pleasant sweetness and are superior to sucrose in
thermostability. The two compounds cannot be digested by human body and are ideal
functional sweeteners for the diets of diabetic and fat patients.
Carbohydrates 95
Antibacterial agent
The antibacterial activity of COS is related to its molecular weight and medium pH. It is
generally recognized that COS of molecular weight 1500 has the highest antibacterial
activity. Medium pH affects the dissociation of amino groups and therefore influences the
antibacterial activity. COS is more effective in inhibiting microbial growth in acidic medium
than in neutral or alkaline medium. Short-chain COS, such as those with seven or more
monomers, can enter inside microbial cells and inhibit the biosynthesis of mRNA and
proteins by binding to DNA, thus killing the microbes.
COS is more effective in inhibiting the growth of molds in soy sauce than benzoic acid
and sodium benzoate without affecting the taste and color of soy sauce.
Preservative
COS has abundant free amino and hydroxyl groups and therefore has strong water
retention capability. The mixture of COS and high-molecular weight chitosan with strong
film forming ability has been used as fruit and vegetable coatings to prevent water
evaporation and Vc loss and elongate the shelf life. COS also significantly reduces the
spoilage rate of fruits and vegetables as chitosan.
COS of DP 3~7 reduces the excretion of fecal calcium and increases the fracture force of
rat thighbone in contrast to chitosan, which hinders the absorption of calcium.
Guar gum and locust bean gum are important thickening polysaccharides and are widely
used in the food and other industries. Guar gum produces the highest viscosity of all natural
and commercial gums.
Guar gum is also known as guaran and occurs in the endosperm of the seeds of guar bean
(Cyamopsis tetragonolobus). It is composed of galactose and mannose and the backbone is a
linear chain of β-1,4-linked mannose residues to which galactose residues are 1,6-linked at
every second mannose, forming short side-branches. The structure of guar gum is shown in
Figure 3-46.
Guar gum readily absorbs water and is rapidly hydrated in cold water to produce highly
viscous and thixotropic fluids. The viscosity of guar gum solutions is affected by temperature
and the presence of other components.
Heating accelerates the dissolution of guar gum, but it can be decomposed in high
temperatures. Because guar gum yields very high viscosity even in low concentration, the
addition of guar gum in foods is generally less than 1%.
The aqueous solution of guar gum is neutral and its viscosity is not affected by pH.
Hence, guar gum is compatible with most food components. Ionic strength has little effects on
the viscosity of guar gum solutions, but the presence of high concentrations of sucrose
96 Dongfeng Wang, Jipeng Sun, Guoqing Huang et al.
reduces the viscosity and delays the arrival of the peak viscosity. Wheat starch synergistically
improves the viscosity of guar gum solutions.
Guar gum prevents ice crystal growth and produces desired consistency, chewiness, and
heat stimulation resistance in ice cream. In cheese, guar gum is added to avoid syneresis. In
bakery foods, guar gum elongates the shelf life and reduces the water absorption of sucrose in
the glace of pastries.
Locust bean gum, also called carob gum, occurs in the seeds of carob tree (Ceratonia
siliqua). It structure is similar to that of guar gum, except that the galactose residues are
distributed randomly along the β-1,4-linked mannose backbone.
The ratio of mannose/galactose residues of locust bean gum ranges from 3:1 to 6:1 and its
molecular weight is about 31000. Due to the irregular distribution of galactose residues, some
mannose residues are exposed or naked without attached galactose residues. Due to this
difference, locust bean gum has different properties compared to guar gum. For example, the
viscosity of locust bean gum solutions is lower than that of guar gum solutions.
Locust bean gum is used as a thickener, binder and stabilizer in canned meats, salad
dressings, sausages, soft cheeses, and ice creams. It also improves the water binding capacity
of dough especially in the case of low-gluten flour. Locust bean gum can improve the
viscosity of other gelatinous polysaccharides. For example, the viscosity of the solution
containing 0.5% agar and 0.1% locust bean gum is 5 times higher than that of agar alone.
Gum Tragacanth
Gum tragacanth is a plant exudate collected from the plants of the Astragalus genus. The
gum has been used for over 2000 years as Arabic gum and is mainly produced in Iran, Syria,
and Turkey.
Gum tragacanth has a very complex structure and composition. When gum tragacanth is
suspended in water, one fraction is dissolved and this part is called tragacanthic acid.
Tragacanthic acid accounts for 60%~70% of gum tragacanth and consists of 43% D-
galacturonic acid, 10% fucose, 4% D-galactose, and 40% D-xylose and L-arabinose, of
which, the galacturonic acid residues form the backbone and the other residues are attached as
side chains. The molecular weight of tragacanthic acid is about 800000. The insoluble
fraction is termed bassorin, which contains 75% L-arabinose, 12% D-galactose, and 3% D-
galacturonase and L-rhamnose with molecular weight of 84000.
Gum tragacanth produces high viscosity and hence is used as thickening agents. Gum
tragacanth is used as a thickening agent and a stabilizer in salad dressings (0.4–1.2%) and in
fillings and icings in bakery goods. As an additive in ice creams (0.5%), it provides a soft
texture.
Microbial Polysaccharides
Microorganisms can produce multiple polysaccharides, of which, dextran and xanthan are
the most important for the food industry.
Dextran is an extracelluar polysaccharide produced by Leuconostoc mesenteroides,
Streptobacterium dextranicum, Streptococcus mutans and other species. Dextran is composed
of glucose units, of which, the monomers in the straight chain are connected through α-1,6
linkages, while branches begin mainly from α-1,3 linkages (Figure 3-47), with part 1,4- and
1,2- linkages. The type and number of the glycosidic linkages vary with the source. The
dextran produced by Leuconostoc mesenteroides NRRL B512 contains 95% 1,6- linkages and
the remaining 5% are 1,3- and 1,4- linkages.
Dextran is used in confections to improve viscosity and water retention and inhibit sugar
crystallization. In chewing gum and soft sweets, dextran is added as gelling agent. Dextran
inhibits ice crystal formation in ice creams and provides desired consistency and mouthfeel
for puddings.
Xanthan is secreted by multiple species of the Flavobacterium genus and the commercial
xanthan is produced by Xanthomonas campestris. Xanthan can be considered as derivative of
cellulose.
On an average, every second glucose residue bears in the 3-position a trisaccharide of the
structure β-D-Manp- (1→4)-β-D-GlcpA(1→2)-α-D-Manp as the side chain. The mannose
bound to the main chain is acetylated in position 6 and ca. 50% of the terminal mannose
residues occur ketalized with pyruvate as 4,6-O-(1-carboxyethylidene)-D-mannopyranose
(Figure 3-48). The molecular weight of xanthan is greater than 2×106 Dal.
Xanthan is readily soluble in both cold and hot water and provides high viscosity even in
low concentrations, but the jellification is weakened in high xanthan concentrations. Xanthan
solutions are pseudoplasitc fluids and exhibit obvious shear thinning. Xanthan is compatible
with most edible salts and edible acids and can coexist with them in foods. Xanthan interacts
with guar gum to give rise to a synergistic increase in solution viscosity and with locust bean
gum to produce a heatreversible gel.
Xanthan is widely used to stabilize aqueous dispersions, suspensions, and emulsions.
Xanthan is added to juices and canned foods as suspending and stabilizing agents. In starch
gels, the addition of xanthan gum substantially improves their freeze-thaw stability and
reduces syneresis. Due to the high stability of xanthan gels, xanthan can be used in seasonings
with high salt contents or acidity.
Glucomannan
Gum Arabic
Gum Arabic is extracted from the exudate of various Acacia species, primarily Acacia
senegal. Gum Arabic is a proteoglycan and its molecular weight lies in the range
260000~1160000. The glycan fraction accounts for 70% of the total gum and consists of L-
arabinose, D-galactose and D-glucuronic acid in the molar ratio of 3.5:1.1:2.9:1.6. The
backbone of gum Arabic consists of β-D-galactopyranosyl residues linked by 1→3 bonds and
side chains are attached at position 6 (Figure 3-49). Gum Arabic is present as acidic or neutral
salts and the counter ions are Ca2+, Mg2+, and K+. The protein fraction accounts for 2% of the
Carbohydrates 99
total gum, but the value can reach up to 25% in some species. The glycan fraction is
covalently connected to the hydroxyproline and serine residues of the protein fraction.
Gum Arabic is readily soluble in water and provides low viscosity, but the viscosity
increases dramatically in high gum Arabic concentrations. This property is different from
other polysaccharides, which can provide high viscosity even in low concentrations. The
solubility of gum Arabic reaches up to 50% by weight. Arabic gum solutions with
concentration less than 40% are Newtonian fluids, but those with higher concentrations
exhibits the pseudoplastic behavior.
In the presence of ions, the viscosity of gum Arabic solutions varies with pH and the
highest viscosity is obtained at pH 6~8. The viscosity reduces proportionally when the
valence and concentration of ions increases. Gum Arabic is compatible with most gums,
except gelatin and sodium alginate.
Gum Arabic is used as emulsifier and stabilizer. It retards sugar crystallization and fat
separation in confectioneries and large ice crystal formation in ice creams, and can be used as
a foam stabilizer in beverages. Gum Arabic is also applied as a flavor fixative in the
production of encapsulated, powdered aroma concentrates. For example, essential oils are
emulsified with gum Arabic solution and then spray-dried. In this process, the polysaccharide
forms a film surrounding the oil droplet, which protects the oil against oxidation and other
changes.
DIETARY FIBER
Dietary fibers (DF) were once considered as nonnutritive crude fibers and unimportant
for human diets. However, with the rapid improvement of social economy and people's living
standards, people‘ dietary structure changes greatly. The proportion of plant-derived foods in
diets decreases obviously and that of animal-derived foods containing high calorie, high
protein content and high fat contents increases significantly instead, which impairs the
nutrition balance of the diets. Due to the imbalance, the incidences of adiposity, hypertension,
diabetes, cancer, and cardiovascular diseases keep rising. The emergency of these diseases
has been contributed to the decreased intake of DF and DF has been widely accepted as the
seventh essential nutrient.
Definition
Various definitions of dietary fibers have been proposed. In 1987, FDA and WHO
defines dietary fiber as ―the material isolated by AOAC method 985.29‖. In 1998, dietary
fiber was defined by a committee of dietary fiber experts of the American Association of
Cereal Chemists (AACC) as ―the edible parts of plants or analogous carbohydrates that are
resistant to digestion and absorption in the human small intestine with complete or partial
fermentation in the large intestine. Dietary fiber includes polysaccharides, oligosaccharides,
lignin, and associated plants substances. Dietary fibers promote beneficial physiological
effects including laxation, and/or blood cholesterol attenuation, and/or blood glucose
attenuation‖. The definition proposed by AACC has been widely accepted in the world.
Classification
By Solubility
Based o solubility, DF is subdivided into soluble DF (SDF) and insoluble DF (IDF).
SDF is soluble in warm and hot water and absorb water to gel. Dissolved SDF can be
precipitated by 4 volumes of ethanol. SDF mainly includes pectins, gums (gum Arabic, guar
gum, locust bean gum, and agar), mucilages, and some hemicelluloses. IDF is insoluble in hot
water and is the important component of plant cell wall, including cellulose, hemicellulose,
ligin, protopectin, vegetable wax and some animal-derived compounds, such as chitin and
chitosan.
Carbohydrates 101
SDF and IDF have different physiological and health functions. IDF cannot be
metabolized by human body, but can absorb water as it moves through the digestive system,
thus easing defecation. SDF can be partially fermented by the microorganisms inhabited in
the colon and produce active byproducts. SDF protects against cholesterol gallstone [33],
increase heavy metal evacuation, reduce cholesterol levels in serum and liver, inhibit
postprandial blood glucose increase, and prevent hypertension and heart disease. IDF
increases defecation and prevents obesity, laxation, and intestinal cancers. The ratio of IDF to
SDF markedly affects the physiological functions of DF.
By Source
DF can be obtained by extraction from plants (including algae) and animals or by
synthesis, of which, plants are the major source at present. Chitin and chitosan are typical
representatives of animal-derived DF. Dextran is a water soluble DF. In addition to
microorganism, it is also synthesized from dextrin by transglucosylation of dextrin dextranase
(EC 2.4.1.2) [34].
Physichemical Properties
DF molecules with ordered and less branched structures have strong inter-molecular
bonding capacities and thereby poor solubility. For example, the linear cellulose is insoluble,
but pectins with irregular structure are readily water soluble. Insoluble DF can be converted
to soluble DF by high temperature, high pressure, or shearing force. Conversion of IDF to
SDF is an important measure to improve DF quality. SDF are viscous upon ingestion and can
complex with heavy metals, fats, and cholesterol.
Water retention
Most DFs contain abundant hydrophilic groups and can absorb much water. The water
retention capacity of DFs varies with the source, composition, structure, preparation method,
and particle size. Generally, cellulose-based DFs have lower water retention capacity
compared with other DFs. Too low particle sizes reduce the index. Besides, high temperature
treatment, cooking, and enzymatic hydrolysis could change the physical properties of DFs
and thereby influence the water retention capacity.
The abundant active groups on the surface of DF can absorb bile acid, cholesterol, and
mutagens in the intestines of human body and therefore affects their metabolism and
adsorption.
Some DFs contains carboxyl groups, hydroxyl groups, amino acids, and some other
active groups. Various cations, such as Ca2+, Fe2+, Zn2+, Cu2+, and Pb2+, can bind to these
groups or exchange with the ions attached to these groups. The binding or exchange is
reversible and changes the pH, osmotic pressure, and redox potential of the intestine and
provides a buffering environment that is beneficial for digestion and absorption. Cations with
high polarizability, such as Pb2+, are preferred in absorption by DF. Hence, DF has the
function of removing toxic metals. The ions bound to DF can exchange with Na+ and K+. The
exchange reduces the Na+/K+ ratio in the blood and consequently lowers the blood pressure. It
should be noted that DF also reduces the adsorption of some beneficial elements. Hence, it is
necessary to supplement some minerals in DF-containing foods to avoid mineral imbalance.
Prebiotics
DFs are only partially fermented in the colon. DFs are the nutrition source of the
microbes in the colon and support the growth of multiple bacteria, of which, most are
beneficial for human body. Besides, DFs can induce the substantial propagation of aerobes
and thereby reduces the incidence of some cancers.
Bulking effect
DFs have markedly increased volume after swelling and can cause satiety. Besides, the
presence of DF affects the digestion and absorption of other food components and delays the
feeling of hunger. Hence, DFs are effective in preventing adiposity.
Metabolism
As mentioned in the definition, DFs cannot be digested in the mouth, stomach, or small
intestine and only partially fermented by the microbes in the large intestine. The degree and
rate of decomposition are associated with the solubility, chemical structure, particle size, and
ingestion mode of DF. Soluble DFs, such as pectin and seaweed gums, are readily digested in
the large intestine, but insoluble cellulose cannot be easily utilized by intestinal
microorganisms. Some of the metabolites, such as fatty acids, can be absorbed by human
body as energy source and some metabolites have important physiological functions.
Safety Aspects
Although DFs have multiple beneficial effects on human body, excessive intake of DFs
can cause discomfort and affect the absorption of fats, proteins, and essential elements. It
should be mentioned that these effects vary with DF composition and individuals.
Some IDFs, such as guar gum, can be fermented by intestinal microorganisms to produce
volatile fatty acids, carbon dioxide, and methane, which can cause abdominal distension. The
filling effect of DFs reduces the adsorption of proteins, fatty acids, and carbohydrates and the
increased viscosity of gastrointestinal fluids prevents the contact between these substrates
Carbohydrates 103
with digestive enzymes. Hence, DFs reduce their bioavailability. DFs can bind metal ions and
can reduce their absorption.
Some DFs interfere with the absorption of vitamins. It is reported that konjac mannan
reduces fat-soluble vitamin absorption by removing bile acids, but does not reduce fat-
insoluble vitamin absorption in the intestine [35].
No uniform standards have been formulated for the daily intake of DFs due to the
complexity of DFs and individual differences. The daily intake recommended by FDA is
20~35g for adults and that in Japanese is 20 g or more. The Chinese Nutrition Association
enacted the Chinese dietary intake references in 2000 and suggests that the daily dietary fiber
intake of adults is 30.2 g.
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In: Food Chemistry ISBN: 978-1-61942-125-7
Editors: D.Wang, H. Lin, J. Kan et al. © 2012 Nova Science Publishers, Inc.
Chapter 4
LIPIDS
ABSTRACT
Lipids are a broad group of naturally-occurring molecules that are soluble in organic
solvents but insoluble or only sparingly soluble in water. Triacylglycerols account for
95% of total lipids in foods. Lipids are major energy source for human body and protect
human body from mechanical damage and heat loss. Lipids are also the carriers of fat-
soluble vitamins and the precursors of many bioactive molecules such as prostaglandin,
sex hormone, and epinephrine. This chapter deals with the nomenclature, classification,
and fatty acid distribution theories of lipids and their functional properties, including
polymorphism, plasticity, and emulsification. Lipids undergo multiple chemical reactions
during processing and storage, such as hydrolysis, oxidation, and thermal decomposition.
The effects of these reactions, especially oxidation, on food flavor and safety are
elucidated in detail. Lipid processing techniques, including refinement, hydrogenation
and interesterification, are also concerned in this chapter.
1. INTRODUCTION
It should be understood that though the term lipid is used majority of the times as a
synonym for fats, in fact, fats are a subgroup of lipids called triglycerides. Lipids encompass
molecules such as fatty acids and their derivatives including tri-, di-, and monoglycerides and
phospholipids, as well as other sterol-containing metabolites such as cholesterol. Humans and
other mammals have a variety of pathways to synthesize and metabolize lipids. Some lipids
cannot be synthesized by mammals and therefore must be ingested from the diet. Such lipids
are termed essential fatty acids (EFAs).
108 Shengrong Shen, Dongfeng Wang and Undurti N. Das
All plants and animals eaten by humans contain lipids. Various vegetables and most fruits
contain very little amounts of lipids, generally about 0.3%, except avocado, whose edible
portion contains about 20% lipids. The lipid content in the muscle tissue of lean beef, fish,
white poultry, and shell fish is about 2%, about 3.7% in cow‘s milk, about 2-4% in grains,
about 30% in fatty pork, 32% in an egg yolk, and about 35% in fillets of fatty fish. Oil-
bearing nuts and seeds contain from 20% fat in soybeans to 65% fat in walnuts.
1.1. Nomenclature
Trivial nomenclature
Lipids are named according to their sources, such as palmitic acid, lauric acid, butyric
acid, stearic acid, and oleic acid.
Systematic nomenclature
Symbol nomenclature
Fatty acids can be represented by a simple numerical expression consisting of two terms
separated by a colon, with the first term depicting the number of carbon atoms and the second
the number of double bonds. For example, hexadecanoic acid,
CH3CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2COOH
can be named as 16:0 and linoleic acid (9, 12-octadecadienoic acid) can be presented as 18:2.
This notation can be ambiguous, because some different fatty acids might have the same
numbers.
Unsaturated fatty acids can be named in the n-x or ω-x system. In this system, the
terminal methyl carbon is designated as ω or n and x represents the location of the first double
bond. Carbon atoms are counted from the terminal methyl carbon (namely ω or n) to the
carbonyl carbon. Because all adjacent double bonds in all natural polyenoic acids (containing
2 to 6 double bonds) are spaced by a methylene, the locations of all other bonds can be
determined if the first double bond is specified. For example, linoleic acid is presented as
18:2(ω-9). Because the first double locates in the 9th carbon, the second double occurs
between C12 and C13.
The geometric configuration of double bonds is usually designated by the use of cis and
trans, indicating whether the alkyl groups are on the same or opposite sides of the molecule.
Unsaturated fatty acids occur naturally in the cis form, but the trans form is more
thermodynamically stable.
If the four groups attached to the two carbon atoms of a double bond are different, the
configuration can be designated according to the Cahn-Ingold-Prelog rules. In this system,
each group is assigned a priority. If the two groups with higher priority (greater atom number)
locate in the same side of the double bond, the letter Z is used to designate the configuration.
If the two groups are on the opposite sides, the letter E is used.
Table 4-1 lists the systematic and common names of some fatty acids in naturally-
occurring lipids.
Figure 4-1. Structure of acylglycerols. R denotes fatty acid; there may be fatty acid, two fatty acids or
three fatty acids in the acylglycerols, which is mono-acyglycerol, di-acyglycerol or triacylglycerol
respectively; R1=R2=R3, the triacylglycerol is defined as simple triacylglycerol, otherwise mixed
triacylglycerol.
1.1.2. Acylglycerols
Lipids are the mixtures of mono-, di-, and triesters of glycerol with fatty acids, which are
termed monoacylglycerols, diacylglycerols, and triacylglycerols, respectively. Natural fats are
mainly present as triacylglycerols.
In order to designate the configuration of glycerol derivatives, the stereospecific
numbering (Sn) system is used in acylglycerol nomenclature. In this system, the carbon atom
that appears on top in that Fischer projection that shows a vertical carbon chain with the
hydroxyl group at carbon-2 to the left is designated as C-1 and the prefix 'sn' (for
stereospecifically numbered) is printed immediately preceding the glycerol term. An example
is shown in Figure 4-1. If R1 denotes stearic acid (St), R2 oleic acid (O), and R3 linoleic acid
(L) in the structure, this triacylglycerol is named Sn-glycerol-1-stearic acid-2-oleic acid-3-
linoleic acid, Sn-18:0-8:1-18:2, or Sn-StOL.
If the product is the racemic mixture of two antipodes, the prefix 'rac-' (for racemo) can
be used preceding the full name, such as in rac-StOM. In this case, the middle acid (O,
standing for the oleic acid) is in position 2 and the remaining two fatty acids (St and M,
standing for stearic and myristic acids respectively) are equally distributed in positions 1 and
3.
If the prefix β is used before the name, such as β-StOM, it indicates that the middle acid
is in position 2, but the distribution of the other two acids is unknown.
In the case of simple triacylglycerols or those with unknown fatty acids distribution, the
prefix can be omitted. For example, StOM can be used to express any mixture of Sn-StOM,
Sn-MOSt, Sn-OStM, Sn-MStO, Sn-StMO, and Sn-OMSt.
1.1.3. Phospholipids
Phospholipids refer to any lipids that contain phosphoric acid in the structures as mono-
or diester. According to the type of hydroxyl donors, phospholipids are divided into
phosphoglycerides and sphingolipids (sphingophospholipids), in the former structure the
alcohol is glycerol and the later sphingosine.
1.2. Classification
Based on chemical structure and composition, lipids can be divided into simple lipids,
compound lipids, and derived lipids.
Simple lipids are compounds consisting of fatty acids and alcohols and include fats, oils,
and waxes.
Compound lipids contain many other groups in addition to fatty acids and alcohols.
Glycerophosphonolipids, sphingomyelins, cerebroside, and ganglioside are the examples of
compound lipids.
Derived lipids are the derivatives of simple and compound lipids and have the common
properties of lipids. Steroids, hydrocarbons, carotenoid, and fat-soluble vitamins are examples
of this group.
Most lipids in foods are acylglycerols. According to composition, lipids in animal and
plant-derived foods are divided into the following:
Milkfat
Milkfat exists in the latex of mammals. Milkfat consists mainly of palmitic acid, oleic
acid, and stearic acid. Compared with other animal-derived lipids, milkfat contain abundant
C4~C12 short-chain fatty acids, small amounts of odd- and branch-chain fatty acids, and
trans double bonds.
Laurates
Laurates are mainly found in palme plants such as coconut palm and babassu. Laurates
are featured by their high lauric acid contents, which reach up to 40%~50%. Laurates have
medium contents of C6, C8, and C10 fatty acids, low unsaturated fatty acid contents, and low
melting points.
Plant butter
Plant butter originates from the seeds of tropical plants and is characterized by narrow
melting point range. Although plant butter has a higher content of saturated fatty acids than
112 Shengrong Shen, Dongfeng Wang and Undurti N. Das
unsaturated fatty acids, trisaturated glycerides have not been identified in plant butter. Plant
butter is widely used in candies and cocoa butter is the most important plant butter.
Oleate-linoleate
Lipids of this category are the most abundant in nature and are found only in plants. The
lipids have high contents of oleic acid and linoleic acid and the contents of saturated fatty
acids are less than 20%. Peanut oil, corn oil, olive oil, palm oil, sesame oil, cottonseed oil,
and sunflower oil are important members of this category.
Linolenates
Linolenates contain large amount of linolenic acid and soybean oil, wheat germ oil, and
perilla oil belong to this category.
Animal fats
Lipids of this group, such as lard and tallow, are the storage fat of domestic animals.
Animal fats contain large amount of C16 and C18 fatty acids and medium contents of
unsaturated fatty acids, mostly oleic and linoleic acids, and small amount of odd-numbered
fatty acids. Animal fats contain appreciable amount of fully saturated triacylglycerols and
thus exhibit high melting points.
Marine oils
Marine oils contain abundant long-chain unsaturated fatty acids and are rich in vitamins
A and D. Eicose pentaenois acid (EPA) and docosahexenoic acid (DHA) are typical examples
of this category. Due to high unsaturation degree, marine oils are susceptible to oxidation.
This theory was proposed by Hilditch and Williams in 1964 [1]. According to this theory,
the fatty acids in triacylglycerols tend to be distributed as broadly as possible. In this case,
when an acid, S, accounts for less than one-third of the total fatty acids present, it should not
appear more than once in any triacylglycerol. If X refers to the other fatty acids present, only
XXX and SXX species should be found. If a fatty acid accounts for between one-third and
two-thirds of the total fatty acids, it occurs at least once but never three times in any one
Lipids 113
molecule; that is, only SXX and SSX should be present. If a fatty acid forms more than two-
thirds of the total acids, it should occur at least twice in every molecule; that is, only SSX and
SSS should be present.
However, analysis of many natural fats, especially those of animal origin, reveals marked
deviation from this theory. Trisaturated acylglycerols have been found in fats containing less
than 67% saturated fatty acids. This theory is applicable only to triacyglycerols that consist of
two components and does not take positional isomers into consideration. This theory is no
longer considered valid.
According to this theory, fatty acids are distributed randomly both within each
triacylglycerol molecule and among all the triacylglycerols. Thus, the fatty acid composition
of all the three positions of glycerol should be the same and also equivalent to the fatty acid
composition of the total fat. The proportion of any given fatty acid species can be calculated
according to the following equation:
%sn-XYZ = (mol% X in total fat) × mol% Y in total fat) × mol% Z in total fat) × 10-4.
For example, if a fat contains four fatty acids, including 8% palmitic acid (P), 2% stearic
acid (St), 30% oleic acid (O), and 60% linoleic acid (L), 64 possible triacylglycerol species
would exist. The percentages of any species can be calculated by taking the following
equations as example:
The fatty acid distribution of most lipids does not conform to the random distribution
theory. In natural lipids, the fatty acids in the Sn-2 position are different from those in
positions Sn-1 and Sn-3. Hence, great deviation exists between the predicted and actual
distribution of fatty acids in natural lipids. However, this theory can be used to predict the
fatty acid distribution in randomly interesterified fats.
This theory was initiated by Kartha in 1953 [2]. According to this theory, saturated and
unsaturated fatty acids in animal fats are distributed randomly. Fully saturated triacylglycerols
(SSS) can be present, but only to the extent that the fat can remain fluid in vivo. Excess SSS,
according to this theory, can exchange with UUS and UUU to generate SSU and SUU.
Kartha's calculations do not account for positional isomers or positioning of individual acids.
1, 3-Random-2-Random distribution
114 Shengrong Shen, Dongfeng Wang and Undurti N. Das
This theory was proposed by Vander al, Coleman, and Fulton between 1960 and 1961
based on their researches of directed hydrolysis of Sn-1 and Sn-3 fatty acids by steapsin.
According to this theory, the fatty acid composition at position 2 is different and independent
from that of positions 1 and 3 and fatty acids are distributed randomly in Sn-2 and Sn-1,3.
Thus, the composition at positions 1 and 3 will, presumably, be identical. According to this
theory, the content of any given triacylglycerol can be calculated with the following equation:
This theory was proposed by Tsuda in 1962. According to this theory, fatty acids are
separately but randomly distributed at each of the three positions of the triacylglycerol
molecules of a natural fat. Thus, the possibility of a given fatty acid appearing in each Sn
position would likely be different. The content of a given triacylglycerol species can be
calculated as:
This theory is applicable to the predication of common animal fat, milkfat, and seed fats.
Table 4-2. Positional distribution of fatty acids in triacylglycerols of some natural fats
[3]
Source Position 14:0 16:0 18:0 18:1 18:2 18:3 20:0 20:1 20:2 20:0
Coconut 1 34 50 12 1
2 2 2 87 9
3 37 53 9 -
Peanut 1 14 5 59 19 1 1 1
2 2 - 59 39 - - 0.5
3 11 5 57 10 4 3 6 3
Soybean 1 14 6 23 48 9
2 1 22 70 7
3 13 6 28 45 8
Lipids 115
Source Position 14:0 16:0 18:0 18:1 18:2 18:3 20:0 20:1 20:2 20:0
Beef 1 4 41 17 20 4 1
2 9 17 9 41 5 1
3 1 22 24 37 5 1
Pig 1 1 10 30 51 6
2 4 72 2 13 3
3 - - 7 73 18
Lard has different fatty acid distribution patterns compared with other animal-derived
fats. For example, palmitic acid is mainly found in position Sn-2, stearic acid is distributed in
Sn-1, linoleic in Sn-3, and oleic acid in Sn-3 and Sn-1.
In milkfat, short-chain fatty acids attach specifically to position Sn-3, while the long-
chain polyunsaturated fatty acids are preferably esterified at position Sn-2 of marine oils.
The fatty acid distributions of some natural fats are listed in Table 4-2.
2.1.1. Density
The density of fatty acids and glycerides reduces with the increase of carbon chain length
and the decrease of degree of unsaturation. Generally, fatty acids and glycerides with high
hydroxyl and carbonyl contents have the highest density.
Natural lipids are the mixture of multiple acylglycerols and thus the relationship between
density and composition is rather complex. The densities of lipids are smaller than that of
water at room temperature and tend to decrease in higher temperatures. It is estimated that,
when a triacylglyceride is melted, its density decreases by about 10%.
For example, the smoking point of refined edible oil is generally higher than 240 °C, but
the presence of free fatty acids dramatically decreases the index. The flash point of plant-
derived edible oil is generally over 225-240 °C and the fire point is usually 20-60 °C higher
than the flash point.
heated to above 55 °C until completely melts and is then allowed to cool slowly until 29 °C.
The crystals are reheated to 32 °C to melt other crystal forms than the β form. The later
process is repeated until cocoa butter is completely transformed to the β form.
2.3. Plasticity
Lard and butter that are solids in room temperature are actually the mixtures of liquid oils
and solid fats. The lipids are completely solidified only in very low temperatures. Such
homogeneous mixtures of liquid oils and solid fats are defined as the plastic fat. Plastic fat
can maintain their shape even in exposure to external forces. The plasticity of fats is affected
by the following factors:
Fat crystals in the β' form have the best plasticity, because substantial amount of small
bubbles are trapped in the β' crystals. In contrast, only a small amount of air bubbles are
trapped in β crystals and the air bubbles are large in volume. Hence, fats in the β form have
less plasticity.
The fat/oil ratio significantly affects lipid plasticity. If the percentage of the solid phase is
too high, rigid crosslinking occurs and the fat exhibits high hardness and poor plasticity. If the
percentage of liquid phase is too high, the fat is flowable, soft, and susceptible to
deformation.
Figure 4-4. Heat content (H) or dilatometric (D) melting curve of a glyceride mixture [3].
Lipids 119
The solid phase to liquid phase ratio is also termed as the solid fat index (SFI). SFI is the
most important index that determines the plasticity of lipids and can be determined by
measuring the expansion of the fat, i.e. the volume increase of the fat during its transition
from solid to liquid.
The volumes of solid fat and liquid oil increase when heated. The expansion without
phase transformation is defined as thermal expansion. When solid fat is transformed to the
liquid state in high temperatures, the volume increase is called melting dilation. The melt-
expansion curve of plastic fats can be followed by measuring the specific volume change of
liquid oil and solid fat in different temperatures. As shown in Figure 4-4, solid fat starts to
melt at point X and is gradually melted until to point Y, at which the fat is completely
liquefied. The fat in point b is a mixture of solid and liquid. In this point, the percentage of
solid fat is ab/ac and that of liquid oil is bc/ac. Hence, the SFI in point b is ab/bc.
If a lipid melts in a very narrow temperature range, the slope between points X and Y is
high. Otherwise, the lipid exhibits a wide plastic range. Hence, the plastic range of lipids can
be modified by adding lipids with different melting points.
SFI can be measured exactly by using a dilatometer. However, measurement with
dilatometer is time consuming and is applicable only to fats with SFI less than 50%. Pulsed
nuclear magnetic resonance is the most common method for SFI determination. Because
ultrasonic travels faster in solid fat than in liquid oil, ultrasonic methods have been developed
for SFI measurement.
2.4.1. Emulsion
Emulsions are dispersed system composed of two immiscible liquids. In an emulsion
system, one phase is dispersed in another phase in the form of liquid crystal or droplets with
diameter ranging from 0.1 μm to 50 μm and is thus designated as the inner phase or dispersed
phase and is surrounded by the outer phase or continuous phase. According to the natures of
the two phases, two emulsion systems, including oil-in-water (O/W) and water-in-oil
emulsions (W/O), have been identified. Milk is an example of the O/W emulsion and cream is
an example of the W/O emulsion.
The formation of small dispersed droplets increases the area of the interface between the
two phases and the interface area increases exponentially when the droplet diameter is
decreased. Due to the increased interface area, high energy is required to maintain positive
free energy for the interfaces. Hence, emulsions are unstable thermodynamic systems and
demulsification might occur under specific conditions. Emulsions can be destabilized in one
of the following ways:
Creaming
When the two phases differ in density, one phase migrates to the top or bottom of the
emulsion due to gravity. Large droplet size of the dispersed phase and density difference
accelerate the creaming process.
120 Shengrong Shen, Dongfeng Wang and Undurti N. Das
Flocculation
When the amount of static charge on the surface of dispersed droplets turns insufficient,
the repulsion between droplets is reduced. As a result, the droplets attach to each other and
flocculation occurs. The membranes of droplets remain intact after flocculation.
Coalescence
The membranes of dispersed droplets are disrupted and the drops move to each other,
leading to coalescence. Coalescence reduces the interface area of the dispersed phase and
planar interface might occur when coalescence is serious.
2.4.2. Emulsifier
Emulsifiers are divided into anionic, cationic and nonionic types according to structure
and property. Based on origin, emulsifiers can be divided into natural and synthetic ones.
Based on functions, emulsifiers are divided into surfactants, viscosity reinforcing agents and
solid absorption agents. According to polarity, emulsifiers are divided into hydrophilic and
lipophilic ones.
Fatty monoglycerides and their derivatives (including glycerol monostearate and stearic
acid glyceride), sucrose fatty acid ester, sorbitan fatty acid ester and their derivatives (such as
sorbitan monooleate (Span 80) and polyoxyethylene sorbitan monostearate (Span 60)), and
phospholipids (such as modified soybean phospholipid), are widely used in the food industry
as emulsifiers.
Lipids can be hydrolyzed by acid, alkali, heat, and enzymes to release free fatty acids in
the presence of water. Triacylglycerols are firstly hydrolyzed to diacylglycerols, followed by
monoacylglycerols and finally glycerol in sequence.
Free fatty acids are not found in living animals, but can be liberated by enzymatic
hydrolysis after animals are slaughtered. When mature oil seeds are harvested, lipid
hydrolysis occurs. Free fatty acids are less stable than the corresponding glycerides and are
more susceptible to oxidative rancidity. Hence, oils are neutralized by alkali in refinement to
reduce free fatty acid content and improve the quality and shelf life.
Lipids 121
When foods are fried, water might migrate into hot lipids, leading to lipid hydrolysis and
fatty acid release. Frying decreases the smoke point of lipids and deteriorate the quality of
foods.
Lipid hydrolysis is not preferred in most cases. However, moderate lipid hydrolysis can
create special flavors for some foods. For example, in cheese production, microbes and milk
lipases are added to produce desired flavor. In breads and yogurts, lipid hydrolysis also
contributes to flavor formation.
3.2. Oxidation
3.2.1. Autoxidation
The autoxidation of lipids is a typical free radical chain reaction and the autoxidation rate
is markedly inhibited by chemicals which can interfere with free radical reactions. Light and
free radical-producing substances catalyze the reaction and the quantum yields exceed unity
when the oxidation reaction is initiated by light. Lipid autoxidation yields high levels of
hydroperoxides (ROOH) and the induction periods of pure substrates are longer than mixture
substrates.
The lipid autoxidation process is comprised of three steps: initiation, propagation, and
termination.
In initiation, the hydrogen atom on the α-carbon atom of the double bonds of unsaturated
fatty acids or their triacylglycerols (designated as RH) is detached by metal catalysis or
exposure to light or heat and a fatty acid radical known as the alkyl radical (R•) is produced.
R• then reacts with oxygen to produce peroxy radicals ROO•, which grabbles the hydrogen
atom from α-carbon atom of another molecules (RH) to yield hydroperoxides (ROOH) and
new free radicals R•. The reactions are repeated and lead to the propagation of lipid
autoxidation. Once these free radicals are combined to produce stable non-free radical
products, the chain reaction is terminated.
Initiation needs high activation energy and is therefore the limiting step of lipid
autoxidation.
122 Shengrong Shen, Dongfeng Wang and Undurti N. Das
Oleate
In autoxidation, the hydrogen atoms in C8 and C11 of oleates are detached and two
allylic radical intermediates are generated. Oxygen then attacks the end carbons of each
radical intermediates and an isomeric mixture of 8-, 9-, 10-, and 11-allylic hydroperoxides are
produced, as shown in Figure 4-5.
The percentages of 8- and 11-hydroperoxides are slightly higher than those of the 9- and
10-isomers in the mixture. When autoxidation occurs at 25 °C, the product mixture contains
equalmolar cis and trans 8- and 11-hydroperoxides and predominant percentages of trans 9-
and 10-isomers.
Linoleate
The hydrogen atoms attached to position 11 is highly active. Hence, only one radical
intermediate is produced upon autoxidation and an equalmolar mixture of conjugated 9- and
13-diene hydroperoxides is generated. The two hydroperoxide products undergo geometric
isomerization and hence are found in both the cis, trans and the trans, trans forms, as shown
in Figure 4-6.
Linolenate
Linolenate contains two 1, 4-pentadiene structures and their autoxidation products are a
mixture of 9-, 12-, 13-, and 16-hydroperoxides (Figure 4-7).
OOH CHO
H2
R C C C CHO R C C C CHO CH2 RCHO
H H H H H
CHO
C5H11 O C5H11
3C5H11CHO
O O
C5H11
Figure 4-9. Tripentyltrioxane formation by polymerization of three hexanals.
124 Shengrong Shen, Dongfeng Wang and Undurti N. Das
Each of the four hydroperoxides has multiple geometric isomers with the conjugated
diene system in the cis, trans or the trans, trans configuration, but the unconjugated double
bond is always cis. Linolenate autoxidation results in more 9- and 16-hydroperoxides than the
12- and 13-isomers, because oxygen prefers C9 and C16 and the 12- and 13-hydroperoxides
are decomposed rapidly. The 12- and 13-hydroperoxides can form six-membered peroxide
hydroperoxide via 1,4-cyclization or prostaglandin-like endoperoxides via 1,3-cyclization.
The quantity, location, and geometrical configuration of double bonds in fatty acid
components significantly affect lipid autoxidation. Lipids containing more double bonds are
oxidized faster than those with less double bonds. For example, the relative oxidation rates of
arachidonic acid, linolenic acid, linoleic acid, and oleic acid are 40, 20, 10, and 1 respectively.
The cis fatty acids are more susceptible to oxidation than the trans isomers. Conjugated
double bonds are oxidized more easily than unconjugated double bonds. Saturated fatty acids
are much more resistant to oxidation than unsaturated fatty acids. Compared with
triacylglycerols, free fatty acids are oxidized more rapidly and the autoxidation rate of lipids
increases when the free fatty acid content exceeds 0.5%. Random distribution of fatty acids in
lipids decreases the autoxidation rate.
Temperature
High temperature accelerates lipids autoxidation, though high temperature decreases the
solubility of oxygen. This is because the release of free fatty acids and the decomposition of
hydroperoxides are enhanced in high temperatures.
Lipids 125
Oxygen concentration
The autoxidation of lipids is not affected by oxygen level in the case of sufficient partial
pressure of oxygen. However, when the partial pressure of oxygen is low, the lipid
autoxidation rate is proportional to the partial pressure of oxygen.
Surface area
The lipid autoxidation rate is positively correlated with the area of the interface in contact
with air. In the case of a large surface area to volume ratio, the decrease of oxygen partial
pressure exerts no significant effect on oxidation rate. In O/W emulsions, the autoxidation
rate is determined by the diffusion of oxygen to the oil phase.
126 Shengrong Shen, Dongfeng Wang and Undurti N. Das
Water activity
Lipids are oxidized very rapidly in dried foods with aw less than 0.1. When aw is
increased, lipid autoxidation rate decreases dramatically. When the aw reaches 0.3, lipids are
oxidized in the minimum rate. This is because water reduces the catalytic activity of metals,
quenches free radicals, enhances non-enzymatic browning (producing antioxidant
compounds), and prevents the contact between foods and oxygen. When aw increases in the
range 0.3~0.7, the water solubility of oxygen and the fluidity of catalysts increase and more
reaction sites on substrates are exposed, leading to accelerated oxidation. When the aw further
increases, the lipid oxidation rate is reduced again due to diluted oxygen and catalyst
concentrations.
Auxiliary oxidants
Some divalent or polyvalent transit metals with appropriate redox potentials, such as Co,
Cu, Fe, Mn, and Ni, are effective auxiliary oxidants. These metals can shorten the initiation
period and accelerate lipid oxidation in concentrations as low as 0.1 mg/kg.
Visible light, UV light and high-energy radiation can initiate the formation of free
radicals and decompose hydroperoxides, thus stimulating lipid oxidation. Hence, lipids or
lipid-containing foods should be stored in dark place or packed with opaque materials.
Special attention should be paid to this issue in the radiation sterilization of foods.
Antioxidants
Antioxidants can delay and retard the autoxidation of lipids. The effects of antioxidants
on lipid oxidation are detailed in Section 3.2.7.
Singlet oxygen does not show obvious specificity to substrate structure and can react with
any double bonds in unsaturated fatty acids. The rate of photosensitized oxidation is
proportional to the number of double bonds and is not affected by their locations. This
property is evidenced by the rate constants of the reactions of singlet oxygen with oleic acid,
linoleic acid, linolenic acid, and arachidonic acid, which are 0.74 × 105 mol-1 · S-1 · L, 1.3 ×
105 mol-1 · S-1 · L, 1.9 × 105 mol-1 · S-1 · L, and 2.4 × 105 mol-1 · S-1 · L respectively. In the
case of triplet oxygen, it is much less active and the rate constant of the reaction with linoleic
acid is only 89 mol-1 · S-1 · L, which is 1450 times lower than that of singlet oxygen. Hence,
the oxidation initiated by singlet oxygen predominates in the oxidation of unsaturated fatty
acids.
Based on action mechanism, antioxidants are divided into free radical scavengers, singlet
oxygen quenchers, hydroperoxide decomposers, enzyme inhibitors, and antioxidant
synergists.
Free radical scavengers are either hydrogen or electron donors. Hydrogen donors, such as
phenolic antioxidants, can convert free radicals to their more stable forms by supplying an H·
radical. Because the resultant free radical cannot initiate a new free radical reaction, the chain
reaction is terminated as a result. Antioxidants of the electron donor type exert their functions
in the similar mechanism.
Singlet oxygen quenchers such as vitamin E react with singlet oxygen and convert it to
less active ground state oxygen and the quenchers themselves are transformed to the excited
state, which release the energy and return to the ground state immediately.
Hydroperoxide decomposers inhibit lipid oxidation by converting hydroperoxides
generated in chain reactions to non-active compounds.
Superoxide dismutases catalyze the formation of ground state oxygen and peroxide from
superoxides. The produced peroxide is then hydrolyzed to water and ground state oxygen by
catalase.
Antioxidant synergists are used together with antioxidants and can enhance the
antioxidant capability of antioxidants. Citric acid, fumaric acid, amino acids, vitamin C and
its esters, tartaric acid, and phospholipids are common antioxidant synergists. Synergists
reduce the catalytic activities of metal ions as well by complexing with them. Besides, some
synergists act by reducing the intermediate free radicals generated by antioxidants.
Common antioxidants
R1 R1
R3 R3
+
R4 R4
R2 R2
Thermal polymerization occurs either between different molecules (Figure 4-15) or inside
the same molecule (Figure 4-16).
In oxidative thermal polymerization, homolysis occurs in the α-carbon of a double bond
and the resultant free radicals react with each other to produce non-cyclic dimmers or add to a
double bond to yield cyclic or non-cyclic compounds.
The thermal polymerization of lipids deteriorates the quality of foods and adversely
affects food nutrition and safety. However, these reactions are desired in some cases. For
example, thermal polymerization contributes to the formation of special flavors in fried foods.
3.4.1. Refining
Oils extracted from the tissues of plants and animals by compression, organic solvent
extraction, and cooking contain free fatty acids, phospholipids, sugars, proteins, water,
pigments, and many other impurities. These impurities adversely affect the color, flavor, and
stability of lipids and some compounds, such as aflatoxin and gossypol, threaten the health of
consumers. Hence, the refinement process is required to remove these impurities.
Degumming
Phospholipids are removed in this step. Phospholipids are soluble in oils with low water
content. When the water content increases, phospholipids are hydrated and precipitated from
Lipids 131
oil. In degumming, oils are added with 2%-3% water or vapor and then agitated. The water
phase is then separated by settling or centrifugation. Carbohydrates and proteins are also
removed in this step.
Neutralization
To remove free fatty acids and part phospholipids and pigments, NaOH solutions of
appropriate concentrations are added to heated oils. The resultant foots or soapstock is
separated and used for making soap.
Gossypol and aflatoxin are also removed or destroyed in neutralization.
Bleaching
Chlorophyll, lutein, carotene, and other pigments affect the appearance of oil and
decrease the stability against oxidation. These coloring materials can be removed by
absorbents, such as floridin, emathlite, and active carbon. Other impurities, such as
phospholipids, soaps, and some oxidation products are also absorbed by the absorbents. The
absorbents are then separated by filtration.
Deodorization
The off-flavors of lipids are caused by the volatile compounds generated in lipid
oxidation. These compounds can be removed by distillation in reduced pressure. Some
nonvolatile off-flavor compounds are also destroyed by water steam and are then distilled
away.
Table 4-3. Content changes of harmful substances in rapeseed oil during refining(μg/kg)
The quality of oils is obviously improved after refining. Table 4-3 lists the removal of
various harmful substances in rapeseed oil during refining. It should be noted that some
useful components, such as fat-soluble vitamins and natural antioxidants are lost during
refining. Hence, additional antioxidants are often added to refined oils to improve the
antioxidant capacity.
3.4.2. Hydrogenation
Hydrogenation is the addition of hydrogen to the double bonds of unsaturated fatty acids.
Due to the insufficient supply of natural solid fat, liquid oils are hydrogenated to produce
semisolid fats. Hydrogenated fats have gained wide applications in the production of
margarine and shortening oil.
132 Shengrong Shen, Dongfeng Wang and Undurti N. Das
Reaction rate constants can be calculated from the starting and ending fatty acid
compositions and the hydrogenation time. Selective hydrogenation reduces the formation of
fully saturated glycerides, avoids excessive hardening of fats, and increases fat stability by
decreasing the content of linoleic acid. However, selective hydrogenation yields undesired
amount of trans isomers that cannot be absorbed by human body.
As shown in Table 4-4, both catalyst species and operating conditions affect the
hydrogenation selectivity.
3.4.3. Interesterification
The distribution pattern of fatty acids in lipids markedly affects the properties of lipids.
Because these properties affect the application of lipids in industries, interesterification has
been performed to improve lipid performance. Interesterification changes the distribution
pattern of fatty acid in triacylglycerols and is thus of industrial importance. Both intra-
(Figure 4-18) and inter-molecular interesterification (Figure 4-19) can occur, depending on
the composition and structure of triglycerides.
Interesterification can be accomplished by heating lipids in high temperatures for a long
period. In the presence of catalyst, interesterification occurs at lower temperatures in a short
period (50°C, 30min). Alkali metals and alkylated alkali metal are effective low-temperature
catalysts and sodium methoxide is the most common one. The dosage of catalyst is generally
about 0.1% of lipids.
R1 R2 R1
R2 R1 R3
R3 R3 R2
R1 R2 R1 R2
R1 + R2 R2 + R1
R1 R2 R1 R2
R1 R2
R1 + R2
R2 R1
Excessive catalyst leads to more lipid loss due to the formation of soap and methyl esters.
Impurities, such as free fatty acids and peroxides, can react with sodium methoxide and
these impurities must be present in low levels in interesterification. Besides, sodium
methoxide can react with water and lost the catalytic activity. Hence, interesterification
reactions can be terminated by adding water.
134 Shengrong Shen, Dongfeng Wang and Undurti N. Das
REFERENCES
[1] Hilditch, TP; Williams, PN. The Chemical Constitution of Natural Fats, 4th edition.
London: Chapman and Hall, 1964.
[2] Kartha, ARS. The glyceride structure of natural fats. II. The rule of glyceride type
distribution of natural fats. Journal of the American Oil Chemists' Society, 1953, 30,
326–329.
[3] Fennema, OR. Food Chemistry. 3rd edition. New York: Marcel Dekker; 1996.
[4] Chan, HW; Levett, G. Autoxidation of methyl linoleate: Analysis of methyl
hydroxylinoleate isomers by high performance liquid chromatography. Lipids, 1977,
12, 837-840.
[5] Chan, HW; Levett, G. Autoxidation of methyl linoleate: Separation and analysis of
isomeric mixtures of methyl linoleate hydroperoxides and methyl hydroxylinoleates.
Lipids, 1977, 12: 99-104.
[6] Frankel, EN. Autoxidation in Fatty Acids. Journal of the American Oil Chemists'
Society, 1979, 353-390.
[7] Sreenivasan, B. Interesterification of fats. Journal of the American Oil Chemists'
Society, 1978, 796–805.
In: Food Chemistry ISBN: 978-1-61942-125-7
Editors: D.Wang, H. Lin, J. Kan et al. © 2012 Nova Science Publishers, Inc.
Chapter 5
PROTEINS
ABSTRACT
Protein is one of the most important components in foods. Most proteins are
constituted with 20 kinds of amino acids that are linked through peptide linkages. The
combination of these amino acids leads to the occurrence of substantial amount of
proteins with different structures and functions. Theoretically, all proteins produced by
organisms can be utilized by human body. However, only proteins that are readily
digestible, non-toxic and nutritious with specific functions are used in diets. This chapter
briefly describes the properties and structures of amino acid components and proteins and
highlights the properties of important dietary protein sources. Denaturation is an
important change in food processing. The mechanism of denaturation, properties of
denatured proteins and factors causing denaturation are also included in this chapter. In
addition to the nutrition attribute, some functional properties, including emulsifying,
foaming, gelling, and viscosity, also contribute to its wide applications in the food
industry. These functional properties are described in detail in this chapter. Proteins
undergo various changes during processing. These changes might greatly affect the
quality of foods. This chapter also emphasize on the changes of proteins occurred in
various processing techniques.
138 Hong Lin, Lisha Wu and Shuhui Wang
The acylated products are more stable against various reagents and can be removed by
many methods. Hence, carbobenzoxy chloride has been widely used in protein synthesis for
amine group protection.
The azide compound can react with another amino acid ester by condensation to produce
a dipeptide:
140 Hong Lin, Lisha Wu and Shuhui Wang
1.3.1. Bitterness
Amino acids contain multiple functional groups and can act with various taste receptors
to exhibit different tastes. Sweet amino acids are primarily found among amino acids of the D
form, while the tastes of L-series amino acids are significantly affected by their side chains.
When the side chain is small, the sweet taste predominates. For example, glycine (Gly),
alanine (Ala), proline (Pro), hydroxyproline (Hpr), homocysteine (Hcys), serine (Ser),
threonine (Thr), asparagine (Asn), and glutamic acid methyl ester (Glu-OMe) contain small
side chains and taste sweet. When the side chain contains more than three carbons, such as
leucine (Leu), isoleucine (Ile), norleucine (Nle), phenylalanine (Phe), tyrosine (Tyr),
tryptophane (Trp), histone (His), lysine (Lys), arginine (Arg), the bitter taste predominates. If
the side chain is of moderate size, the amino acids taste both sweet and sweet, such as valine
(Val) and ornithine (Orn). The sensory property of amino acids also depends on the
hydrophobicity of side chains. If the side chain is only slightly hydrophobic, the amino acid
tastes slightly sweet without bitterness, such as glutamin (Gln), cysteine (Cys), and
methionine. If the side chain is acidic, the amino acids taste sour, such as aspartic acid (Asp)
and glutamic acid (Glu). Table 5-1 lists the relationship between the sensory properties and
side chain structure of amino acids.
Table 5-1. Relationship between the side chain structure and taste of amino acids
(1) Neutral peptides consisting of type I and V amino acids and those containing only
type II amino acids exhibit light tastes.
(2) The sodium salts of oligopeptides consisting of only type I amino acids or type I and
type II amino acids taste fresh, such as Glu-Glu, Glu-Asp, Glu-Ser, and Glu-Thr.
(3) The combination of type III amino acids with type I amino acids remove the bitter
taste, but remain the sour taste.
(4) Peptides composed of type III, IV, or V amino acids only or their combinations are
bitter.
(5) Peptide formation, carboxyl group esterification, or diketopiperazine formation by
coupling of type IV and V amino acids enhances the bitter taste.
(6) Peptides with type IV and V amino acids locating at the C terminal are 3~5 times
bitterer than those with the amino acids locating at the N terminal or the middle of the
peptides.
(7) Type II amino acids (especially Gly) locating at either terminals or cyclized increase
the bitterness.
All peptides contain AH polar groups. However, because peptides differ markedly in
molecular weight and nature of hydrophobic groups, they have different bitterness receptor
binding capabilities. The bitterness intensity of peptides can be predicated by calculating the
average hydrophobicity of side chains, which is related to the total hydrophobicity of
nonpolar amino acids. Table 5-2 lists the hydrophobicity of various amino acids. The average
hydrophobicity of a peptide can be calculated by using the following formula:
In which, ⊿G is the free energy change of the side chains of amino acids and n is the
number of resides in the peptide.
Peptides with Q greater than 6.85kJ/mol are bitter and those with Q less than 5.43kJ/mol
are not bitter. No rules have been found for the taste of peptides with Q in the range
5.43~6.85kJ/mol. However, exceptions have been found. For example, all peptides with
molecular weight more than 6000 taste light despite of the Q value. If Gly is attached to one
or both ends of a peptide, the peptide tastes bitter even though Q is less than 5.43kJ/mol. This
is possible due to the less steric hindrance of Gly that facilitates the contact with bitterness
receptors. For this reason, it has been proposed to exclude Gly from Q calculation. Arg-Arg,
Lys-Ala, Val-Ah, Arg-Gly-Pro, and Ser-Lys-Gly-Leu, are also exceptions to the rule. The Q
values of these peptides are less than 5.43kJ/mol, but they taste bitter.
Besides, the bitterness intensity of peptides with similar Q values might differ
significantly. The bitterness intensity of Gly-Gly-Gly-Leu is greater than its three positional
isomers and that of Leu polymers are Leu-Leu-Leu-Leu, Leu-Leu-Leu, Leu-Leu, and Leu in
decreasing order. In the case of bitter peptides in cheese, the bitter taste disappears after the
Gln at the N terminal is cyclized, though the Q value is not changed. These inconsistencies
indicate that the bitterness intensity of peptides is also affected by their molecular weights and
higher structures in addition to Q values.
142 Hong Lin, Lisha Wu and Shuhui Wang
Only dissociated glutamic acid salts can enhance flavor, of which, monosodium
glutamate (MSG) has the purest taste. Glutamic acid derivates that cannot dissociate
have no the flavor enhancing capability.
5‘-Inosine monophosphate (5‘-IMP), 5‘-guanosine monophosphate (5‘-GMP), and
5‘-xanthine monophosphate (5‘-XMP) are good flavor enhancers, but adenylate has
no the flavor enhancing ability.
L-Cys, sodium salt of thiosulfonic acid, homocysteine, L-Asp, L-aminoadipic acid,
and succinic acid, display flavor enhancing abilities similar to L-MSG.
Proteins 143
Many fruit acids, such as malic acid, tartaric acid, and citric acid, enhance the taste of
foods. The combination of anyone of the acids with lactic acid can improve the odor
of soybean product. Besides, citric acid juice enhances the taste of strawberry.
Fumaric acid and maleic acid can suppress the unpleasant odor of garlic.
Glutathione enhances the taste of meat broth. Polyphosphates improves the taste of
chicken meat and cheese.
The diamine salts of dicarboxylic acids with carbon atom number ranging from 3 to
10 can be used as the substitutes of table salt.
It is proposed that all flavor enhancers show a common structure O-(C)n-O, in which, n
ranges from 3 to 9. In another word, the compounds must contain an alkyl chain with 3~9
carbons and the two ends must be negative charged. Compounds with 4~6 carbons have the
highest enhancing ability. The alkyl chain can be straight, branched, or cyclic and the carbon
atoms can be replaced by O, N, S, and P. The negative charges on the two ends of the
molecule are crucial for the enhancing ability. If the carboxylic acid group is esterified,
amidated, or converted to lactone or lactam upon heating, the enhancing ability is obviously
reduced. The negative charge of an end can be replaced by a negative dipole. For example,
the enhancing abilities of tricholomic acid and ibotenic acid are 5~30 times higher than that
of L-MSG.
For economic and safety reasons, only Glu- and nucleotide-type flavor enhancers have
gained commercial applications.
In addition, MSG is racemized under alkaline solutions when heated and loses flavor
enhancing ability. Hence, MSG should be added after dishes or soups are cooked.
2. STRUCTURE OF PROTEIN
2.1. Primary Structure
Primary structure is the sequence of amino acid residues in proteins and is decided by
the genetic codes in genes. The primary structure decides the higher structures of proteins. All
proteins are composed of 20 amino acids and the combination of these components leads to
the occurrence of tremendous number of proteins with different spatial structures and
biological functions.
The polypeptide chains of proteins occur as folded and twisted conformation under
suitable conditions and these conformations determine the biological and physicochemical
properties of the molecules in addition to their amino acid sequences.
(1) Multiple peptide bond planes rotate through the α-carbon atom spin, twisting each
other into a tight solid right-handed helix.
(2) Each helical rotation involves 3.6 amino acid residues. Each residue extends the axial
length by 1.5 Å and the angle of rotation per residue is 100°.
(3) α-Helices are stabilized by hydrogen bonding. In this structure, each backbone N-H
group is hydrogen bonded to the C=O group of the fourth preceding residue in the same
chain.
(4) The side chains of amino acid residues are located on the outer of the helix and their
shape, size, and charge affect helix formation. α-Helix is often not found in areas with
abundant acidic or basic amino acids due to charge repulsion or areas consisting more amino
acids with large side chains, such as tryptophan and isoleucin. Proline is generally not
146 Hong Lin, Lisha Wu and Shuhui Wang
involved in α-helix formation, because it cannot rotate or hydrogen bond with other amino
acids readily. The presence of glycine affects helix stability, because its side chain (H)
occupies the minimum space.
(1) The β-sheet structure is an extended structure. Amino acid residues involved are
arranged in a zigzag pattern and their residues are located on the upside or downside of the
pleat plane. The angle between adjacent peptide bond planes is 110°.
(2) The conformation is stabilized by hydrogen bonding of C=O and –NH between
adjacent strands of a peptide.
(3) When adjacent strands run in the same direction, the peptide chains are parallel.
When the chains run in opposite directions, a planar, antiparallel sheet structure is stabilized.
Both parallel and antiparallel sheets can occur in one peptide.
(4) In parallel β-sheet, the distance between any two adjacent residues is 0.65 nm and
that in anti-parallel β-sheet is 0.7 nm.
a
electrovalent bond;
b
hydrogen bond;
c
hydrophobic bond;
d
Vander Wasls force;
e
disulfide bond.
Figure 5-3 shows the combination pattern of the subunits of hemoglobin. The structures
of subunits in a protein may be the same or different. For example, the coat protein of tobacco
streak virus consists of 2200 identical subunits and normal hemoglobin A is a tetramer
containing two α subunits and two β subunits. The smallest subset of different subunits of a
protein is defined as the protomer. For example, the aspartate carbamyl transferase contains
six protomers and each protomer consists of one catalytic subunit and one regulatory subunit.
Some proteins can further aggregate into polymers and each repeating unit is called a
monomer. According to the number of monomers, protein polymers can be divided into
dimer, trimer, oligomer and multimer. For example, insulin might occur as dimer and
hexamer in human body.
3. CLASSIFICATION OF PROTEINS
3.1. Classification by Amino Acid Composition and Quantity
According to the composition of amino acids and their contents in proteins, proteins are
divided into complete, partially complete, and incomplete proteins.
3.2.1. Albumin
Albumin refers to any protein that is soluble in water and moderately soluble in
concentrated salt concentrations. Albumin can be precipitated by saturated ammonium
sulphate. Albumin occurs widely in nature. Leucosin in wheat seeds, blood plasma proteinand
ovalbumin in eggs are examples of albumin.
3.2.2. Globulin
Globulins are insoluble in water but soluble in diluted salt, acid, or alkaline solutions and
can be precipitated by half-saturated ammonium sulphate. Globulins have important
biological functions. Legumin in soybean seeds, seroglobulin in blood, myoglobulin in
muscle, and immunoglobulins are of this category.
3.2.3. Histone
Histones are highly alkaline proteins and are soluble in water or diluted acid solutions.
Histones contain rich quantity of Arg and Lys and are the structural components of
chromosomes.
3.2.4. Protamine
Protamines are small, arginine-rich proteins and are soluble in water and diluted acid
solutions. Protamines contain abundant alkaline amino acids and lack Trp and Tyr. The
proteins are found in mature sperm cells and replace histones late in chromosome the haploid
phase of spermatogenesis.
3.2.5. Prolamin
Prolamins are a group of plant storage proteins with high proline contents and found in
the seeds of cereal grains. They are characterized by a high glutamine and proline content and
are generally soluble only in 70%~80% ethanol solutions.
150 Hong Lin, Lisha Wu and Shuhui Wang
3.2.6. Gluten
Glutens are contained in plant seeds, such as barley and rye. Proteins of this category are
insoluble in water or diluted salt solutions but soluble in diluted acid and alkaline solutions.
3.2.7. Albuminoid
Proteins of this category are not soluble in water or salt, diluted acid and diluted alkaline
solutions and occur mainly in skins, hairs, and nails. The roles of such proteins include
protection and support, forming connective tissue, tendons, bone matrices, and muscle fiber.
Keratin, collagen, elastin, and fibroin are all albuminoids.
3.3.1. Nucleoprotein
A nucleoprotein is any protein which is structurally associated with nucleic acid.
Deoxyribonucleoprotein, ribosome, and tobacco mosaic virus are examples of nucleoprotein.
3.3.2. Lipoprotein
A lipoprotein is a complex molecule consisting of both protein and lipid. The lipid might
be phospholipids, sterols, or neutral fats. Many transporters in blood and lipovitellin are
lipoproteins.
3.3.4. Phosphoprotein
In phosphoproteins, phosphoric acid is connected to the Ser or Thr resides of proteins
through ester bonds. Casein and pepsin belong to this category.
3.3.5. Metalloprotein
Metalloproteins refer to any proteins that contain metal ion cofactors. Many important
enzymes, transport proteins and storage proteins are metalloproteins. For example,
hemoglobin contains iron, chlorophyl contains magnesium, and hemocyanin contains copper.
3.3.6. Flavoprotein
Flavoproteins are proteins that contain a nucleic acid derivate of riboflavin. Succinic
acid dehydrogenase and d-amino acid oxidase are examples of flavoprotein.
Proteins 151
4. PROTEIN DENATURATION
4.1. Definition of Denaturation
When a protein is exposed to such physical stresses as heating and ultraviolet irradiation
or such chemical stresses as strong acid and base, its properties are changed, such as decrease
of solubility and loss of activity, but the primary structure remains unaltered. This process is
termed denaturation. Denaturation is an extremely important property of proteins and
markedly affects food processing.
The denaturation theory was first proposed by a Chinese biochemist in 1931. It was
believed that denaturation is the transfer of natural proteins molecules from ordered and
compact states to disordered and loose states because of environmental stresses. The compact
structure of natural proteins is maintained by various secondary bonds. These secondary
bonds are easily interrupted by physical and chemical factors, which induce the destruction or
alternation of protein conformation. Hence, protein denaturation is actually caused by the
changes of secondary, tertiary, and quaternary structures of proteins. The destruction of
spatial conformation of proteins leads to reduced solubility, aggregation, irreversible gelation,
increased sensitivity to protease hydrolysis, and loss of physiological activities.
A protein denatured in mild conditions is present in a relaxed conformation. After the
denaturation factor is removed, the protein can restore to its natural conformation. Hence, this
denaturation process is reversible. For example, when ribonuclease is treated with 8 mol/L
urea and mercaptoethanol, the disulfide bonds in the molecule is reduced and the enzyme
loses its activity due to changed conformation. However, after the regents are removed by
dialysis, the denatured protein is automatically oxidized and returns to its natural
conformation (Figure 5-4).
Trypsin and hemoglobin also undergo reversible denaturation. After trypsin is denatured
by heating at 70~100°C for a short time in an acidic solution, the enzyme loses its catalytic
activity. When the solution is cooled down in a proper rate, trypsin can recover all its
properties.
Haemoglobin can be denatured by low-concentration sodium salicylate. After sodium
salicylate is removed, the protein can restore to its natural conformation. However, the
denaturation of most proteins is irreversible. For example, egg protein is gelated when
cooking and this process is irreversible; soybean protein is irreversibly denatured in tofu
production.
The reversibility of protein denaturation is related to the denaturation agent species,
protein property and the degree of protein conformation destruction. Generally, in reversible
denaturation, the tertiary and quaternary structures of proteins are destroyed, but secondary
structures remain intact. In contrast, in the irreversible denaturation, the secondary, tertiary
and quaternary structures are all interrupted.
The physical, chemical and biological properties of proteins undergo obvious changes
after denaturation.
(1) Hydrophobic groups originally located inside molecules get exposed on molecule
surface and the hydration layer is destroyed. Hence, the solubility of denatured proteins
decreases significantly.
(2) Denatured proteins cannot crystallize as original ones.
(3) The spatial structure of denatured proteins is in random shape. The friction between
molecules increases and the fluidity decreases. Hence, denatured proteins have reduced
diffusion coefficient and their solutions have lower fluidity.
(4) The optical activity of denatured protein changes and the isoelectric point increases
slightly.
(5) Denatured proteins are more susceptible to enzymatic hydrolysis. For example,
natural haemoglobin cannot be hydrolyzed by trypsin, but denatured haemoglobin can be
hydrolyzed easily. This is why cooked foods are digested and absorbed more easily.
(6) Denatured proteins have more exposed side chains, such as –SH and –OH. Hence,
the degree of protein denaturation can be estimated by the reaction between these groups and
specific reagents.
(7) The bioactivities of denatured proteins are completely or partially destroyed. For
example, denatured enzymes lose their catalytic activities; denatured hemoglobin can no
longer transport oxygen; and denatured antigens lose their immunological competences.
4.4.1. Heat
Heating is the most common physical factor of protein denaturation. The temperature
required for detectable denaturation varies with the nature of protein and is also affected by
Proteins 153
protein purity and pH. The denaturation of most proteins can be detected in the temperature
range 45~50°C and the process is accelerated when the temperature is elevated to 55°C.
Denaturation occurring at lower temperatures involves only the disruption of non-covalent
bonds and proteins become unfolded. For example, natural serum albumin is of the oval shape
with the axial ratio of 3:1, while the axial ratio of denatured serum albumin increases to 5:5.
Such denaturation induced by short-time exposure to low temperatures is reversible. When
the temperature increases to 70~80°C, disulfide bonds are broken. Hence, protein
denaturation occurring in long-time high-temperature treatment is irreversible.
Heat treatment leads to protein denaturation by disrupting hydrogen bonding and many
other secondary bonds that maintain protein conformation. It is estimated that the rate of
denaturation increases by up to 600 folds when the temperature increases by 10°C in the
denaturation temperature range.
The sensitivity of a protein to thermal denaturation depends on multiple factors, such as
protein property, protein concentration, water activity, pH, ionic strength and ion species.
Proteins, enzymes, and microbes are more resistant to thermal denaturation in water-
containing conditions than in dry conditions. Besides, high concentration of denatured protein
hinders the renaturation process.
The temperature used in the thermal processing of foods is generally around 100°C and
the central temperature of materials often exceeds 70°C. Hence, most proteins are denatured
and pathogens are inactivated during thermal processing of foods.
4.4.2. Radiation
The impact of radiation on proteins depends on the energy and wavelength of the rays
used. Ultraviolet radiation can be absorbed by aromatic amino acid residues (tryptophan,
tyrosine and phenylalanine) and can change the conformation of proteins. Radiation by high-
energy rays disrupts disulfide bonds. γ radiation and other ionizing radiation can also make
conformation changes, amino acid oxidization, covalent bond disruption, ionization, proteins
free radical formation as well as polymerization.
a)
b)
c)
The interfacial properties of proteins are important for their applications in various food
systems. For example, proteins absorbed at interfaces are beneficial for the formation and
stabilization of emulsions and foams. To keep the natural conformation and functional
properties of proteins, dispersion systems, such as foams and emulsions, should be avoided
during food processing and separation.
4.4.4. pH
It is irreversible that protein denaturation occurs in mild and extreme pH conditions.
Extreme pH changes the ionization of some groups in polypeptide chains and disrupts the
hydrogen bonding required for maintaining conformation and the electrostatic interaction
between differently charged groups. If the pH is lowered far below the isoelectric point (pI) or
elevated above the pI, the protein will contain only positive or negative charges. The charges
will repel each other and prevent the protein from aggregation. In areas with large charge
density, the intramolecular repulsion may be great enough to cause unfolding of the protein.
In some cases the unfolding may be extensive enough to expose hydrophobic groups and
Proteins 155
This same reaction is used in reverse in cases of acute heavy metal poisoning. In such a
situation, a person may have swallowed a significant quantity of a heavy metal salt. As an
antidote, a protein such as milk or egg whites may be administered to precipitate the
poisonous salt. Then an emetic is given to induce vomiting so that the precipitated metal
protein is discharged from the body.
Thermal treatment in combination with high pressure improves the tenderness of beef
and enhances the sterilization effect. Besides, the combined treatment changes the
composition of beef muscles and affects its functional properties, such as color, texture, fat
oxidation and flavor, which are related to protein denaturation. Differential scanning
calorimetry(DSC) is an effective tool for studying the structural and thermodynamic
properties of natural polymers. DSC has been used in the investigation of denaturation and
resultant texture changes of muscle proteins. Figure 5-7(a) Figure 3 shows the thermograms
of intact beef muscle after treatment at pressures from 0.1 to 800MPa at 20°C for 20min. The
three major endothermic transitions seen have been attributed to myosin, collagen and actin
and the peak maxima in this study are seen at 54.6°C (myosin), 67.1°C (collagen) and 77.3°C
(actin). Treatment at 200MPa decreased the myosin and actin peaks and at 400MPa and
higher, the actin peak is not seen.
Figure 5-7(b) shows the thermograms when the samples are treated at 0.1-800MPa at
40°C for 20min. At ambient pressure about 43% of the myosin, is denatured but there is no
obvious effect on collagen and actin. At 200MPa the myosin and collagen are merged into
one broad peak with an onset temperature of 50.1°C. At 400MPa, the actin peak is not seen.
When the pressure is increased to 600 and 800MPa, the new myosin peak and that of collagen
are still discernible.
Proteins 157
a) Peak 1 Peak 3
Peak 2
0.2 mw
0.1 MP2
Peak N
200 MP2
600 MP2
800 MP2
Rescan
50 55 60 65 70 75 80 85
Temperature (˚C)
b)
40 45
Figure 5-7. Thermograms of beef muscle, heated at 10 ˚C min−1 after treatment at different pressures in
air for 20min at 20°C and 40°C [7].
Although the combination of high pressure and thermal treatment has complex effect on
protein properties, it has wide applications in food processing:
The sensory properties of foods result from the complex interaction between various
food ingredients. For example, the flavor, texture, color and shape of a cake is contributed by
the combination of the thermal gelation capacity, foaming capacity, water holding capacity,
emulsification, elasticity and browning reaction of the materials used. Hence, proteins as food
materials must have multiple functional properties (Table 5-7). Animal proteins, such as those
derived from milk, egg and meat, are mixture of multiple protein components and thus have
diverse physical and chemical properties. For example, egg white has good water holding,
gelling, conglutination, emulsification, foaming, and thermal coagulation capabilities and
these properties are contributed by ovalbumin, conalbumin, ovomucin, lysozyme and other
albumins and their interactions. Plant proteins, such as those from soybean and oilseeds, are
also mixtures of multiple protein components.
However, these proteins have only limited functional properties and are only used in
common foods in less quantity.
Bakery products, desserts, beer, milk, ice cream, butter, chopped meat, and other foods
containing emulsions or foams are dispersion systems and amphiphilic components must be
present to stabilize the systems. Proteins are amphiphilic molecules and can spontaneously
Proteins 159
migrate to the air-water or oil-water interface and form highly viscoelastic film at the
interface. The interface system of proteins is more stable than that formed by surfactants.
Table 5-7. Functional properties of proteins required for various food [9]
the interface occur in the train conformation, the segments suspended in the aqueous phase
are arranged as loops, while the peptide chains with the N- and C- terminal in the aqueous
phase are present mainly in the tail conformation. Of the three conformations, the train
conformation occurs in higher probability than the other two conformations and exhibits
lower interfacial intension.
)NTERFACE
-ODERATE PROBABILITY 3TRONG PROBABILITY
.O ADSORPTION OF ADSORPTION OF ADSORPTION
(YDROPHILIC .ONPOLAR SURFACE
SURFACE
!QUEOUS PHASE
(YDROPHOBIC CORE
Figure 5-8. Probability of protein adsorption to the interface as a function of hydrophobic domain
number [11].
1IBTF
USBJO
*OUFSGBDF
UBJM
MPPQ
1IBTF
The stability of a protein at the interface determines the mechanical strength of the film
formed at the interface and the film strength is also affected by the electrostatic attraction, and
hydrogen bonding, and hydrophobic interaction between molecules. Disulfide bonds increase
the film viscoelasticity. When the concentration of protein in the interfacial film reaches
about 20%~25% (W/V), gelation occurs. To maintain the stability viscoelasticity of the gelled
film, the secondary interactions involved must be in balance. If the hydrophobic interaction is
too strong, the protein flocculates, aggregates, and even precipitates. If the electrostatic
repulsion far exceeds electrostatic attraction, a thick cohesive membrane is not formed
readily.
The emulsifying capability of a protein can be evaluated by droplet size and distribution,
emulsifying activity, emulsion capacity, and emulsion stability.
Emulsifying activity refers to the total interfacial area of an emulsion. The emusifying
activity of a protein is often presented as the emulsifying activity index (EAI), namely the
interfacial area created per unit mass of protein. The EAI of a protein can be determined
easily in the turbidimetric method. The turbidity of an emulsion can be calculated by the
following equation:
Emulsion capacity (EC) is the volume (ml) of oil that can be emulsified by per gram of
protein before phase inversion (a change from oil-in-water emulsion to water-in-oil) occurs.
In the determination of TC, oil or melted fat are added at a constant rate and temperature to an
aqueous protein solution that is continuously agitated. Phase inversion is detected by an
abrupt change in viscosity or color (usually a dye is added to the oil).
EMULSIFYING ACTIVITY INDEX %!)-G
$(
Figure 5-10. Effect of molecular weight on EAI (DH is the degree of hydrolysis) [13].
162 Hong Lin, Lisha Wu and Shuhui Wang
Note: ○ - 0.1mol/L NaCl; ● – 0.2 mol/L NaCl; ▲ – 0.5mol/L NaCl; □ – 1.0mol /L NaCl.
Figure5-11. Effect of pH and NaCl concentration on the emulsion volume of peanut protein isolate [14].
The emulsion stability (ES) is measured as the final volume of the emulsion after
centrifuging the initial volume or standing for several hours at specified conditions. It may
also be determined as the quantity of oil or cream separated from the emulsion, or the time
required for the emulsion to release a specified quantity of oil.
In most cases, the disperse phase is air or carbon dioxide and the continuous phase is
composed of two films of proteins adsorbed on the interface between a pair of air bubbles,
with a thin layer of liquid between them. The diameters of bubbles might range from 1μm to
several centimeters, depending on the surface tension and viscosity of the aqueous phase and
energy input. Evenly distributed small bubbles can impart foods with desired consistency,
exquisite texture, and softness and improve the dispersivity and flavor. The formation of
bubbles is shown in Figure 5-12.
# &
%
$
"
The pH is an important factor that affects the foaming ability and foam stability of
proteins. Generally, high solubility is a prerequisite for good foaming ability and foam
stability. However, insoluble protein granules, such as fibrillin in its isoelectric point, may
164 Hong Lin, Lisha Wu and Shuhui Wang
impart good foam stability. Some proteins give rise to small to foam volume in their
isoelectric points, but the produced foams have excellent stability, such as globulins in pH
5~5, glutelin in pH 6.5~7.5, and lactalbumin in pH 4~5. Some protein-stabilized foams are
more stable in extreme pH values, possible due to increased viscosity of involved proteins.
The foams in most foods are formed in other pH than the isoelectric points of contained
proteins.
Sugars suppress the expansion of protein-stabilized foams, but increase the foam
stability. This is because sugars can increase the viscosity of the bulk phase and reduce the
drainage of the lamella fluid. Sugars can stabilize the conformation of proteins and hinder
their adsorption and unfolding on the interface. Hence, proteins cannot produce large
interfacial area and foam volume in the presence of sugars. This is why sugars are often
added after the foam expansion has already been completed in the manufacture of meringue
and other sugar-containing foods.
Lipids in low concentrations (about 0.1%) seriously impair the foam ability of proteins.
This is because lipids are more surface-active than proteins. Lipids readily adsorb at the air-
water interface and inhibit adsorption of proteins during foam formation. Besides, lipid films
lack the cohesive and viscoelastic properties necessary to withstand the internal pressure of
the foam bubbles, the bubbles rapidly expand, then collapse during whipping. Thus, lipid-free
whey protein concentrates and isolates, soy proteins, and egg proteins without egg yolk
display better foaming properties than do lipid-contaminated preparations.
Partially denatured proteins have improved foaming abilities than their nature forms.
Moderate heat treatment can enhance the foaming ability of soybean protein (70~80°C) and
lactalbumin (40~60°C). Although moderate heat treatment increases the expansion capacity,
it decreases the foam stabilization. Excessive heat treatment might impair the foaming ability
of proteins.
To obtain enough quantity of foam, the whipping operation must last long enough in
suitable strength for sufficient unfolding and adsorption. However, excessive whipping can
reduce the expansion volume and foam stability. For example, ovalbumin is very sensitive to
excessive whipping. Whipping of ovalbumin for 6~8min can lead to coagulation-flocculation
in the air-water interface. These insoluble proteins could not be completely absorbed on the
interface and the viscosity of the formed liquid sheet cannot meet the requirement of high
stability of foams.
Most proteins contain more than one subunit. Hence, the foaming ability of a protein is
also affected by the interaction between the subunits absorbed on the interface. For example,
the excellent foaming ability of egg whit has been attributed to its protein composition.
Acidic proteins can get improved foaming ability when complexing with an alkaline protein.
No close correlation between emulsifying ability and foaming ability has been found for
protein.
Salts affect the foaming of proteins by influencing the solubility, viscosity, unfolding
and aggregation of proteins. The foaming ability and foam stability of most globular proteins,
such as bovine serum albumin, egg albumin, gluten and soy proteins increase with increasing
concentration of NaCl. This behavior is usually attributed to neutralization of charges by salt
ions. However, some proteins, such as whey proteins, exhibit the opposite effect: Both foam
ability and foam stability decrease with increasing concentration of NaCl (Table 5-10).
Bivalent cation ions, such as Ca2+ and Mg2+, in concentration 0.02~0.04mol/L could bridge
Proteins 165
with the carboxyl group of proteins to form protein films with good viscoelasticity. Hence,
the presence of these ions can increase the foam stability.
5.2. Viscoelasticity
Viscoelasticity is the property of materials that exhibit both viscous and elastic
characteristics when undergoing deformation.
Table 5-10. Effect of NaCl on the foaming ability and foam stability of whey protein
isolate [17]
Concentration of Total interfacial area (cm2/mL of Times of 50% collapse of initial area
NaCl(mol/L) foam) (second)
0.00 333 510
0.02 317 324
0.04 308 288
0.06 307 180
0.08 305 165
0.10 287 120
0.15 281 120
Wheat protein is very unique among food proteins because it can produce dough with
both viscous and elastic properties. When a mixture of wheat flour and water (about 3:1 ratio)
is kneaded, a dough with viscoelastic properties forms that is suitable for making bread and
other bakery products.
These unusual dough characteristics are mainly attributable to the proteins in wheat flour.
Wheat flour contains 20% soluble and 80% insoluble protein fractions. The soluble proteins
are primarily albumin, globulin-type enzymes and minor glycoproteins. These proteins do not
contribute to the dough-forming properties of wheat flour. The major storage protein of wheat
is gluten. Gluten is a heterogeneous mixture of proteins, mainly gliadins (soluble in
70%~90% ethanol) and glutenins (insoluble in water or ethanol, but soluble in acidic and
alkaline solutions). Gluten can entrap gas during fermentation to produce the viscoelastic
property. Besides, the starch granules, pentosan, polar and non-polar lipids, and soluble
proteins in wheat flour facilitate the formation of the viscoelastic protein network and dough
texture. Gluten is rich in Gln (more than 33% of the amino acid residues) and hydroxyl-
containing amino acids. Hence, the amino acids can form hydrogen bonding readily and this
property contributes to the water adsorption and cohesion-adhesion property of gluten. About
30% of gluten's amino acid residues are hydrophobic, and the residues contribute greatly to its
ability to form protein aggregates by hydrophobic interactions and to bind lipids and other
nonpolar substances.
Cysteine and cystine residues account for 2~3% of gluten's total amino acid residues.
During formation of the dough, these residues undergo sulfhydryl-disulfide interchange
reactions resulting in extensive polymerization of gluten proteins.
Several physical and chemical transformations occur during mixing and kneading of a
mixture of wheat flour and water. Under the applied shear and tensile forces, gluten proteins
absorb water and partially unfold. The partial unfolding of protein molecules facilitates
hydrophobic interactions and sulfhydryl-disulfide interchange reactions, which result in
166 Hong Lin, Lisha Wu and Shuhui Wang
formation of thread-like polymers. These linear polymers in turn are believed to interact with
each other, presumably via hydrogen bonding, hydrophobic associations, and disulfide cross-
linking, to form a sheet-like film capable of entrapping gas.
Because of these transformations in gluten, the resistance of the dough increases with
time until a maximum is reached, and this is followed by a decrease in resistance, indicative
of a breakdown in the network structure. The breakdown involves alignment of polymers in
the direction of shear and some scission of disulfide cross-links, which reduces the polymer
size. The time it takes to reach maximum dough strength during kneading is used as a
measure of wheat quality for bread making—a longer time indicating better quality.
The development of the viscoelastic dough is thought to be related to the extent of
sulfhydryl-disulfide interchange reactions. This is supported by the fact that when reductants,
such as cysteine, or sulfhydryl blocking agents, such as N-ethylmaleimide are added to
dough, viscoelasticity decreases greatly. On the other hand, addition of oxidizing agents, such
as iodate and bromate, increase the elasticity of the dough. This implies that wheat varieties
that are rich in SH and S-S groups might possess superior bread-making qualities, but this
relationship is unreliable. Thus, the role of sulfhydryl-disulfide interchange reactions in the
development of viscoelastic dough is poorly understood.
The strength of dough is related to the contents of glutenin and completely insoluble
residue proteins. Experiments on wheat flour supplemented with glutenins and gliadins of
different proportions indicate that glutenins determine the elasticity, cohesiveness, mixture
tolerance, extensibility, the expansion of dough and the mobility of gliadins. Suitable
proportions of the two categories of proteins are important for bread making.
High glutenins contents can increase the cohesiveness of dough and suppress the
expansion of entrapped CO2, while high gliadins contents increase the elongation and make
the gluten film fragile and permeable, leading to poor CO2 retention and bread collapse.
The different effects of glutenins and gliadins on bread-making may be related to the
differences in their structure and composition. In gluten these exist as single polypeptides
with molecular weight ranging from 30,000 to 80,000. Although gliadins contain about 2~3%
half-cystine residues, they apparently do not undergo extensive polymerization via
sulfhydryl-disulfide interchange reactions. The disulfide bonds appear to remain as
intramolecular disulfides during dough making. Dough made from isolated gliadins and
starch is viscous but not viscoelastic.
Glutenins are heterogeneous polypeptides with molecular weight ranging from 12,000 to
130,000. These are further classified into high-molecular-weight (M.W. >90,000, HMW) and
low-molecular-weight (M.W. <90,000, LMW) glutenins. In gluten, glutenin polypeptides are
present as polymers joined by disulfide cross-links, with molecular weights ranging into the
millions. Because of their ability to polymerize extensively via sulfhydryl-disulfide
interchange reactions, glutenins contribute greatly to the elasticity of dough. Therefore, an
optimum ratio of gliadins and glutenins seems to be necessary to form viscoelastic dough.
Some studies have shown a significant positive correlation between HMW glutenin content
and bread quality in some wheat varieties, but not in others. Available information indicates
that a specific pattern of disulfide crosslink association among LMW and HMW glutenins in
gluten structure may be far more important to bread quality than the amount of this protein.
For example, association/polymerization among LMW glutenins which have the similar
structure form the HMW gliadin. This type of structure contributes to viscosity of the dough,
but not to elasticity. In contrast, if LMW glutenins link to HMW glutenins via disulfide cross-
Proteins 167
links (in gluten), then this is believed to contribute to dough elasticity. It is possible that in
good-quality wheat varieties, more of the LMW glutenins may polymerize with HMW,
whereas in poor-quality wheat varieties, most of the LMW glutenins may polymerize among
themselves. These differences in associated states of glutenins in gluten of various wheat
varieties may be related to differences in their conformational properties, such as surface
hydrophobicity, and reactivity of sulfhydryl and disulfide groups.
Baking does not lead to the re-denaturation of gluten, because glutenins and gliadins
occur naturally in partially unfolded form and are further unfolded during kneading. When
heated in 70~80°C, gluten loses water and the water is absorbed by gelatinized starch
granules. Hence, gluten can maintain the softness and water content (40%~50%) of bread in
baking.
Soluble protein fractions, including albumin- and globulin-type proteins, are denatured
and coagulated during baking. This partial gelling is beneficial for the cohesion of crumbs.
Hence, supplementation of external proteins is good for bakery foods quality, such as
nutrition fortification. However, not all proteins are beneficial for gluten network formation.
For example, supplementation of wheat flour with albumin- and globulin-type proteins, such
as whey proteins and soy proteins, adversely affects the viscoelastic properties and baking
quality of the dough. These proteins decrease bread volume by interfering with formation of
the gluten network. Addition of phospholipids or other surfactants to dough counters the
adverse effects of foreign proteins on loaf volume. In this case, the surfactant/protein film
compensates for the impaired gluten film. Although this approach results in acceptable loaf
volume, the textural and sensory qualities of the bread are less desirable than normal.
5.3. Gelation
5.4. Hydration
and rehydration properties of proteins markedly affect their applications in the food industry.
Figure 5-13 illustrates the sequence of interactions occurred between dry protein and water.
Protein
Solution
disperses in
is formed
water
Figure 5-13. Sequence of the interactions between dry protein and water [10].
5.5. Solubility
It is a long process for proteins to reach their equilibrium solubility and the protein
solubility varies with the pH, ionic strength, and temperature of the environment and protein
concentration. The solubility of most proteins decreases irreversibly when heated. However,
heat treatment is unavoidable during food processing and protein denaturation might occur
during extraction and purification even in mild conditions. Hence, the nitrogen solubility
index (NSI) of soybean protein powder, concentrated soybean protein, and soybean protein
isolate vary in the range 10%~90%.
Proteins 169
The solubility of proteins is essential for determining the optimum conditions of protein
extraction, purification and separation and is an important indicator of its application range.
The degree of insolubility can be used as a measure to evaluate the denaturation and
agglutination of proteins. It is reported that proteins with greater initial solubility can disperse
quickly and yield well dispersed hydrocolloid system with macrostructure and smooth
texture. In addition, high initial solubility facilitates the diffusion between of proteins to the
gas/water and oil/water interface for enhanced their surface activity.
5.4. Viscosity
The viscosity or consistency of a liquid reflects its resistance to flow under an applied
force or shear stress and can be represented in viscosity coefficient η, which is defined as the
ratio of shear stress to shear rate (or flow rate). The viscosity of protein fluids is largely
related to the apparent diameter of dispersed protein molecules or protein particles. The
apparent diameter of proteins is decided by the following parameters: (1) the inherent nature
of protein molecules, such as molar concentration, molecular size, molecular volume,
molecular structure and charge; (2) protein-solvent interaction, which affects the swelling and
solubility of proteins and the hydrokinetics of the fluid surrounding protein molecules; (3)
protein-protein interaction. The interaction determines the size of protein aggregates and the
interaction opportunity increases in high protein concentrations.
The viscosity coefficient of protein-containing solutions, such as homogenates,
emulsions, pastes and gels, might decrease with the increase of shearing stress. This behavior
is known as shear thinning. During shearing, protein molecules are redirected to the flow
direction and the friction drag is reduced as a result. Besides, the break of hydrogen bonds
and other weak bonds can cause the dissociation of protein aggregates and network. The
break of weak bonds is a slow process so that the shear stress and apparent viscosity
decreases with the proceeding of shearing before the protein fluid reaches steady flow. When
the shearing force is no longer applied, the original aggregates or network can or cannot be
reformed. If the aggregates or networks can be completely or partially reformed, the change
of viscosity coefficient is irreversible.
The viscosity or consistency of protein system is an important property for liquid and
semisolid-type foods such as beverages, broth, sauces and cream. The fluid property of
protein dispersion systems is of practical significance in determining the optimum operation
conditions. For example, during transfer, blending, heating, cooling, and spray drying, the
fluidity of protein dispersion systems significantly affects the transfer of both mass and heat.
Muscle derived from mammals, birds and fish is the main source of meat. The skeletal
muscle of these animals contains 16%~22% proteins. Muscle protein can be divided into
myofibrillar protein, sarcoplasmic protein and matrix protein. Proteins of these three
170 Hong Lin, Lisha Wu and Shuhui Wang
categories differ markedly in their solubility. Sarcoplasmic proteins can be extracted by water
or buffers with low ionic strength (0.15mol/L or lower), myofibrillar protein can be extracted
only in high salt concentrations, and matrix proteins are insoluble. Sarcoplasmic proteins
contain large amounts of glycolytic enzymes and many other enzymes in addition to
myoglobin and haemoglobin, which affect the color of meat.
Myofibrillar proteins account for about half of animal skeletal muscle proteins. These
proteins are intensively charged hydrated and are insoluble under physiological conditions.
Matrix proteins participate in the formation of connective tissues. Collagen, reticulum
and elastin are examples of matrix proteins. Collagen is fibrous and occurs in all muscle
tissues. Reticulin refers to a type of fiber in connective tissues composed of type III collagen.
The proteins crosslink and form a fine mesh network. This network acts as a supporting mesh
in soft tissues such as liver, bone marrow, and the tissues and organs of the lymphatic system.
Elastic fiber is composed of the protein fibrillin and elastin made of simple amino acids such
as glycine, valine, alanine, and proline. Elastin helps skin to return to its original position
when it is poked or pinched. Elastin is also an important load-bearing tissue in the bodies of
vertebrates and used in places where mechanical energy is required to be stored. These matrix
proteins are less water soluble than sarcoplasmic and myofibrillar proteins.
6.2. Casein
Milk contains multiple types of proteins and the proteins exhibit different properties
(Table 5-11). In skimmed milk, casein accounts for about 80% of total protein. Casein is a
mixture of phospho-contaning proteins and precipitate out from skimmed milk at pH4.6 and
20°C. Casein is extremely hydrophobic and occurs as micelles in milk. Casein is composed of
αs1-casein, casein, β-casein, αs2-casein and κ-casein. The diameters of casein micelles range
from 50nm to 300nm with molecular weight range of 107~3×1010 Daltons. Casein micelles
are aggregated by sub-micelles, which has a diameter range from 10 to 20nm and molecular
weight range from 3×105 to 6×105.
Sub-micelles consist of αs1-casein, β-casein, αs2-casein and κ-casein and the fractions
aggregate through hydrophobic interaction. The core of sub-micelles is hydrophobic in
contrast to the hydrophilic surface. The carbohydrate-rich κ-casein is restricted on a region of
the surface through self-association. Therefore, the surface of sub-micelles contains one
carbohydrate-rich regions and one phosphate-rich region that is formed by other caseins.
Casein micelles are the aggregation of sub-micelles. The electrostatic interaction
contributed by colloidal calcium phosphate facilitates the aggregation of sub-micelles. The
aggregation occurs between the negatively charged serine residue on casein and the
positively-charged colloidal calcium phosphate, which occurs in Ca9 (PO4)6 clusters. Because
κ-casein contains no phosphate groups, the electrostatic interaction occurs only between α-
casein and β-casein.
During casein micelle formation, sub-micelles with low content of κ-casein or without κ-
casein are located in the interior of casein micelle. When the surface of the micelle is
completely covered by κ-casein, the micelles stop growing up.
Proteins 171
The main constitutients of whey proteins are β-lactoglobulin, α-lactoglobulin and serum
albumin in decreasing order in content, as shown in Table 5-9. These proteins are soluble at
pH 4.6 in their natural or denatured forms. In the manufacture of caseinate and country
cheese, these protein fractions remain in the whey. Hence, whey protein is a by-product of
cheese making.
Whey protein is soluble in a wide range of pH, temperature and ionic strength, pH4~5,
which is near the isoelectric point. Solubility is most important physicochemical and
functional property of natural whey protein. In addition, whey protein produces stable gel
when heated. This property together with its surface properties imparts whey protein with
important application in the food industry.
According to solubility, wheat proteins are divided into albumins (water soluble),
globulins (soluble in 10% NaCl but insoluble in water), gliadin (soluble in 70%~90%
ethanol), and glutenin (insoluble in water or ethanol but soluble in acid or alkali solutions).
Albumin and globulin account for about 10% to 15% of wheat endosperm proteins. The
two fractions contain free sulfhydryl and higher proportion of alkaline and charged amino
acids. Albumins are relative smaller molecules with molecular weight ranging from 12000 to
26000 compared with that of globulin of up to 100000. Gliadin and glutenin are the major
constituents of gluten and account for about 85% of flour protein. Both gliadin and glutenin
are complex mixtures of multiple protein components and the two fractions share similar
contents in wheat flour. Amino acid analysis indicates that gliadin and glutenin have very
high contents of glutamine and praline and very low contents of lysine and ionized amino
acids. Gliadin and glutenin are among the least charged proteins. Although the sulfur-
contaning amino acids are low, these amino acids play an important role in gluten structure
and dough formation.
172 Hong Lin, Lisha Wu and Shuhui Wang
The compact spherical structure of gliadin is related to the intramolecular disulfide bond.
Glutenins associate with each other through inter-molecuar disulfide bonding. Hence,
glutenins are found as large and stretched associated molecules. Glutenin is insoluble due to
intermolecular disulfide bonds, but treatment with reducing agents increases its solubility.
The formation of gluten is the result of both covalent and non-covalent interactions of
multiple protein constituents. Glutenins contribute to the formation of the network structure,
while gliadin and other proteins are trapped within the structure. Wheat flour contains 12%
protein, 70% starch and 2% fat. During kneading, these components are incorporated into the
gluten network structure and a starch-protein-fat composite matrix is formed.
The reduction of disulfide bonds during kneading the re-oxidation of sulfhydryl during
dough storage occur mainly in cross-linked glutenin. The reduction of disulfide bonds
facilitates the gluten relaxing and enhances the non-covalent interactions between fat, starch
and other additives, leading to the formation of a continuous starch-protein-fat complex.
Soybean contains 42% protein, 20% oil and 35% carbohydrates on dry basis. Soybean
protein is very sensitive to physical and chemical treatment. For example, heating under
moisture conditions and alteration of pH can cause significant changes in the physical
properties of soybean protein, such as solubility, viscosity and molecular weight.
Globulins are the most important constituents of soybean protein. Globulins are
insoluble in their isoelectric points, but the addition of NaCl or CaCl2 dissolves the proteins.
Globulins are soluble in water in the absence of NaCl or CaCl2 in other pHs than their
isoelectric points. Soybean proteins are least soluble in the pH range of 3.75~5.25, but are
most soluble in pH1.5~2.5 and that higher than 6.3. At pH6.5, about 85% nitrogen of defatted
soybean protein can be extracted by water and the yield can be further increased by 5%~10%
by increasing the pH.
According to the sedimentation coefficient, the water-extractable components of soybean
protein are divided into four fractions: 2S, 7S, 11S, and 15S, of which, 7S and 11S protein are
the most important. 7S protein accounts for 37% of the total protein, while the 11S fraction
accounts for 3l%. Soybean protein concentrates and soybean protein isolates are the most
important commercial products of soybean protein and their contents are higher than 70% and
90% respectively.
Soy protein concentrate can be prepared from defatted soybean meal in one of three
methods, namely by extraction with 60%~80% ethanol, with pH 4.5 aqueous solution, or with
water after heat denaturation. In these methods, extraction with the solvents remove soluble
carbohydrates from the material and the nitrogen content in the residue is increased as a
result. Removal of soluble carbohydrates markedly improves the flavor of soy protein
concentrate and flatulence factors are removed at the same time. Soy protein concentrates are
often used as the material of thermoplastic extrusion.
In the preparation of soybean protein isolate, proteins in defatted soybean meal are firstly
extracted with water at neutral or higher pH. Then, the proteins are precipitated by adjusting
the pH to the isoelectric point. The protein precipitate is collected and redissolved by
changing the pH and finally is applied to spray dryer. Soy protein isolate can be modified by
chemical, heat or enzymatic treatments to improve its functional properties.
Proteins 173
Due to the increase of world population and people‘s living standard, the demand on
protein keeps increasing and the deficiency of protein resources has turned to be a worldwide
issue. Improving the utilization efficiency of existing protein resources and exploiting new
protein resources are effective measures to solve the protein resource deficiency problem.
1) A wide range of materials can be used for single cell protein production. For example,
fiber resources such as straw, wood chips and bagasse can be used as the fermentation
substrate.
2) The investment for single cell protein production is low and the biomass grows very
quickly. The generation time of microorganisms is about only tens of minutes. It is estimated
that a 500 kg cow produces only 0.4kg protein, while yeast of the same weight can produce at
least 5000 kg proteins per day.
3) The industrial production of single cell protein does not need large area of arable lands
and are not affected by seasons and climate conditions.
174 Hong Lin, Lisha Wu and Shuhui Wang
The development of single cell protein resources has bright prospect. However, the high
content of nucleic acid in most single-cell proteins restricts their direct consumption by
consumers. Heat and alkaline treatment can improve the digestibility and amino acid
availability of single cell protein and reduce nucleic acids contents. Long-term toxicological
study indicates that heat- or alkaline-treated single cell protein is nontoxic.
The quality of proteins is mainly decided by the composition of essential amino acids
and their digestibility. High-quality proteins should contain all the essential amino acid and
their contents should be higher than the reference levels recommended by FAO/WHO/UNU.
Besides, the digestibility of high-quality proteins should be comparable or greater than that of
albumen and milk protein.
Table 5-12. Essential amino acid contents and nutritive values of proteins derived from several foods
(mg/g protein) [18, 19]
Item Source
Egg Milk Beef Fish Wheat Rice Corn Barley Soybean Broad bean Pea Peanut Kidney
bean
His 22 27 34 35 21 21 27 20 30 26 26 27 30
Ile 54 47 48 48 34 40 34 35 51 41 41 40 45
Leu 86 95 81 77 69 77 127 67 82 71 70 74 78
Lys 70 78 89 91 23(1) 34(1) 25(1) 32(1) 68 63 71 39(1) 65
Met+Cys 57 33 40 40 36 49 41 37 33 22(2) 24(2) 32 26
Phe+Tyr 93 102 80 76 77 94 85 79 95 69 76 100 83
Thr 47 44 46 46 28 34 32(2) 29(2) 41 33 36 29(2) 40
Trp 17 14 12 11 10 11 6(2) 11 14 8(1) 9(1) 11 11
Val 66 64 50 61 38 54 45 46 52 46 41 48 52
Total 512 504 480 485 336 414 422 356 466 379 394 400 430
Protein content (%) 12 3.5 18 19 12 7.5 / / 40 32 28 30 30
Chemical score /% (by 100 100 100 100 40 59 43 55 100 73 82 67 /
FAO/WHO pattern)
PER 3.9 3.1 3.0 3.5 1.5 2.0 / / 2.3 / 2.65 / /
BV(on rat) 94 84 74 76 65 73 / / 73 / / / /
NPU 94 82 67 79 40 70 / / 61 / / / /
Note: Chemical score is defined as the proportion of the content of a limiting amino acid in the material to that of the reference protein.
176 Hong Lin, Lisha Wu and Shuhui Wang
The proteins derived from major cereals and beans are deficient in at least one essential
amino acid. For example, the proteins of rice, wheat, barley and oat, are deficient in Lys but
rich in Met and this is reversed for the proteins of beans and seeds of oil crops. The proteins
of some seed plant seeds, such as peanuts, are deficient in both Met and Lys. Essential amino
acids with contents lower than that in reference protein are defined as limiting amino acids.
Adults that intake proteins only from crops and beans cannot maintain health and children
that intake only one of the two kinds of protein mentioned above cannot grow in the normal
rate. Table 5-12 lists the contents of essential amino acid in some proteins.
Generally, the proteins derived from plants and animals contain enough His, Ile, Leu,
Phe, Trp and Val and these amino acids are often not limiting amino acids in common foods.
However, Lys, Thr, Trp and sulfur-containing amino acid are often present in insufficient
quantity and are regarded as limiting amino acids.
Mixing a protein that deficient in an essential amino acid with another protein that is rich
in the essential amino acid can increase the nutrition value of the protein. For example, the
mixture of cereal protein and bean protein can provide complete and balanced essential amino
acids. The nutritive value of proteins can be improved also by supplementing the
corresponding limiting amino acids. For instance, supplementation of Met and Lys improves
the nutritive value of cereal and bean proteins.
If the protein or protein mixture contains all the essential amino acids and the contents
and proportions of the amino acids can maintain the optimum growth rate and health
conditions for consumers, the protein or protein mixture is though to have an ideal nutritive
quality. Table 5-13 lists the ideal amino acid distribution patterns for adults and children.
7.2. Digestibility
(1) Structure: The structure of proteins markedly affects their hydrolysis by enzymes.
Generally, native proteins are more resistant to enzymatic hydrolysis than their denatured
forms and the hydrolysis of insoluble fibrous proteins is more difficult than that of thoroughly
denatured globular proteins.
Proteins 177
(2) Antinutrients: Most vegetable proteins isolated and protein concentrates contain
trypsin inhibitors, chymotrypsin inhibitor, and exogenous lectins. The inhibitors prevent the
complete hydrolysis of proteins derived from legumes and oil seeds by trypsin. Lectins hinder
the absorption of amino acids in intestines. Heat treatment can destroy these antinutrients and
make proteins more susceptible to digestion. In addition to the antinutrients mentioned above,
proteins derived from plants also contain phytic acid, tannin and other anti-nutrients.
(3) Association with other components: Association with polysaccharides and dietary
fiber reduces the hydrolysis speed and thoroughness of proteins.
(4) Processing: Heat and alkaline treatment can cause chemical reactions in proteins,
such as Lys residue generation. These changes reduce the digestibility of proteins. Besides,
Millard reactions might occur between reducing sugars and proteins. These reactions reduce
the digestibility of Lys residues.
Toxic proteins have been found in many kinds of plants. Chemically, the toxic proteins
can be divided into two categories: lectins and enzyme inhibitors. Lectins occur widely in
leguminous plants, such as soybeans, peas, kidney beans, sword bean and castor seed. These
toxins can agglutinate red blood cells. Hence, the intake of uncooked or undercooked seeds of
these plants can cause poisoning. The main symptoms of lectin poisoning include nausea,
vomiting, and even death. Enzyme inhibitors are found in beans, potatoes, taros, wheat and
immature bananas. These proteins inhibit the activities of trypsin or amylase and affect the
digestion and absorption of nutrients by human body.
During food processing, temperature, moisture, pH, presence of other components and
pressure are main factors that lead to protein changes. Among these factors, moisture and
temperature have the largest effect on proteins. Hence, only the effects of dry and moist heat
treatments on protein are detailed.
8.1.1. Boiling
Boiling is a common processing method in the food industry. Boiling does not reduce
the quantity of proteins or essential amino acids of fish and meat. Boiling of milk neither
affects the amino acid content nor reduces the bioavailability. The egg white and yolk have
different sensitivity of heat treatment. The digestibility of raw egg white is only 50%, but raw
yolk can be digested and absorbed completely. Moderate cooking of eggs can yield of nearly
100% of digestibility and biological value due to heat denaturation of proteins. Moist heat
treatment is desired for most vegetable proteins, especially for proteins derived from beans.
Moist heat treatment increases the nutritive value of bean proteins due to protein denaturation,
inactivation of protease inhibitors and toxic substances, and disrupt of tissues and starch
granules.
Enzymes, such as lipase, lipoxygenase, protease, and polyphenol oxidase, can be
inactivated during blanching or steaming. Enzyme inactivation can prevent the formation of
undesired colors and flavors and the loss of vitamins. Heat treatment of rape seeds inactivates
myrosinase and avoids the formation the goitrogenic 5-vinyl-2-sulfur-oxazolidinone.
8.1.2. Pasteurization
It is generally believed that either the tank pasteurization method or the high-temperature
short time pasteurization has only slight effects on milk proteins, though whey proteins are
partially denatured. Extensive studies on infants, school-age children, adults and experimental
animals indicate that the nutritional value of milk is not affected by pasteurization.
Sealed container must be heated thoroughly until the contents are sterile. The required
intensity of heat treatment depends largely on the physical state of the contents. In
Proteins 179
pasteurization, the heat transferred from the vessel wall to the center in semi-solid foods is
much less than in foods containing liquids as the heat transfer medium. High-frequency
oscillatory electron heating and aseptic canning can overcome these problems, but their
applications are still very limited.
Pasteurization reduces the biological value of liquid milk by 6%, lysine content by 10%
and cystine content by 13%. The decrease in biological value may be due to the loss of
cystine. Pasteurization has much more significant effects on concentrated milk. Hence,
pasteurization can significantly reduce the bioavailability of proteins with limited lysine
contents.
8.1.4. Dehydration
Milk and dairy products can be dehydrated by spray drying or drum drying. The effects
of these methods on the nutritional value of milk proteins have attracted wide attentions. In
drum drying, milk is spread on the drum and the nutrient loss varies with the conditions
applied. Dehydration might lead to the loss of Lys. However, since Lys is not the limiting
amino acid of milk, moderate dehydration dose not impair the nutritive value of milk powder.
At present, dehydration has not been widely used in the industrial processing of meats,
because dehydration cannot impart meats with competitive price, quality, and consumer
acceptability compared with other products, through freeze-dried meats are more nutritional
than heat-treated or irradiated products. Nevertheless, the quality of freeze-dried products
cannot last long and critical changes might occur during storage.
Fish meal prepared from fish by dehydration is widely used as feed and only very few
are used in human foods. Fish can be dehydrated in many technologies, including flame
drying, steam pipe drying, and solvent drying. Therefore, the changes of protein quality vary
with the technology used.
8.1.5. Freeze-Drying
Most foods are dried in conventional methods. However, freeze-drying has potential
applications in the drying of unstable and gourmet foods. Studies have confirmed that freeze-
drying under proper conditions does not impair the quality of proteins.
180 Hong Lin, Lisha Wu and Shuhui Wang
Many researchers have confirmed that reactions of proteins with glucose at high
temperature and pressure significantly reduce the nutritive value of proteins, even when the
reaction time is short. Under these conditions, carbonyl compounds cause extensive cross-
linking of proteins through Strecker degradation and aldol condensation. In this case, the
value of any protein as the amino acid source is very limited.
As mentioned above, reducing sugars can react with proteins and cause amino acid loss.
However, it has also been found that sucrose is also involved in the reaction with proteins.
The initial reaction between lysine and sucrose is the 'aminolysis' of the 1, 2 glycosidic
linkage between the glucose and fructose residues by the ε-amino group of lysine. Breakdown
182 Hong Lin, Lisha Wu and Shuhui Wang
of the glycosidic linkage yields reducing groups, which undergo typical Maillard reaction
with another molecule of lysine. It has been reported that sucrose at relatively high levels in
oil seeds may be largely responsible for the damage to protein quality observed when they are
severely processed [22].
significantly affect the functional properties of proteins. The degree and result
(conformational change and aggregation) of thermal denaturation depend largely on the
nature of proteins and environmental conditions. Mammalian collagens start to unfold,
dissociate, and dissolve when heated to 65°C in the presence of large quantity of water. In
contrast, actins undergo contraction, aggregation and water holding capacity reduction under
same conditions.
Caseinate monomers are very resistant to heat treatment. Vigorous heat treatment dose
not affect the properties of caseinate. Mild heat treatment dose not lead to the destruction or
generation of covalent bonds or serious changes of higher structures in proteins. Hence, from
the nutritional point of view, the changes induced by mild heat treatment are beneficial.
Heat treatment can eliminate the toxic effects of lectins in legumes, because the lectin is
a thermal unstable protein which can bind polysaccharides. It can reduce the nutritional value
of natural plant proteins in the diet. The presence of lectins can form compounds by
combining intestinal brush border membrane polysaccharide, which can diminish the abilities
of shifting and digestion in amino acid, produce toxicity to human and animal; heat treatment
can eliminate their harmful effects.
Protease inhibitors in foods, including trypsin inhibitors and chymotrypsin inhibitors, are
inactivated during heat treatment. High temperature treatments, such as high-pressure
sterilization, puffing, sterilization, cooking and baking, can destroy all antinutrients factors
(Figure 5-14). Therefore, moderate heat treatment can markedly improve the nutritional value
of vegetable proteins.
Many proteins, such as soybean globulin, collagen and egg albumin, are more digestible
after moderate heat treatment.
Figure 5-14. Effect of steaming on trypsin inhibitor activity and protein efficiency ratio of soybean
meal feed [20]
After heat treatment, the proteins are more susceptible to enzymatic hydrolyze due to
unfolding and amino acid residues exposure. Besides, heat treatment can remove off-odor
compounds in soybean protein and avoid the undesired flavor caused by lipid oxidase.
8.3.2. Dehydration
When the water in a protein solution is removed, aggregation occurs to the proteins. This
is the case especially when water is removed by evaporation at high temperatures, because the
184 Hong Lin, Lisha Wu and Shuhui Wang
solubility and surface activity decline sharply. Hence, the effects of drying on the functional
properties of protein should not be ignored. Drying changes the size and internal and surface
porosity of particles and consequently alters the wettability, absorption, diapersion and
dissolution of food proteins. When water is quickly removed as steam, particles shrink in the
minimum level and salts and carbohydrates migrate to the dried surface, yielding porous
powder particles. This change can be observed in freeze-drying and spray-drying.
Introduction of bubbles to protein solution before drying or the implementation of controlled
aggregation during drying can be applied to increase the porosity of particles.
8.3.3. Irradiation
Irritation causes inter- and intra-molecular cross-linking of proteins or peptide bond
breakdown in foods with low moisture content. In the presence of catalase, Tyr is oxidized
and condensed to dityrosine.
8.3.4. Oxidation
Oxidants are important additives in the food industry. For example, hydrogen peroxide is
sterilization and bleaching agent which can be used as a low-temperature fungicide in
package. It can also been used to improve the color of fish protein concentrates, flours and oil
seed protein isolates. Benzoyl peroxide can oxidize cysteine in flour to cystine so as to
enhance gluten strength and bleach flour. In some cases, benzoyl peroxide can also be used in
whey powder bleaching. Peroxides are also found in foods without artificially added oxidants
and these peroxides are often the reason for the degradation of proteins present in the foods.
Light oxidation, irradiation, trace metals, oxygen, hot air drying and aeration during
fermentation can all induce oxidative denaturation of amino acids in proteins.
Trp is the most sensitive amino acids to oxidation, followed by tyrosine and histidine in
sequence. The oxidation of sulfur-containing amino acids occurs mainly in the sulfur-
containing side chains and that of aromatic-containing amino acids mainly occurs in the side
chains containing aromatic rings.
processed drinks. The hydrolytes can also be used as alternative protein sources for patients
allergic to milk and gluten or those with digestive tract diseases.
Partial hydrolysis can improve the emulsifying and foaming abilities of thermally
denatured proteins, because the increased solubility of proteins facilitates their diffusion to
the oil/water and gas/water interfaces. However, when the degree of hydrolysis exceeds
3%~5%, the viscosity and thickness of protein layer absorbed on the interface are insufficient
to stabilize emulsion and foam. Hydrolysis reduces the volume of proteins, which is
unfavorable for the gelling ability and viscoelasticity of proteins, but limited hydrolysis of
gluten can enhance the expansion degree of dough in bread making and improve the flakiness
of biscuits.
In addition, proteases can connect low molecular weight peptides through peptide
transferring to produce new larger peptides, namely proteinoids.
Peptides with molecular weight greater than 6kD cannot the action sites of taste
receptors and are hence tasteless. Whether a peptide with molecular weight less than 6kD is
bitter and its bitter intensity is related to its hydrophobicity. For details, see Section 5.1.3.
9.2. Off-Odors
Some protein products must undergo the deodorizaton process to remove off-odor
compounds bound to proteins. Ketones, aldehydes, alcohols, phenols, and lipid oxidation
products can produce beany flavor, rancidity, bitterness, and harsh taste. These compounds
can bind to proteins. When the proteins are cooked or chewed, these compounds are released
and the undesired tastes or odors are delivered to consumers, which markedly reduce the
acceptability of foods.
In addition to off-odors, proteins can also serve as the carrier of flavors. For example,
textured vegetable proteins can impart the meat flavor. Ideally, the desired volatile flavor
components should bind to carriers during storage and processing and be released rapidly and
completely in the oral cavity upon ingestion. Any factors that change the conformation of
proteins affect the binding to volatile compounds to proteins. In the presence of water
facilitates the binding to polar compounds to proteins, but shows no effect on that of nonpolar
compounds. Volatile compounds have only limited diffusion in dried protein components.
However, when the water activity is slightly improved, volatile compounds diffuse to their
binding sites rapidly. Casein can bind more volatile carbonyl compounds, alcohols and esters
in neutral and alkaline conditions than in acidic solutions. Oxidates and sulfates in high
concentrations can cause protein unfolding and thus improve the binding of proteins to
carbonyl compounds. Agents that can dissociate proteins or interrupt disulfide bonds improve
the binding of proteins to volatile compounds. When oligomers are dissociated to subunits,
the hydrophobic areas between subunits are masked during conformation change of the
subunits. Hence, the binding to nonvolatile compounds is reduced.
Thorough hydrolysis of proteins reduces their ability of binding volatile compounds. For
example, one kilogram of soybean protein can bind 6.7 mg caproaldehyde. After the protein
is hydrolyzed by acidic protease, the binding capability is reduced to 1 mg/kg protein. Hence,
the beany flavor of soybean protein can be alleviated by hydrolysis. Thermally denatured
proteins generally have improved volatile binding capabilities. For example, when 10%
soybean protein isolate is heated at 90°C for 1~24h in the presence of caproaldehyde and is
then free dried, the amount of caproaldehyde bound is 3~6 times more than that of unheated
protein. Dehydration process, such as free drying, can release more than 50% of bound
volative compounds. However, if a volatile compound has a low vapour pressure and is
present in low content, it can be well retained after the treatments. It should be noted that the
presence of lipids is beneficial for the binding and retention of volative compounds, including
those generated by lipid oxidation.
derivates, and dihydrochalcone and their derivates. The potential of perilla aldehyde and its
derivates as sweetener has also attracted much attention.
Some naturally occurring amino acids have been found to be sweet, including Gly, D-
Ala, L-Ala, D-Ser, L-Ser, D-Thr, L-Thr, D-Trp, D-Pro, D-hydroxyproline, and D-Glu. Some
amino acid derivates are also found to be sweet. For example, the specific saccharinity of 6-
methyl-D-Trp reaches 1000 and is a potential novel sweetener.
In 1969, it was found that many dipeptide derivates of aspartic acid are sweet and
phenylalanine methyl ester (aspartame) has been approved by FDA for use in foods as a
sweetener. Aspartame is the sweetest compound among all sweeteners identified and is 2.7
times sweeter than sucrose. These dipeptide sweeteners are non-sugar compounds. Their
components are natural molecules and can be metabolized by human body. Besides, their
sweetness curves fit that of sucrose very well and the sweetness tastes very well. The
shortcoming is that they are unstable in high temperatures.
The proteins of food have little flavor of their own, but are known to bind trap aroma
compounds. The most extensively studied protein is the milk protein β-lactoglobulin. The
protein can interact with many flavour compounds, such as aldehydes and ketones, ionones
and esters. Both reversible binding and irreversible binding can occur between proteins and
flavor compounds. The type of interaction between a protein and a flavor compound depends
on the nature of both the protein and the aroma compound. As most aroma compounds are
hydrophobic in nature, hydrophobic and reversible binding is predominant. On the other
hand, certain flavor compounds, such as aldehydes, can form covalent bonds with proteins
and such interactions are irreversible.
Proteins can be used as flavor carriers in the food industry. It is suggested that β-
lactoglobulin, the major whey protein, could be engineered to bind and protect a wide range
of volatile and unstable flavors during food manufacturing or to release them in more or less
controlled ways by chemical or physical modifications.
Processing significantly affects the interactions between flavors and proteins. Studies on
the interactions between whey protein isolate and flavor compounds (2-nonanone, 1-nonanal,
and trans-2-nonenal). It was found that hydrophobic interactions are weakened upon heating
or high pressure denaturation, whereas covalent interactions were enhanced [30]. Conditions
of high hydrostatic pressure treatment (HHP) and flavor species significantly affect flavor
retention. HHP treatments did not result in significant changes in the flavor retention for
benzaldehyde in WPC solutions, but significant decreases of nonanone retention were only
observed at 100 ppm when WPC solutions were HHP-treated for 10 min. While use of HHP
treatment of WPC has potential in real food systems, these findings demonstrate the
188 Hong Lin, Lisha Wu and Shuhui Wang
importance of careful selection of HHP treatment times and flavor concentrations for desired
outcomes in food application [31].
Milk protein-flavor interactions are very dependent on the conformational state of a
protein. Therefore, factors such as pH, temperature, and high pressure that influence protein
conformation can markedly change flavor binding characteristics of proteins. Interactions of
vanillin with soy, casein, and whey proteins Bindings of vanillin with casein and whey
protein were enthalpy driven, while the interaction of vanillin with soy protein was highly
entropy driven. The researchers inferred that conformational changes of soy protein might be
important in binding of vanillin [32].
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2005.
[2] Murray RK, Granner DK, Rodwell VW, Mayes PA. Harper's Biochemistry. 25th
edition. McGraw-Hill Companies, 1999.
[3] http://www.hemaquest.com/indications/hemoglobin.asp.
[4] Xie, BJ. Food chemistry. 1st edition. Beijing: Science Press, 2004: 255.
[5] Damodaran S. Influence of protein conformation on its adaptability under chaotropic
conditions. International Journal of Biological Macromolecules, 1989, 11:2-8.
[6] Han JM, Ledward DA. High pressure/thermal treatment effects on the texture of beef
muscle. Meat Science, 2004, 68: 347-355.
[7] Wang DF. Food Chemistry. 1st edition. Beijing: Chemistry Industry Press. 2007: 118.
[8] Xie BJ. Food chemistry. 1st edition. Beijing: Science Press, 2004: 259.
[9] Xie BJ. Food chemistry. 1st edition. Beijing: Science Press, 2004: 260.
[10] Hu WW, Xie BJ. Food Chemistry. 1st edition. Beijing: Science Press, 1992: 165.
[11] Damodaran S. Interfaces, protein films, and foams. Advances in Food and Nutrition
Research. 1990, 34: 1-79.
[12] Xie BJ. Food chemistry. 1st edition. Beijing: Science Press. 2004: 280.
[13] Wang DF. Food Chemistry. 1st edition. Beijing: Chemistry Industry Press. 2007: 118.
[14] Xie BJ. Food chemistry. 1st edition. Beijing: Science Press. 2004: 278.
[15] Xie BJ. Food chemistry. 1st edition. Beijing: Science Press. 2004: 281.
[16] Pusztai A, Clarke EMW, Grant G, King TP. The toxicity of Phaseolus vulgaris lectins.
Nitrogen balance and immunochemical studies. Journal of the Science of Food and
Agriculture. 1981, 35: 701-711.
[17] Zhu H, Damodaran S. Effects of calcium and magnesium ions on aggregation of whey
protein isolate and its effect on foaming properties. Journal of Agricultural and Food
Chemistry. 1994, 42: 856-862.
[18] Eggum BO, Beames RM. The nutritive value of seed proteins. In: Gottschalk W,
Müller PH. Seed Proteins: Biochemistry, Genetics, Nutritive value. Berlin: Springer.
1983: 499-531.
[19] FAO/WHO/UNU. Energy and Protein Requirements, Report of a Joint
FAO/WHO/UNU Expert Consultation. World Health Organization Technical Report
Series. 1985: 724.
Proteins 189
[20] Lund D. Effect of commercial processing on nutrients. In: Karmas E, Harris RS.
Nutritional Evaluation of Food Processing. New York: Van Nostrand Reihhold. 1988:
319-354.
[21] Wang DF. Food Chemistry. 1st edition. Beijing: Chemistry Industry Press. 2007: 124.
[22] Hurrell RF, Carpenter KJ. Mechanisms of heat damage in proteins. The role of sucrose
in the susceptibility of protein foods to heat damage. British Journal of Nutrition. 1977,
38: 285-297.
[23] Je JY, Park PJ, Kim, SK. Antioxidant activity of a peptide isolated from Alaska pollack
(Theragra chalcogramma) frame protein hydrolysate. Food Research International.
2005, 38: 45-50.
[24] Kim SY, Je JY, Kim SK. Purification and characterization of antioxidant peptide from
hoki (Johnius belengerii) frame protein by gastrointestinal digestion. The Journal of
Nutritional Biochemistry. 2007, 18: 31-38.
[25] Song R, Wei RB, Zhang B, Yang ZS, Wang DF. Antioxidant and Antiproliferative
Activities of Heated Sterilized Pepsin Hydrolysate Derived from Half-Fin Anchovy
(Setipinna taty). Marine Drugs. 2011, 9: 1142-1156.
[26] Song R, Wei RB, Zhang B, Yang ZS, Wang, DF. Optimization of the Antibacterial
Activity of Half-Fin Anchovy (Setipinna taty) Hydrolysates. Food and Bioprocess
Technology. 2011: 1-11.
[27] Rajapakse N, Mendis E, Jung WK, Je JY, Kim SK. Purification of a radical scavenging
peptide from fermented mussel sauce and its antioxidant properties. Food Research
International. 2005, 38: 175-182.
[28] Virtanen T, Pihlanto A, Akkanen S, Korhonen H. Development of antioxidant activity
in milk whey during fermentation with lactic acid bacteria. Journal of Applied
Microbiology. 2007, 102: 106-115.
[29] Minelli A, Bellezza I, Grottelli S, Galli F. Focus on cyclo(His-Pro): history and
perspectives as antioxidant peptide. Amino acids. 2008, 35: 283-289.
[30] Kühn J, Considine T, Singh H. Binding of Flavor Compounds and Whey Protein
Isolate as Affected by Heat and High Pressure Treatments. Journal of Agricultural and
Food Chemistry. 2008, 56: 10218-10224.
[31] Liu XM, Powers JR, Swanson BG, Hill HH, Clark S. High Hydrostatic Pressure
Affects Flavor-binding Properties of Whey Protein Concentrate. Journal of Food
Science. 2005, 70: C581-C585.
[32] Li Z, Grün IU, Fernando, LN. Interaction of Vanillin with Soy and Dairy Proteins in
Aqueous Model Systems: A Thermodynamic Study. Journal of Food Science. 2000,
65: 997-1001.
In: Food Chemistry ISBN: 978-1-61942-125-7
Editors: D.Wang, H. Lin, J. Kan et al. © 2012 Nova Science Publishers, Inc.
Chapter 6
VITAMINS
ABSTRACT
Vitamin is one important group of nutrients that determines the nutritional value of
foods. These compounds play extremely important role in many metabolisms in organism
as cofactors of various enzymes and long-term vitamin deficiency can cause various
diseases and even death. Besides, some vitamins, such as Vc and sulfur-containing
compounds, also markedly affect the color and flavor of foods. This chapter introduces
the structures, properties, physiological functions and deficiency symptoms, and stability
of the vitamins that have been identified one by one. Then, the factors that influence
vitamin contents in foods and the changes of vitamins during processing and storage are
discussed.
1. CLASSIFICATION OF VITAMINS
Vitamins are classified by their biological and chemical activities, as well as the
chronological order of being found, but not their structures. Basically each "vitamin" has a
multiple chemical substances (called vitamers) that show similar biological activity, rather
than having a fixed chemical structure. For example, Vitamin A includes retinol, retinal, and
four known carotenoids. The classification and some functions of vitamins are summarized in
Table 6-1.
Vitamins are classified into two water-soluble and fat-soluble ones according to
solubility. Among the 13 vitamins identified, the eight members of the B family and vitamin
C are water soluble, while vitamins A, D, E, and K are fat soluble.
192 Yibin Zhou, Dongfeng Wang and Ping Dong
Because water-soluble vitamins can dissolve in body fluid and can not be stored readily,
consistent daily intake is required. On the other hand, fat-soluble vitamins, absorbed through
the intestinal tract with the help of lipids (fats), can be easily accumulated in the body. Water-
soluble vitamins are readily excreted from the body so their consumption can be simply
checked by the degree of urinary output.
2. VITAMINS IN FOODS
As described above, vitamins are a class of natural organic compounds that maintains the
normal physiological functions of human body. Although, the amount required for daily diet
is only several micrograms or milligrams, they are essential for human health.
Microorganisms in intestines can synthesize some vitamins, but the quantity far from the need
of human body. Therefore, vitamins have to be largely provided by foods.
2.1. Vitamin A
hyperkeratosis, and keratomalacia. Vitamin A is needed by the retina of the eye as the light-
absorbing molecule of retinal, without which the vision will be lost. An oxidized form of
vitamin A – retinoic acid, is a hormone-like growth factor for epithelial and other cells.
Vitamin A was discovered in 1917 by Elmer McCollum (University of Wisconsin–Madison),
Lafayette Mendel (Yale University) and Thomas Burr Osborne (Yale University). In 1919,
Steenbock (University of Wisconsin) proposed that yellow plant pigments (beta-carotene)
might be vitamin A, which was named as ―fat-soluble factor A". Vitamin A exists in animal
tissues, plant tissues and fungi.
(1) Structure.
Structures of vitamin A and its precursors are shown in Table 2.
β-carotene 50
α-carotene 25
β-Apo-8´- 25-30
carotenal
Zeaxanthin 0
Canthaxanthin 0
Astacin 0
Lycopene
0
the beta-ionine ring. Usually vitamin A refers to vitamin A1, retinol. The biological effect of
vitamin A2 is about 40% of that of vitamin A1.
In foods of animal origin, the major form of vitamin A is an ester, primarily retinyl
palmitate, which is converted to retinol in small intestine. Retinol can be converted to its
visually active aldehyde form, retinal. The associated acid (retinoic acid), a metabolite that
can be irreversibly degraded from vitamin A, has only partial vitamin A activity, and does not
function in the retina for the visual cycle.
Food carotenoids, mainly include beta-carotene and lutein (Table 6-2), are also
precursors of vitamin A. Usually they have two connected retinyl groups, which are used in
the body to contribute to vitamin A activity. The well-known orange pigment of carrots (beta-
carotene), which shows some vitamin activities itself, is an important source of vitamin A.
(2) General properties.
Usually, vitamin A is a light yellow viscous liquid. Pure vitamin A1 is a light-yellowish
(or primrose yellow) crystal and melts at 62°C-64°C. Vitamin A is fat soluble and is stable
under alkali conditions or inert atmosphere. Vitamin A is thermal stable and is not destroyed
in temperatures up to 120°C-130°C, but it is liable to decomposition in exposure to air,
oxidants and ultraviolet radiation. Both vitamin A and carotene can react with antimony
trioxide in ethanol to produce dark blue yellow. This property has been used for the
spectrometric determination of vitamin A and carotene.
(3) Physiological functions and deficiency symptoms.
Vitamin A promotes the growth of human body. Besides, it maintains the integrity and
health of epithelial tissue and ensures the normal vision.
Deficiency of vitamin A for a long time can cause night blindness and loss of dark
adaptation. In subjects suffering severe vitamin deficiency, the keratinized epithelial cells at
gastrointestinal tract and eye cornea can even not be produced. The obvious characteristic of
vitamin A deficiency is xerophthalmia, such as cornea hyperemia, inflammation and sclerosis.
This is why vitamin A is also known as the antixerophthalmic vitamin. Excessive intake of
vitamin A (more than 65,000~500,000 international units) can result in poisoning, but the
symptoms can disappear several days later if vitamin A is excluded from the diet.
(4) Stability and degradation.
All naturally occurring carotenoids are present in the trans conformation. The compounds
can transform to the cis conformation and lose its activity when heating. The isomerization of
carotenoids occurs readily during storage, as shown in Table 6-3. In addition, exposure to
light, acids and watery iodine also causes the transform from cis- to trans-conformation of
carotenoids and retinols.
The destruction mechanisms of vitamin A precursors vary with processing conditions
(Figure 6-1). The cis-trans transformation of beta-carotenes upon heating occurs only in the
absence of oxygen. Beta-carotene is decomposed to a series of aromatic hydrocarbons at
higher temperatures and the major decomposition product is lonene, which has important
implications on food flavor. Carotene is often intentionally added to foods to produce aroma
during food processing.
Vitamins 195
Oxygen, light, enzymes, and lipid hydroperoxide enhance the oxidative degradation of
carotene. Oxidation of beta-carotene first involves the formation of the 5, 6-epoxide, which
will isomerize to beta-carotene oxide, namely 5, 8-epoxide. Vitamin A and provitamin A are
usually inactivated in dehydrated foods, but the loss varies with the drying technology (Table
6-4). Maintenance of Aw and oxygen partial pressure in low levels can reduce the loss of
carotenoid and vitamin A.
2.2. Vitamin D
Vitamin D is also known as anti-rickets or anti-rachitis vitamin. Six members have been
ascertained, including Vitamin D2, Vitamin D3, Vitamin D4, Vitamin D5, Vitamin D6, and
Vitamin D7, among which Vitamin D2 and Vitamin D3 are the most important.
Vitamin D in food always coexists with vitamin A. Fat in fishes or liver in animals are
rich in vitamin D. The content of Vitamin D in fish oil from seafood is much high, followed
by egg yolks, milk, and butter. Sunlight can promot the synthesis of vitamin D in animals.
Thus, the levels of vitamin D in milk and cream produced in summer are more than those in
winter due to the stronger sunlight in summer.
(1) Structure.
The vitamin D members are steroids that contain the cyclopentanoperhy drophenanthrene
ring structure and they are distinguished by their structures of the branch chain R, as shown in
Figure 6-2. Vitamin D is found only in animal tissues, but most plants contain sterols, which
can be converted to vitamin D by ultraviolet light.
(2) General properties.
Vitamin D members are colorless crystal and fat soluble. Vitamin D is quite stable
against acids, alkali, and oxygen, but is readily destroyed by light and temperatures higher
than 160°C.
(3) Physiological functions and deficiency.
Vitamin D regulates the metabolism of calcium and phosphorus and maintains the level
of calcium and phosphorus in blood. Hence, the deficiency of calcium and phosphorus is
often related to the level of vitamin in human body. The increased requirements of pregnant
and lactating women on calcium and phosphorus can be realized by vitamin D-reinforced
diets.
Vitamin D deficiency leads to osteomalacia and rickets. However, excessive intake of
vitamin D can cause posioning. The symptoms of acute vitamin D poisoning include loss of
appetite, nausea, vomiting, diarrhea, headache and polyuria and those of chronic poisoning
include weight loss, albinism, and even soft-tissue calcification or serious kidney failure.
Vitamins 197
R
CH 3
19
11 12 13 17 16
CH 2 15
9 14
8
1 10
2
3 5 7
4 6
HO
CH2
Vitamin D2 R= CH CH CH CH CH
CH3 CH3 CH3
CH2
R= CH CH2 CH2 CH2 CH
Vitamin D3
CH3 CH3
CH3
R= CH CH2 CH2 CH CH
Vitamin D4
CH3 CH3 CH3
CH3
Vitamin D5 R= CH CH2 CH2 CH CH
CH3
CH3 CH 2C H 3
CH3
R= CH CH CH CH CH
Vitamin D6
CH3 CH3
C H 2C H 3
CH3
Vitamin D7 R= CH CH2 CH CH2 CH
CH3 CH3
CH3
2.3. Vitamin E
Table 6-5. Contents of tocopherol in plant oil and some foods [4,5]
Relative
Side chain Name R1 R2 R3 Occurrence
biological value
α- tocopherol -CH3 -CH3 -CH3 Wheat embryo 1
β- tocopherol -CH3 -H -CH3 Wheat embryo 0.5
γ- tocopherol -H -CH3 -CH3 Corn 0.2
[ ]3
δ- tocopherol -H -H -CH3 Bean 0.1
Σ- tocopherol -CH3 -CH3 -H Rice 0.5
η- tocopherol -H -CH3 -H Rice 0
ε- tocopherol -CH3 -H -CH3 Corn 0.5
[ ]3
Σ1- tocopherol -CH3 -CH3 -CH3 Rice 0.5
Figure 6-4. Oxidation pathway of α-tocopherol initiated by peroxide free radicals [6].
2.4. Vitamin K
Vitamin K is found due to its blood coagulation functions. Two kinds of vitamin K have
been identified, including vitamin K1, which is extracted from alfalfa, and vitamin K1, which
is obtained from degraded fishes.
200 Yibin Zhou, Dongfeng Wang and Ping Dong
Vitamin K occurs mainly in plant tissues. Green leafy vegetables, such as alfalfa,
cabbage, cauliflower, spinach and cabbage, contain more vitamin K1 than vitamin K2, with
the latter derived mainly from the metabolism of intestinal bacteria.
(1) Structure.
Vitamin K1 and K2 are the derivatives of 2-methyl-1, 4-naphthoquinone and the two
compounds differ in their side chains, as shown in Figure 6-6.
(2) General properties.
Vitamin K1 is a viscous yellow oily liquid can be crystallized from alcohol solution
under low temperature, and its melting point is -20 °C. Vitamin K2 is a yellow crystal and
melts in the temperature range from 53.5°C to 54.5°C. Both vitamin K1 and K2 are stable
Vitamins 201
against heating, but are readily destroyed by alkali and sunlight. K2 is more susceptible to
oxidation than K1.
(3) Physiological function and deficiency.
Vitamin K promotes blood coagulation and is essential for the synthesis of prothrombin
in liver. Vitamin K deficiency leads to reduced content of prothrombin in plasma and
prolonged duration of blood coagulation. Vitamin K will lose its promotion of prothrombin
synthesis in liver if liver dysfunction occurs. In addition, vitamin K also enhances intestines
peristalsis and secretion.
2.5. Vitamin B1
Vitamin B1 is also known as thiamin. Yeast is reported to have the highest content of
vitamin B1, followed by muscle, drupe, and eggs. Vitamin B1 in cereals occurs mainly in
cortex and embryo. Table 6-7 lists the contents of vitamin B1 in some cereal products.
(1) Structure.
Vitamin B1 contains a pyrimidine ring that contains an amino group and a thiazole ring
thatn contains a sulfur residue, as shown in Figure 6-7.
(2) Properties.
The hydrochloride salt of vitamin B1 is a white crystal. The crystal is stable at 100°C for
24 hours, but is decomposed in temperatures higher than 249°C. Vitamin B1 is water soluble
and one gram of vitamin B1 can dissolve in 1mL water, 18 mL glycerin, 100 mL 95% alcohol
or 315 mL anhydrous alcohol, but is insoluble in ethyl ether, acetone, chloroform or benzene.
Vitamin B1 has a smell similar to that of yeast and tastes bitter.
Vitamin B1 is stable in solutions with pH less than 3.5. Under these conditions, the
vitamin can maintain its activity even when heated at 120°C; however, it is easily destroyed
when the pH exceeds 3.7. For example, 25% of thiamin is lost when heated in 97°C at pH 4.3
for 1 hour and the value reaches 80% when the pH is further increased to 7.0. Though vitamin
B1 is readily damaged by high temperatures in alkaline conditions, cooking is insufficient to
completely destroy the vitamin in rice. During bread bakery, about 15~30% of the total
amount of vitamin B1 in flour is lost.
Both vitamin B1 and its pyrophosphate salt can be oxidized by mild oxidant (such as the
alkaline solution of potassium ferricyanide) to produce the dark blue fluorescence-emitting
thiochrome. This reaction has been used to quantitative determination of vitamin B1. The
structure of thiochrome is shown in Figure 6-8:
Thiamine can be converted to thiamine pyrophosphate (TPP, Figure 6-9) by thiamine
kinase in the presence of ATP. TPP plays an important role in sugar metabolism.
(3) Physiological function and deficiency.
Vitamin B1 participates in the oxidative decarboxylation of α-keto acid, such as pyruvic
acid and α- ketoglutaric acid, as cocarboxylase. Vitamin B1 deficiency results in the
accumulation of pyruvic acid in blood. Meanwhile, the accumulated pyruvic acid inhibits the
activity of dehydrogenase and leads to the accumulation of lactic acid. Hence, vitamin B1 is
essential for sugar metabolism.
Vitamin B1 is of special importance for consumers with starch as the main energy source.
It is reported that the amount of vitamin B1 required is propontional to the amount of
carbohydrates consumed and it is recommended that 1 microgram of vitamin B1 is needed for
the metabolism of 1 gram of carbohydrates.
The early symptom of vitamin B1 deficiency includes nervous system disorder, mental
and physical fatigue, dyspepsia and loss of appetite. If vitamin B1 cannot be supplemented in
time, the patients develop polyneuritis or beriberi. In this stage, the patients become poor in
heath status and other symptoms include lower limb edema, nerve paralysis, loss of muscle
contraction capacity, and even death.
(4) Stability and degradation.
Vitamin B1 is the most unstable among all the vitamins identified and is susceptible to the
influence of aw, pH, temperature, ionic strength, buffer solution and the presence of other
compounds. The degradation of vitamin B1 is initiated by the nucleophilic substitution of the
Vitamins 203
methylene carbon between the two rings. Therefore, vitamin B1 can be readily destroyed by
strong nucleophiles such as HSO3-.
Vitamin B1 is stable at low aw and room temperature. For example, nearly no loss of
vitamin B1 is observed when cereal foods with aw ranging from 0.1 to 0.65 are stored at
37°C. In storage temperature 45°C and aw 0.2~0.5, the decomposition of vitamin B1
increases. The maximum vitamin B1 degradation is observed in aw 0.5. As the aw further
increases, the loss of vitamin B1 decreases, as shown in Figure 6-10.
Temperature significantly affects the retention of vitamin B1 during storage (Table 6-8).
In 1.5°C, no loss of vitamin B1 is detected in tomato juice, pea and orange juice after storage
for 12 months. When the storage temperature is elevated to 35°C, up to 50% of vitamin B1 is
lost.
The relationship between vitamin B1 degradation rate and pH is shown in Figure 6-11.
The same relationship is observed in either phosphate buffer or cereal. That is, the
degradation of vitamin B1 increases with the rise of pH.
Similar to other other-water soluble vitamins, rinsing and boiling cause great loss of
vitamin B1. Table 6-9 lists the effect of various processing methods on the retention of
vitamin B1 in various foods.
The thermal degradation of Vitamin B1 can generate special flavor compounds, such as
hydrogen sulfide, furan, and dihydro-thiophenol. These compounds impart foods with special
flavor.
2.6. Vitamin B2
Vitamin B2 is also known as riboflavin and is found mainly in yeast, liver, milk, muscle
and yolk. In addition, Greenery vegetables, grain and germinated seed also contain vitamin
B2.
Figure 6-10. Relationship between vitamin B1 degradation rate and aw of cereal foods when stored at
45°C [9].
204 Yibin Zhou, Dongfeng Wang and Ping Dong
(1) Structure.
Riboflavin is the condensation product of D-ribitol and 7, 8-dimethyl-isoalloxazine. The
structure of vitamin B2 is showed in Figure 6-12.
(2) General properties.
Riboflavin is an orange needle crystal and tastes bitter taste. This vitamin melts in 282 °C
and sparingly soluble in water, but readily soluble in alkaline solutions.
The aqueous solution of riboflavin generates yellow fluorescence in wavelength range
440~500nm. This property can be used to spectrometrically determine the content of the
compound.
Riboflavin is more thermal stable than vitamin B1. After dried yeast is heated in 120 °C
for several hours, nearly all vitamin B1 is lost, but vitamin B2 is completely retained.
Riboflavin is unstable in the presence of light and ultraviolet, especially in alkaline and
high temperature conditions. In the presence of light, riboflavin in alkaline solutions is
converted to lumiflavin. This product has the same color and fluorescence emission capability
as riboflavin. In acidic or neutral solutions, riboflavin is transformed to lumichrome, which
can emit blue fluorescence. The structures of the two compounds are illustrated in Figure 6-
13.
(3) Physiological function and deficiency.
Vitamin B2 is an essential cofactor for enzymes involved in cellular respiration and
dehydrogenation. Vitamin B2 deficiency leads to reduced respiration capacity and retarded
metabolism. The symptoms of vitamin B2 deficiency include stomatitis, angular cheilitis, eye
keratitis, and dermatitis.
(4) Stability and degradation.
Riboflavin is stable against thermal treatment and oxygen. Riboflavin is resistant to light
in acidic solutions, but is readily decomposed by light in alkaline solutions. In light-induced
decomposition, photochemical degradation occurs in ribitol to generate inactive lumiflavin
and a series of free radicals (Figure 6-14). Lumiflavin has stronger oxidizability than
riboflavin and its generation accelerates the destruction of other vitamins, especially Vc. The
special off-odor of sunlight-exposed milk has been attributed to the light-induced
decomposition of riboflavin.
Pantothenic acid (Vitamin B5) is a water soluble vitamin and occurs widely in foods,
including yeast, liver, kidney, egg, muscle, skimmed milk, pea, peanut and sweet potato. The
contents of pantothenic acid in unpolished rice, wheat, and corn are about 1.7 mg/100g, 1.0-
1.5 mg/100g, and 0.46 mg/100g respectively. Intestinal bacteria and some plants can
synthesize pantothenic acid.
(1) Structure.
The chemical name of pantothenic acid is N-(α, γ-dihydroxy-β, β-dimethyl-butyryl)- β-
alanine. Its structure is shown in Figure 6-15.
(2) Properties.
CH3
HOCH2 C CH CO NH CH2 CH2 COOH
CH3 OH
4 COOH CONH2
5 3
61 2
N N
Nicotinic acid Nicotinamide
Pantothenic acid is light yellow and viscous. It is soluble in acetic acid and water, but
insoluble in chloroform and benzene. In neutral solutions, pantothenic acid is resistant to heat,
oxidation and reduction, but can be decomposed β-alanine and other compounds by acids,
bases, and dry heating. The calcium salt of pantothenic acid is a colorless crystalline powder.
Calcium pantothenate tastes slightly bitter and is water soluble. It is stable against light and
air, but its aqueous solutions of pH 5~7 can be destroyed by heat.
In organisms, pantothenic acid takes effect mainly in the form coenzyme A (CoA) form.
(3) Physiological function.
Pantothenic acid is the coenzyme of many enzymes involved in carbohydrate, lipid and
protein metabolism and plays an important role in the transfer of the acetyl group.
Pantothenic is also essential for the growth of some microorganisms.
(4) Stability and degradation.
Pantothenic acid is stable in neutral solutions, but is easily decomposed in acid solutions.
In the pH range 6~4, its decomposition rate increases with the increase of acidity. Due to the
heat liability and strong hygroscopicity of pantothenic acid, the calcium salt of pantothenic
acid has been commercially used as an alternative. The changes of pantothenic acid contents
in foods are affected by processing methods in addition to the materials. For example, the loss
of pantothenic acid in pasteurized milk is usually less than 10%. The loss of pantothenic acid
in vegetables is about 10-30 % and most of vitamin is lost during rinsing. The bioavailability
of dietary pantothenic acid is about 51%.
2.8. Vitamin B3
Vitamin B3 is known as vitamin PP and is famous for its anti-pellagra capability. Two
members of the family have been identified, including nicotinic acid and nicotinamide. Both
te two compounds occur widely in yeasts, liver, muscle, milk, peanut, and soybean. The
cortex and embryo of cereal grains also contain high levels of the two compounds.
(1) Structure.
Both nicotinic acid and nicotinamide are the derivates of pyridine and their structures are
shown in Figure 6-16.
(2) Properties.
Both nicotinic acid and nicotinamide are colorless needle crystals. Nicotinic acid melts in
235.5-236°C. It is sparingly soluble in water but readily soluble in ethanol. The melting point
of nicotinamide is 129-131°C and the compound is readily water soluble. Nicotinic acid is the
most stable among all the vitamins identified and is not destroyed by light, air, heating, acids,
or bases. Nicotinamide is converted to nicotinic acid in acidic solutions upon heating.
208 Yibin Zhou, Dongfeng Wang and Ping Dong
Nicotinic acid can react with cyanogen bromide to yield a yellow-green compound. This
reaction has been used for the quantitative analysis of nicotinic acid and nicotinamide.
The double bond between C4 and C5 can be reduced. Hence, the two compounds can be
present either in oxidized or reduced form.
Nicotinamide implements its in vivo function as nicotinamide dinucleotide (NAD, also
known as coenzyme I) or nicotinamide dinuclotide phosphate (NADP, CoII). NADP can be
converted from NAD by phosphorylation with ATP.
(3) Physiological functions and deficiency.
Nicotinamide is a main component of CoI and CoII, which are the coenzymes of many
dehydrogenases. Nicotinamide in the two enzymes occur either in the reduced and oxidized
states and the transformation between the two states realize the transfer of hydrogen (Figure
17).
Nicotinamide deficiency results in pellagra. The symptoms in the early phase include
symmetrical dermatitis in hands, cheeks, foreheads and other naked areas, gastrointestinal
disorders, mouth and tongue inflammation, indigestion and diarrhea. If nicotinamide is not
supplemented in time, the patients might suffer neurological disorder and even death.
(4) Stability and degradation.
As mentioned previously, nicotinic acid is the most stable vitamin. However, non-
chemical processing of vegetables, such as dressing and rinsing, can cause loss of this vitamin
as other water-soluble ones. The loss of nicotinic acid of pork and beef during storage is
attributed to biochemical reactions, roasting seems to have no effect the content of nicotinic
acid. No loss of nicotinic acid is detected in processed diary products.
2.9. Vitamin B6
Pyridoxine can be converted to pyridoxal or pyridoxamine and all the three compounds
can be phosphorylated, of which, pyridoxal phosphate and pyridoxamine phosphate (Figure
6-19) are the major active forms of vitamin B6 and they are the coenzymes of amino acid
decarboxylases and amino transferases.
(3) Physiological functions and deficiency.
Vitamin B6 is the coenzyme of amino acid decarboxylases and amino transferases and
participates in many metabolism reactions. Long-term deficiency of vitamin B6 may cause
skin irritation and damage of the central nervous system and hematopoietic organ.
(4) Stability and degradation.
The three members of vitamin B6 exhibit excellent thermal stability, of which,
pridoxamine is the most stable and is selected in food fortification. In the presence of oxygen,
vitamin B6 can be transformed to inactive 4-pyridoxine acid by UV irradiation. Vitamin B6 is
easily degraded in alkaline solutions, but is stable in acidic conditions.
Vitamin B6 can react with amino acids to produce Schiff base when heated (Figure 6-20).
In acidic solutions, the formed Schiff base undergoes further dissociation. In addition, the
Schiff base can rearrange to yield many cyclic compounds.
Vitamin B6 suffers more or less loss during processing. For example, about a half of the
vitamin is lost in sterilized liquid milk and the loss further increases during storage for 7~10
days. High temperature-short time pasteurization (92°C, 2~3s) causes only a loss of 30% in
milk, but the values reaches up to 84% when sterilized in 119~120°C for 13 to 15 min.
210 Yibin Zhou, Dongfeng Wang and Ping Dong
2.10. Vitamin H
Vitamin H is also called biotin and includes α- and β-biotin, of which, the former exists
in yolk and the later in liver. Biotin widely distributes in plant and animal tissues. Most of
vitamin H is bound with proteins and only a little portion occurs in the unbound state. Many
organisms can synthesize biotin on their own. In human body, part of this vitamin is
synthesized by intestinal bacteria.
(1) Structure.
Both the two members of biotin are thionic compounds and they are differentiated by
their side chains, as shown in Figure 6-21.
(2) Properties.
Biotin is a colorless needle crystal and its melting point is 232~233°C. Biotin is soluble
in hot water and ethanol, but is insoluble in ether or chloroform. It is stable against light,
heating, acids, but can be destroyed by high temperatures and oxidants.
(3) Physiological functions and deficiency.
Biotin is the cofactor of many carboxylases. It is the carrier of CO2 in many CO2 fixation
reactions. Because biotin can be synthesized intestinal microorganisms in addition to intake
from foods, biotin deficiency occurs rather occasionally compared with other vitamins. The
symptoms of biotin deficiency include dermatitis, muscle pain, hypersensitivity, fatigue,
anorexia, and slight anemia.
Vitamin B11 is also called as folic acid or folate. Folic acid occurs widely in nature.
Green leaves, liver, kidney, cauliflower, yeast, beef and kernels are found to have high
contents.
(1) Structure.
Vitamin B11 is composed of pteridine, p-aminobenzoic acid and L-glutamate, as shown
in Figure 6-22.
(2) Properties.
Folic acid is a bright yellow crystal and is sparingly soluble in water. It is easily
destroyed by light in aqueous solutions. Caron atoms in positions 5, 6, 7, 8 can be reduced by
NADP·H2, positions to yield tetrahydrogen folic acid (THFA).
THFA is the carrier of many one-carbon groups, such as formyl, formaldehyde, and
methyl and plays important role in the synthesis of proteins and nucleic acids.
(3) Physiological function and deficiency.
Folic acid is involved in the synthesis of proteins and nucleic acids. Its deficiency can
cause blood diseases and the symptoms include pernicious anemia, glossitis and
gastrointestinal problems. Because intestinal bacteria can synthesize folic acid, the incidence
of folic acid deficiency is very low.
(4) Stability and degradation.
Dihydrofolate (FH2) and tetrahydrofolate (FH4) are easily oxidized in air and are
sensitive to pH. The two compounds are the most stable in pH ranges 8-12 and 1-2. In neutral
solution, FH4 and FH2, and folic acid are quickly oxidized to p-aminobenzoyl-L-glutamic
acid (PABG), pteridine, xanthine, 6-methyl pterin and many other pterin derivatives. FH4 is
oxidized more quickly in acidic solutions than in alkaline solutions and its oxidation products
include PABG and 7,8-dihydro-pterin-6-carboxyl aldehyde. Reducing agents, such as thiol
and ascorbic acid, can slow down the oxidation of FH2 and FH4.
The stability of several derivatives of THFA follows the decreasing order of 5-formyl-
tetrahydrofolate > 5-methyl-tetrahydrofolate > 10-methyl-tetrahydrofolate > tetrahydrofolate.
Table 6-11. Loss of folic acid in some foods during processing [11]
The loss of folic acid in foods varies with food species and processing technologies, as
listed in Table 6-10.
Vitamin B12 contains cobalt and is therefore also called cobalamine. To present, at least
five members of this family have been identified, but vitamins B12 sometimes refer solely to
cyanoccbalamin.
Liver has the highest vitamin B12 content, followed by milk, meat, egg, and fish.
Vitamin B12 is not found in plants. Because only bacteria can synthesize vitamin B12,
vitamin B12 in animal tissues derives either from foods or intestinal microbes. Vitamin B12
are bound to proteins in foods and are absorbed only after it is dissociated from the complex
by heating or protease hydrolysis.
(1) Structure.
Vitamins of the B12 family are polycyclic compounds and contain one trivalent cobalt
ion (Figure 6-23). According to the structure the R group, cobalamide is divided into
cyanocobalamin (R = CN), hydroxocobalamin (R = OH), adenosylcobalamin (R = Ado),
nitrosocobalamin (R = nitroso), methylcobalamin (R = CH3), etc.
(2) Properties.
The compounds of the B12 family are pink needle crystals and melt in temperatures higer
than 320°C. The compounds are soluble in water, ethanol and propanol, but insoluble in
chloroform. Vitamin B12 in either crystals or aqueous solutions (pH 4.5~5) are quite stable,
but are readily destroyed strong acids/bases, sunlight, oxidants and reducing agents.
(3) Physiological functions and deficiency.
Vitamins 213
Vitamin B12 is the coenzyme of many enzymes and participates in a variety of reactions.
For example, it is the carrier of methyl and is involved in the biosynthesis of methionine and
thymine. Besides, vitamin B12 increases the bioavailability of folic acid.
Vitamin B12 synthesized by intestinal microbes must combine with the special
mucoprotein (also known as endogenous factor) secreted by gastricism for its adsorption.
Lack of the endogenous factor retard the absorption of vitamin B12 and causes pernicious
anemia and lesions in nervous system, tongue and gastricism.
(4) Stability and degradation.
Vitamin B12 in aqueous solutions is stable in pH range 4~6 in dark environments and
room temperature, but it is quantitatively destroyed in alkaline solutions upon heating.
Reducing agents in low levels protect vitamin B12 from destruction, but those in high
concentrations have opposite effects. Trivalent iron salts can stabilize vitamin B12, but
bivalent iron salts rapidly destroy the vitamin.
Lipoic acid occurs either in the reduced and oxidized forms and their structures are
shown in Figure 6-24). Lipoic acid, which is necessary for the growth of microorganisms and
protozoa and dissolves in water, is generally classified as a vitamin B. Lipoic acid is rich in
liver and yeast, and the human body can synthesize it. Lipoic acid is a coenzyme of pyruvate
dehydrogenase and α-ketoglutarate dehydrogenase, plays the role as acyl transfer.
Lipoic acid is water soluble. It is essential for the growth of microorganisms and protozoa
and is generally considered a member of the B family. Human can synthesize lipoic acid on
their own. Lipoic acid is the coenzyme of pyruvate dehydrogenase and α-ketoglutarate
dehydrogenase and participates in acyl transfer.
2.14. Vitamin C
(1) Structure.
Vitamin C, or ascorbic acid, is an acid derivative of hexose. Vc occurs widely in fresh
fruits and vegetables. Only L-ascorbic acid is bioactive. The structure of vitamin C is shown
in Figure 6-25.
(2) Properties.
Vc is a colorless sliced crystal and melts in 190-192°C. It is soluble in water and ethanol
and its aqueous solutions taste sour. Vc is unstable against heating, sunlight exposure, and
metal ions such as such as Cu2+, Fe3+. However, it is quite stable in oxalic acid or
metaphosphoric acid solutions. Vc is a strong reducing agent and can be reversibly oxidized
to the dehydrogenated form (Figure 6-25). Vitamin C has been widely used as an antioxidant
in the food industry.
L-ascorbic acid can reduce the blue dye 2, 6-dichlorophenol-indophenol to the colorless
leuco and react with 2,4-dinitrophenylhydrazine to yield colored hydrazone. These reactions
can be used for the qualitative and quantitative analysis of Vc.
214 Yibin Zhou, Dongfeng Wang and Ping Dong
R-CO-CO-COOH
Vc has been used as natural antioxidant in foods. For example, because Vc can reduce o-
quinone compounds and thus inhibit enzymatic browning, it has been used as a bread
improver. In addition, Vc can protect folic acid and other oxidizable compounds from
oxidation. Vc is also an effective free radical scavenger. It can remove singlet oxygen,
reducing oxygen and carbon-centered radicals, and regenerate other anti-oxidants such as
copherol. The changes of Vc content during food storage in an indicator of food quality
change. Because Vc is water soluble and is sensitive to heat, pH, and oxygen, processing and
storage cause serious Vc loss in foods. Figure 6-28 shows the effects of heating time on Vc
216 Yibin Zhou, Dongfeng Wang and Ping Dong
content, Figure 6-29 indicates the retention of Vc in various processing methods, and Figure
6-30 illustrates the relationship between Vc destruction rate and aw.
Figure 6-30. Relation between water activity and the rate of Vc destruction. O: Orange juice crystal; ●:
Sucrose solution; : Corn and soybean mixture; □: Wheat flour.
△
Treatment of food materials with sulfur dioxide reduces the loss of Vc. Besides, sugar
and sugar alcohols protect Vc from oxidative degradation, possibly due to their combination
with ions.
Vitamins 217
The contents of various vitamins in foods are affected by many factors, such as maturity
of raw materials, growth environment, soil conditions, fertilizer and water management,
illumination time and intensity, as well as post-harvest or post-slaughter handling. The
properties of the vitamins have been reported by many publications; however, only few
efforts have been made on the changes of the vitamins in complex food systems during
storage and processing. The stability of various vitamins is summarized in Table 6-12.
According to Table 6-13, the maturity of tomato significantly affects the content of Vc.
These enzymes might change the chemical structure and activity of vitamins. For
example, dephosphorylation of VB6, thiamine or riboflavin significantly affects the activities
of the vitamins
The most important factors that affect vitamin stability during storage and processing are
temperature and time, because the activities of enzymes are directly relevant to temperature
and reaction time. For example vitamin C oxidase specifically catalyzes the oxidation of
vitamin C; the loss of beta carotenes in dehydrated food is 15% after storage for 10 days and
the value reaches up to 98% after storage for 60 days.
Foods undergo multiple reactions during storage and processing and these reactions
significantly affect the sensory properties and vitamin contents of the foods. For example,
lipid oxidation produces hydrogen peroxide and epoxide, which initiate the oxidation of
carotenoid, tocopherol, and vitamin C; furthermore, hydrogen peroxide is decomposed to
carbonyl compounds, which can react with thiamine, vitamin B, and pantothenic acid and
lead to loss. In addition, carbonyl compounds generated in non-enzymatic browning of
carbohydrates also partially contribute to the loss of some vitamins. The stability of vitamins
is storage method dependent (Table 6-14).
Cereals are often grinded before further processing. Grinding generates heat and hence is
a potential threat of vitamin stability. Figure 6-31 shows that effect of grinding time
(indicated by flour yield) on the retention of various vitamins.
Rinsing and blanching causes the loss of water-soluble and heat-liable vitamins. For
example, blanching at 100°C for 2 min leads to the loss of 65% of vitamin C in cabbage and
vitamin C is completely lost after the 10 min of blanching. Steaming and boiling lead to
different vitamin losses and water-soluble vitamins are better retained in steaming than in
boiling (Table 6-15).
Vitamins 219
Figure 6-31. Relationship between vitamins retention ratio and wheat flour yield [20].
Various chemicals are often added during the storage and processing of foods and these
compounds affect the stability of some vitamins. For example, decolourants in wheat flour
causes oxidation and consequently loss of some sensitive vitamins; sulfur dioxide, sulphites,
bisulfite, and pyrosulfites are inhibitors of both enzymatic and non-enzymatic browning
reactions and protect vitamin C from oxidation.
Nitrite is added as a color fixative and preservative in bacons. This compound can react
with vitamin C and destroy thiamine and folic acid.
REFERENCES
[1] Chandler, LA; Schwartz, SJ. HPLC separation of cis-trans carotene isomers in fresh
and processed fruits and vegetables. Food Science, 1987, 52, 669-672.
[2] Pesck, CA; Warthesen, JJ. Kinetic model for photoisomerization and concomitant
photo-degradation of ß-carotenes. Journal of Agricultural and Food Chemistry, 1990,
38, 1313-1315.
[3] Dellamonica, ES; McDowell, PE. Comparison of beta-carotene content of dried carrots
prepared by three dehydrated process. Food Technology, 1965, 19, 1597-1599.
[4] Van Niekerk, PJ. Determination of vitamins, in HPLC in Food Analysis. 2nd ed. San
Diego: Academic Press, 1988.
[5] Thompson, JN; Hatina, G. Determination of tocopherols and tocotrienols in foods and
tissues by high performance liquid chromatography. Journal of Liquid
Chromatography, 1979, 2, 327-344.
[6] Herbert, V. Present Knowledge in Nutrition. 6th edition. Washington DC: International
Life Science Institute – Nutrition Foundation, 1988.
[7] Machlin, LJ. Vitamin E in commercial processing on nutrients. In Machlin LM.
Handbook of Vitamins. 2nd ed. New York: Marcel Dekker, 1991
[8] Cort, WM; Borenstein, JH. Nutrient stability of fortified cereal products. Food
Technololgy, 1976, 30, 52-62.
[9] Dennison, DJ; Kirk, J. Storage stability of thiamin and riboflavin in a dehydrated food
system. Journal of Food Processing and Preservation, 1977, 1, 43-54.
[10] Freed, MS; Brenner, S; Wodicka, VO. Prediction of thiamin and ascorbic acid stability
in canned stored foods. Food Technology, 1949, 3, 148-151.
[11] Emilia, L; Jana, K. Vitamin losses: Retention during heat treatment and continual
changes expressed by mathematical models. Journal of Food Composition and
Analysis, 2006, 19, 252–276.
[12] Woodcock, EA; Warthesen, JJ. Riboflavin photochemical degradation in pasta
measured by high performance liquid chromatography. Food Science, 1982, 47, 545-
555.
[13] Weisinger, H; Hinz, HJ. Kinetic and thermodynamic parameters for Schiff base
formation of vitamin B6 derivatives with amino acids. Archives of Biochemistry and
Biophysics, 1984, 235, 34-40.
[14] Bonjour, JP. Biotin. In: Machlin LJ, ed. Handbook of Vitamins. 2nd edition: New York:
Marcel Dekker, 1991.
Vitamins 221
[15] Flavia. NI. Lipoic acid: a unique antioxidant in the detoxification of activated oxygen
species. Plant Physiology and Biochemistry, 2002, 40, 463–470.
[16] Tannenbaum, S. Ascorbic acid. In: Fennema, O. (Ed.), Principles of Food Science Part
I Food Chemistry. Marcel Dekker, New York, 1976, 477–544.
[17] Plank, R. Handbuch der Kältetechnik. Bd. XIV. Berlin: Springer-Verlag, 1966.
[18] Maleski, W; Markakis, P. A research note. Ascorbic acid content of developing tomato
fruit. Journal of Food Science, 1971, 36, 537-539.
[19] Lund, D. Nutritional Evaluation of Food Processing. 3rd editon. New York: Van
Nostrand Reihhold, 1988.
[20] Moran, R. Biotin. Present Knowledge in Nutrition. International chemical form.
Nutrition, 1959, 122, 533-545.
[21] Zhao, H. The loss of vitamin in the process of cooking and food processing. Foreign
medical and hygiene anthology, 2003, 30, 221.
In: Food Chemistry ISBN: 978-1-61942-125-7
Editors: D.Wang, H. Lin, J. Kan et al. © 2012 Nova Science Publishers, Inc.
Chapter 7
MINERALS
ABSTRACT
Among the 92 natural chemical elements identified to present, 81 of them have been
found in human body and 25 elements are found to be essential to life, which are termed
essential minerals. Essential minerals are widely involved in metabolisms in human body
as cofactors or activators of enzymes and some play important role in maintaining
osmotic pressure and cell membrane integrity. Besides, some minerals are important
constituents of human tissues, such as calcium and phosphorus in bone and teeth. This
chapter concerns the classification, distribution, property, and function of minerals and
their occurrence in foods. Besides, the changes of minerals in foods during harvesting,
processing, and storage are also highlighted in this chapter.
1. INTRODUCTION
1.1. Definition and Classification
To present, 115 chemical elements have been discovered, including 23 artificial and 92
natural ones. Of the 115 elements, 81 have been discovered in human bodies. According to
their importance to human body, elements are divided into 3 classes:
Essential elements
Essential elements support the normal biochemical processes of human body. Deficiency
of elements of this class leads to impaired functions of human body and the functions can be
224 Dongfeng Wang, Lina Yu, Haiyan Li et al.
restored in the early stage of the deficiency if the elements are supplemented in time.
Essential elements have special physiologic functions and cannot be replaced by other
minerals. To present, 29 elements have been found essential for the human body, including
oxygen (O), carbon (C), hydrogen (H), nitrogen (N), calcium (Ca), phosphorus (P), potassium
(K), sodium (Na), chlorine (Cl), sulfur (S), magnesium (Mg), ferrum (Fe), fluorine (F), zinc
(Zn), cuprum (Cu), vanadium (V), stannum (Sn), selenium (Se), manganese (Mn), iodine (I),
nickel (Ni), molybdenum (Mo), chromium (Cr), cobalt (Co), bromine (Br), arsenic (As),
silicon (Si), boron (B), and strontium (Sr). The former 11 elements account for up to 99.95%
of the total amount of the 29 elements in human body and are termed main or macro
elements. The remaining 18 elements are trace elements and account for only 0.05% of the
total amount.
Elements of this class are beneficial to the physiological activities of human body when
their contents are in normal levels. However, the elements are toxic when they are present in
high levels. Rubidium (Rb), aluminum (Al), niobium (Nb), zirconium (Zr), lithium (Li), and
some rare earth elements (REEs) belong to this class.
Toxic elements
Toxic elements are also referred to as contamination elements or toxic trace elements.
These elements exert their toxicity even in very low concentrations. Bismuth (Bi), stibium
(Sb), beryllium (Be), cadmium (Cd), mercury (Hg), plumbum (Pb), and thallium (Tl) are
important toxic elements.
The elements except C, H, O, and N are termed minerals. Based on the contents in foods,
minerals are divided into main minerals, trace minerals, and ultra-trace minerals. Main
minerals include Na, K, Ca, P, Mg, S, and Cl; trace minerals include Fe, F, I, Zn, Se, Cu, Mn,
Cr, Mo, Co, and Ni; and ultra-trace minerals include Al, As, Ba, Bi, B, Br, Cd, Cs, Ge, Hg,
Li, Pb, Rb, Sb, Si, Sn, Sm, Ti, Sr, Tl, W, and V.
The toxicity of main elements arranged from left to right in the same period and from top
to bottom in the same group in the element periodic table increases with their atom number
(Figure 7-1). Therefore, the argument that the effect of an element on the biological
eukaryotic cells closely relate to the periodic law of the elements is proposed. The study on
the subgroup elements shows that the change of their optimal concentration stimulated cells
growth with their abundance in the seawater is established (Figure7-2).
Figure 7-1 shows that all the 11 main elements have atom number less than 20 and they
are mainly distributed on the top of the S and P areas in the element periodic table. The
essential trace elements have the tendency to be at the position of the fourth period, especially
at the d and ds areas. Most toxic elements except Be and Ba lie in the bottom of the P area.
The majority of essential trace elements are in the top of the element periodic table and their
atom numbers are less than 35 except I and Mo. Almost all the toxic elements are located in
the lower part of the element periodic table, especially in the fifth and sixth period.
Minerals 225
The distribution of minerals in the environment and human body is displayed in Figure 7-
2. Living organisms have evolved regulatory measures to maintain essential mineral contents
in normal ranges. That is to say, a living organism can maintain a mineral in a constant range
when the element intake is insufficient or excessive.
Figure 7-1. Distribution of macro and trace elements in the element periodic table [8].
Figure7-2. Distribution of elements in the seawater (upper), human body (middle) and crust (lower).
(Data in graph are log c; the unit of c is mg/kg) [5].
Mineral Functions
B Growth promotion and essential for plant growth
F Closely correlated with bone growth
Fe Component of hemoglobin, myoglobin and cytochrome
Zn Involvement in enzyme activity, nucleic acid structure and protein synthesis
I Component of thyroxine
Cu Cofactor of many metalloenzymes
Se Component of glutathione peroxidase and participation in liver function and
muscle metabolism
Mn Activation of enzyme and participation in hematopoiesis
Mo Component of molybdoenzymes
226 Dongfeng Wang, Lina Yu, Haiyan Li et al.
Mineral Functions
Cr Effect of insulin intensive and glucose utilization promotion
Mg Activation of enzyme and component of bone
Si Participation in skeletogeny
P Component of ATP
Co Component of VB12
Ca Component of bone and involvement in neural transmission
S Component of proteins
K Electrochemical and messenger function and extracellular cations
Na Electrochemical and messenger function and extracellular cations
Cl Electrochemical and messenger function and extracellular anions
Table 7-1 lists the functions of main minerals for living organisms.
Minerals play important roles in the human body and their functions often involve
complex mechanisms. The functions of the minerals are affected by their interactions (such as
coordination and antagonism) with other food constituents and the compounds in human
body. For example, P and Ca mutually affect their absorption and their absorption rates are
the highest when the two minerals are present in molar ratio 1:1 in foods. Fe increasingly
antagonizes the absorption of Zn in Fe/Zn ratios range from 1:1 to 22:1 in diets and Zn
reduces the absorption of Cu. Many researches have revealed that both deficiency and
imbalance of minerals cause a number of abnormalities in living organisms.
In contrast to most organic constituents, minerals cannot be synthesized in the human
body and must be ingested from foods and drinking water. Besides, minerals cannot be
metabolized and are repelled from the body by excreting. Therefore, dietary structure
significantly influences the contents of minerals and their proportions in the body.
metabolic antagonist of Cd, competing with Cd for the thiol of metallothionein. Pb is more
poisonous in the absence of Fe and Cr in the diet; Se can complex with Hg and reduce Hg
toxicity. The valence significantly influences the toxicity of metals. As3+ is much more toxic
than As5+; methyl arsenic acid and dimethyl arsenic acid are moderately toxic, while
arsenobetaine and arsenocholine are almost non-toxic. Cr3+ is an essential trace element,
while Cr6+ is toxic and Cr2O72- is a strong carcinogen.
Hence, in evaluating the bioavailability and safety of a mineral in foods, its existence
state must be taken into consideration. Generally, only very few minerals are present as free
ions in foods.
According to the Lewis acid-base theory, metals are Lewis acids which can provide
empty orbitals. Small molecules that are rich in N, S, and O atoms, such as sugars, amino
acids, nucleic acids, chlorophylls, and hemoglobins, contain lone pair electrons and can act as
Lewis bases. Therefore, minerals can form complexes with above-mentioned biomolecules.
α-Amino acids are bidentate ligands and bond to metal ions via an oxygen of the
carboxylic acid group and the nitrogen of the amino group to form a five-membered ring, as
shown in Figure 7-3. Under certain conditions, the side chains of amino acids also participate
in the coordination. In addition to carboxyl terminal peptide and certain groups of amino acid
side chains, the carboxyl in peptide and imino groups are also involved in coordination [10].
O O
C H
N CH2
H2 C Zn
C
N O
H O
Note: Left: Zn(Gly)22H2O, Midmost Glycine tripeptide mineral complex, M = Cu (II) or Ni (II); Right:
Glycine tetrapeptide cupric complex.
for Cu(II) and other divalent minerals and the -OH group plays less role in coordination with
Cu(II). The –OH group on 1-C of GlcNH2GalNH2 is the main coordination group for divalent
minerals, but if the -OH on 1-C is not available due to steric hindrance, such as that in
aminosaccharide derivatives, other –OH groups participate in the coordination. Nagy L et al.
[6] studied the structural parameters of carbohydrate-mineral complexes by EXAFS
(extended X-ray absorption fine structure spectroscopic) and the results are given in Table 7-
2. It could be seen that minerals in foods can form various complexes with carbohydrates and
their derivatives.
Oxalic acid in plant-derived foods is an important mineral chelator. When oxalic acid and
phytic acid are present in high levels in foods, the bioavailability of some essential minerals
and the toxicity of some toxic elements will be significantly reduced.
Phytic acid can form insoluble complexes with Ca, Fe, Mg, Zn and many other minerals.
Besides, phytic acid is also able to form ternary complexes with proteins and minerals. The
reaction not only reduces the bioavailability of proteins, but also weakens the absorption of
minerals. About 10% of P in vegetables cannot be absorbed by bodies because of its
combination with phytic acid. In cereals, the percentage is as high as about 40% and even up
to 90% in some species, as shown in Table 7-3.
The biological functions of certain nucleotides are closely related to minerals. For
example, in the presence of Mg, ATP can be hydrolyzed to ADP and phosphate. All the three
components in nucleotides have the ability to coordinate with minerals and their coordination
capacities decrease in the following order: bases > phosphate groups > pentose. Bases
coordinate with minerals through N-3 of pyrimidine and N-7 of purine base. Ca2+, Mg2+,
Cu2+, Mn2+, Ni2+ and Zn2+ are common coordination minerals for nucleotides. In the case of
coordination with ATP, Ca2+ and Mg2+ bond only to the phosphate groups, whereas Cu2+,
Mn2+, Ni2+ and Zn2+ combine with both phosphate groups and N-7 of adenine. The stability
constants of ATP-divalent minerals follow the following order: Cu2+ > Zn2+ > Co2+ > Mn2+ >
Mg2+ > Ca2+ > Sr2+ > Ba2+ > Ni2+. NMR and Raman spectroscopy reveal that the molar ratio
of the Mg2+-ATP complex is 1:1 (Figure 7-4). 1H-NMR and 31P-NMR indicate that Cu2+
binds to the N-7 of purine or the N-3 of pyrimidine on ATP.
Cu2+, Co2+, Ni2+ and Cd2+ coordinate with the phosphate and N-7 of adenine in ATP in
two ways, with the resultant structures termed macrochelated inner sphere (Figure 7-5A) and
230 Dongfeng Wang, Lina Yu, Haiyan Li et al.
macrochelated outer sphere (Figure 7-5B) respectively. In the former structure, N-7 of
adenine directly binds to the mineral, but the α-phosphate group coordinates through H2O. In
the later structure, N-7 of adenine coordinates with mineral through H2O, whereas the α, β, γ-
phosphate groups directly link with the mineral (Figure 7-5).
a)
b)
Figure 7-5. Two simplified structural models of (ATP) 2-Chelate inner ring (A) and external ring (B)
coordination sphere (M indicates a mineral ion) [7].
Minerals can complex with planar ring ligands in addition to low molecular weight
carbohydrates, amino acids and peptides mentioned above. Take porphyrins as example.
Porphyrins are the derivatives of porphine consisting of four pyrrole rings connected by four
carbon atoms (Figure 7-6a, b). When H atoms in numbered positions of the porphine ring are
replaced by other groups, porphyrins are generated (Table 7-4).
a)
b)
Figure 7-6. Structure of porphine. In (a) and (b), the structure is numbered in
different ways.
232 Dongfeng Wang, Lina Yu, Haiyan Li et al.
Porphyrins Substituents
1 2 3 4 5 6 7
Protoporphyrin IX M V M V M P P
Mesoporphyrin IX M E M E M P P
Deuteroporphyrin IX M H M H M P M
Hematoporphyrin IX M B M B M P P
Spirograhic porphyrin IX M F M V M P P
Corproporphyrin III M P M P M P P
Aetioporphyrin III M E M E M E E
Uroporphyrin III A P A P A P P
Note: A=-CH2COOH, B=-CH (OH) CH3, E=-C2H5, F=-CHO, M=-CH3, H=-H, P=-CH2CH2COOH, V=-
CH=CH2.
Porphyrins can form complexes with Fe2+, Fe3+, Zn2+, Co2+, Cu2+, Mg2+ and other mineral
ions, such as Fe in hemoglobin and Mn in chlorophyll.
Heme (Figure 7-7) consists of an iron atom and a planar porphyrin ring. The iron in the
center is connected with the N-atoms of four pyrrole rings through coordination bonds, and
the fifth coordination point is provided by a histidine residue in globin, and the remaining
sixth coordination point comes from negatively charged atoms in other ligands, such as H2O.
Heme can connect with globin to form myoglobin (Figure 7-8).
Three types of hemes, namely heme a, heme b and heme c, have been found. Heme a is
the prosthetic group of cytochrome c oxidase; heme b is an iron-protoporphyrin IX complex
(Table 7-4) and it is the prosthetic group of hemoglobin, myoglobin, cytochrome b,
cytochrome p-450, catalase and peroxidase; heme c is the prosthetic group of cytochrome c.
Chlorophyll is a green pigment in the higher plants and photosynthetic organisms. It has a
planar molecule and consists of four pyrrole rings connected through the methylene bridge.
The Mg in center is connected with the N-atoms of four pyrrole rings through coordination
bonds (Figure 7-9). Many chlorophyll species have been identified, such as chlorophyll a, b, c
and d, as well as bacteria chlorophyll and chlorobium chlorophyll. Chlorophyll a and b occur
widely in plant-derived foods in the ratio 3:1. Chlorophyll is transformed to pheophytin
during food processing. In acidic conditions, the Mg atom in chlorophyll is replaced by
Minerals 233
hydrogen atoms and the resultant pheophytin is dark olive-brown. Heating accelerates the
transformation. In addition to hydrogen, Mg can also be replaced by other divalent minerals,
such as zinc and copper.
Vitamin B12 consists of a corrin ring and has four pyrrole subunits. Because cobalt is
essential for its bioactivity, Vitamin B12 is also known as cobalamin. Vitamin B12 is a red
crystal and its systematic name is α-(5,6-dimethylbenzimidazolyl)cobamidcyanide. In the
structure, the cobalt atom combines with four inner nitrogen atoms in the corrin ring. If the
sixth coordination site is replaced by cyanide, VB12 is transformed to cyanocobalamin; if the
cyanogroup connected with cobalt is replaced by the hydroxyl group, VB12 is converted to
hydroxocobalamin, which is the ubiquitous form of VB12 in nature. If the cyano group is
replaced by the nitroso group, nitriocobalamin is generated. Nitriocobalamin is found mainly
in some bacteria. The structure of Vitamin B12 is given in Figure 7-10.
Protein consists of amino acids. In addition to peptide bonds, terminal amino groups and
carboxyl groups, as well as some side groups of amino acid residues, such as the hydroxyl
group in serine and threonine, the phenolic hydroxyl group in tyrosine, the carboxyl group in
234 Dongfeng Wang, Lina Yu, Haiyan Li et al.
acidic amino acids, the amino group in basic amino acids, the imidazolyl group in histidine,
the sulfhydryl group in cysteine, and the thioether group in methionine, can coordinate with
minerals. However, only the groups in suitable sites can form complexes with minerals.
Figure 7-11 is the schematic diagram of carboxypeptidase A. Zn2+ coordinates with the
protein constituent through two imidazole groups and a carboxyl group in the protein.
Metals are involved in the activity of a large number of enzymes and such enzymes are
known as metalloenzymes. Zn, Fe, Cu, Mn, Mg, Mo, Co, K, and Ba are the most important
cofactors for such enzymes.
Living organisms synthesize a large variety of proteins for the storage and transport of
minerals.
Minerals 235
Ferritin
Ferritin is mainly distributed in the spleen, liver and bone marrow of animals, as well as
in plants chloroplasts and certain fungi. Its main physiological function is to store unused or
excessively absorbed iron.
Transferrin
Transferrin is mainly distributed in body fluids and cells of vertebrates. A large variety of
transferrins have been identified, such as serotransferrin in serum and lactotransferrin in milk
and lacrimal gland secretion. Serotransferrin is a class of mineral-binding glycoproteins with
molecular weight about 7.7~7.4 × 104. After the transferrin releases all Fe3+ irons, the protein
constituent can combine with other divalent or trivalent ions other than iron, such as Cu2+,
Zn2+, Cr3+, Mn3+, Co3+, and Ga3+.
Iron-sulphur protein
Iron-sulphur proteins are characterized by the presence of the Fe-S chromophore and
their molecular weight is about 10 kD. All the Fe atoms in the proteins have variable valence.
The proteins participate in redox reactions in organism as the electron transfer group and are
involved in biological oxidation, nitrogen fixation and photosynthesis.
Cuprein
Minerallothionein
Metallothionein (MT) was firstly separated from horse kidney in 1957. Later, it was
found that MT is widespread in nearly all organisms. MTs are a category of induced protein
with a molecular weight about 6~10 kD. MTs are characterized by their high Cys contents,
reaching up to 25~35%. The functions of MTs include anti-oxidation, free radicals
scavenging, heavy metal complexing, and mineral storage. The structures of MTs are highly
conserved. Many minerals, such as Cd, Pb and Zn, can induce the synthesis of MTs.
One of the most important functions of MTs is to the alleviate toxicity of heavy metals.
The affinity of MTs to some heavy metals follow the order Cd2+ > Pb2+ > Zn2+. Because the
MT level is positively correlated with contaminant level, it is widely used as an indicator of
environmental pollution.
Capasso, C. et al [1] determined the three-dimensional structure of MT-nc obtained from
the Antarctic fish (Notothenia coriiceps). NMR analysis showed that MT-nc is composed of
the α- and β- domains. The α-domain in the C-terminal consists of eleven Cys residues and
four mineral atoms, and the β-domain in the N-terminal has nine Cys residues and three
mineral atoms (Figure 7-12).
The ninth cystine of MT-nc in the α domain is different from that of mammals.
236 Dongfeng Wang, Lina Yu, Haiyan Li et al.
The terminal amino acid sequence of mammal-derived MTs is CXCC (C denotes Cys, X
denotes any amino acid), while the sequence of fish MT is CXXXCC. This difference
attributes to the different structures of their α domains.
Except few exceptions, the N-terminals of mammal-derived MTs are acetyl Met, and the
carboxyl-terminals are Ala. Each MT molecule contains 20 Cys residues and the Cys residues
are in the same positions. The Cys residues can form five Cys-X-Cys units, one Cys-Cys-X-
Cys-Cys unit and one Cys-X-Cys-Cys unit.
Although the amino acid compositions of MTs in different animal are quite similar, the
MTs differ in the metal binding capacity. Generally, each MT molecule can bind seven
mineral ions and the affinities of some metals to MTs follow the increasing order Zn2+ < Pb2+
< Cd2+ < Cu2+ < Ag+ < Hg+.
a)
b)
a
The main chain composite structure of 31-60 residues in α domain;
b
The main chain composite structure of 2-28 residues in β domain.
Phytochelatins
Phytochelatins are firstly found in plants and have similar metal binding capabilities as
MTs. It is estimated that more than 90% of Cd2+ in plant cells are bound with phytochelatins.
The general formula of phytochelatins is (γ-Glu-Cys)n-Gly. Phytochelatins are major
heavy metal binding peptides in plants and some yeast species. The biosynthesis of
phytochelatins is induced rapidly after exposure to heavy metals, especially Cd2+ and Hg2+.
Heavy metals in living organism are present in both the soluble and insoluble forms, in
which, soluble heavy metals bind mainly to phytochelatins. Phytochelatins from different
crops have the following common characteristics: (1) the molecules have similar structure, as
Minerals 237
shown in Figure 7-14; (2) the Glu residue locates in the N-terminal; (3) the amino acid
connected with Glu-γ-oxo is Cys; (4) the γ-Glu-Cys unit occurs repeatedly in the structure.
Polysaccharides can complex with metals through thiol, amino, and carboxyl groups in
addition to hydroxyls. Complexation with metals enhances the biological functions of
polysaccharides and provides an effective way for removing harmful minerals.
Polysaccharide chains contain a large number of groups for coordination with metals,
such as pectin and alginate of the plated ribbon-type conformation (Figure 7-15). The
conformation of polysaccharides significantly affects the metal-binding capability. In the case
of alginate, Ca2+ facilitates the maintenance of the egg-box conformation, as shown in Figure
7-16.
Ca Ca Ca Ca
3.1.1. Solubility
The transfer and metabolism of most minerals in all biological organisms occur in
aqueous solutions. Therefore, the bioavailability and activity of minerals in foods, to a great
extent, depend on their solubility in water. Mg, Ca and Ba are in the same group (II A) and
their halogenides are readily soluble in water. However, their hydroxids, carbonates,
phosphates, sulphates, oxalates and phytates, are sparingly soluble. Besides, the presence of
phytic acid significantly reduces the bioavailability of some minerals, such as Fe, Zn, Ca, Mg
and Mn.
The solubility of minerals is influenced by pH and other constituents in foods. Generally,
minerals are present in the dissolved state in pH below 6 and their complexation with
proteins, amino acids, organic acids, nucleic acids, nucleotides, peptides and carbohydrates
markedly improve their solubility and bioavailability. Harmful minerals can be removed by
the formation of insoluble complexes. For example, citric acid is sometimes used as a chelator
in lead poisoning treatment.
3.1.3. Activity
The reactivity of an ion in biochemical reactions depends on its activity instead of its
concentration. The definition of the activity of minerals is as follows:
ai= fi·Ci
where: ai denotes the activity of the ion, fi denotes the activity coefficient, and Ci denotes the
ion concentration.
The activity coefficient (fi) increases as the ion concentration decreases. No method has
been developed to determine the accurate activity of minerals in foods.
Because the ion activity is positively correlated with ion concentration, the ion activity
can be presented by ion concentration. Indeed, all mineral-involved biochemical reactions are
related to the concentrations, states, valence state, dietary patterns, and so on (Figure 7-18).
Minerals 239
Figure 7-18. Schematic relationship between biological activity and relative concentration of minerals.
3.2.1. Nutrition
Atomic absorption spectrophotometry is a conventional method for determining the total
content of a mineral in foods. However, the bioavailability and nutritional value of minerals
are affected by multiple factors and the information on the total content is insufficient for
bioavailability and nutrition evaluation. The utilization of minerals is discussed below by
taking Fe as an example.
Fe in diets is present in two forms: heme-iron and non-heme iron. Heme-iron occurs
primarily in animal-derived foods. The heme-iron is bivalent and can be absorbed directly and
stored in intestinal ferritin for human utilization. Non-heme iron is the major form of Fe in
plant-derived foods, such as cereals food, vegetables, fruits and legumes. Non-heme iron is
trivalent and cannot be easily absorbed unless it is reduced to its bivalent form. Some plant-
240 Dongfeng Wang, Lina Yu, Haiyan Li et al.
derived foods contain high contents of phosphates, oxalic acid and tannic acids and these
compounds can precipitate Fe by complexing with it, which further reduces Fe utilization.
The presence of reducing agents in plant-derived foods improves Fe utilization. Generally, the
bioavailability of Fe in animal-derived foods is higher than that in plant-derived foods, as
shown in Figure 7-19.
The utilization of Fe is associated with its sources, existence state and diet structure. For
example, phosphoric acid in milk can precipitate Fe and reduces its utilization; polyphenols in
tea can complex with Fe and affect its utilization; diet with insufficient Cu decreases Fe
absorption, because Cu is essential for hemoglobin synthesis.
The absorption of Fe is also affected by individual or physiological factors. People
suffering Fe deficiency or anemia absorb Fe easily and women generally have a better
absorption than men. Besides, the possibility of Fe deficiency decreases with age increase.
3.2.2. Toxicity
All minerals are toxic when they are present in high levels in foods. In addition to
contents, the toxicity of minerals is also affected by the following factors.
Figure 7-19. Utilization of Fe element in different sources. 1 to 12 represents rice, spinach, beans, corn,
lettuce, wheat, soybean, iron, protein, bovine, fish, hemoglobin, and beef, respectively.
The presence of a metal might enhance or decrease the toxicity of another. For example,
As increases the toxicity of Pb; Cu increases the toxicity of Hg; Cu decreases the toxicity of
Hg; Mo significantly reduces Cu absorption; Co increases the toxicity of S; Se decreases the
toxicity of Cd and Ni; Cd antagonizes the absorption of Zn and Cu.
Valence
The toxicity of an element is closely related its valence. The toxicity of elements depends
on their coordination with biological macromolecules and the valence markedly influences
the coordination. For example, Cr3+ is an essential trace element, while the Cr6+ is highly
toxic.
Chemical form
The toxicity of an element is also related to its chemical forms. For example, the LD50s
(mg/kg) of various arsenides are arsenite 14.0, arsenate 20.0, methyl arsenate 700~1800, 2-
Minerals 241
methyl arsenate 700~2600, arsenocholine 6500 and betaine arsenate complex >10,000. It
could be seen that volatile inorganic arsenic is the most toxic. Arsenocholine and betaine
arsenate are often considered non-toxic.
The poisoning mechanisms of heavy metals are rather complex and affected not only by
their contents in the body, but also by the exposing pathway, metabolism, and health
conditions of ingesters. In general, heavy metals exert their toxicity in one or more of the
following mechanisms:
Heavy metals disrupt the functional groups in biomolecules. For example, Hg(II)
and Ag(II) can bind with –SH of Cys residues in enzymes and block the
participation of –SH in enzymatic reactions.
Heavy metals replace the essential metals in biomolecules. The activity of many
enzymes is closely related to the metal cofactors. The activity of metalloenzymes is
easily destroyed by the replacement of metal factors. For example, Be(II) can
replace the Mg(II) in Mg(II)-containing enzymes.
Heavy metals change the conformation of biomolecules. Heavy metals can bind to
various biomolecules, such as proteins, nucleic acids and change their
conformations. For example, Pb2+, Cd2+ and Ni2+ can bind to double stranded DNA
(dsDNA) and this interaction leads to different modifications in the dsDNA
structure.
Minerals must be in the dissolved state for their nutrition or toxicity. Minerals often occur
as complexes with various organic ligands in foods and the ligands tremendously influence
mineral solubility and bioavailability. For example, Ca in protein-Ca complexes is absorbed
easily, but that in the Ca-oxalic acid complex is insoluble and possibly causes urinary
calculus. The solubility of minerals also depends on the counter ion. For a same heavy metal,
its oxide is less poisonous than its soluble chloride and nitrate. Generally, the counter ion
influences the toxicity of a metal in the following order: Nitrate > Chloride > bromide >
acetate > iodide > perchlorate > sulfate >> phosphate > carbonate > fluoride > hydroxide >
oxides. The solubility of metal salts in aqueous solution decreases with the increase of atomic
weight of the metals.
The physiological functions of minerals are closely related with their valences. Cr3+ plays
an important role in glucose, fat, and cholesterol metabolisms. In contrast, Cr6+ is highly
toxicity and its in vivo transformation to Cr3+ is nearly negligible. When the body
accumulates an excessive amount of Cr6+, poisoning symptoms appear.
242 Dongfeng Wang, Lina Yu, Haiyan Li et al.
The coexistence of other minerals changes the nutrition and toxicity a metal.
Hg, Pb and Cd are well-known toxic metals, but the intake of certain components may
strengthen or weaken their toxicity. For example, lipopolysaccharides increase the
accumulation of Hg in mice and augment the Hg-induced nephrotoxicity.
Content / mg/100g
Food Ca Mg P Na K Fe Zn Cu Se
Fried eggs 57 13 269 290 138 2.1 2.0 0.06 8
Wheat bread 35 6 30 144 31 0.8 0.2 0.04 8
Graham bread 20 26 74 180 50 1.5 1.0 0.10 16
Salt-free macaroni 5 13 38 1 22 1.0 0.4 0.07 19.0
Cooked rice 10 42 81 5 42 0.4 0.6 0.01 13.0
Instant rice 10 42 81 5 42 0.4 0.6 0.01 13.0
Mature black soybean 24 61 120 1 305 2.0 1.0 0.18 7.9
Red cashew 25 40 126 2 356 3.0 0.9 0.21 1.9
Whole milk 291 33 228 120 370 0.1 0.9 0.05 3.0
Skim milk /nonfat milk 302 28 247 126 406 0.1 0.9 0.05 7.6
Ameican cheese 261 10 316 608 69 0.2 1.3 0.01 3.8
Sayda cheese 305 12 219 264 42 0.3 1.3 0.01 7.0
Farmhouse cheese 63 6 139 425 89 0.1 0.4 0.03 7.3
Low fat yogurt 415 10 326 150 531 0.2 2.0 0.10 5.5
Vanilla ice-cream 88 9 67 58 128 0.1 0.7 0.01 4.7
Overbark baked potato 20 55 115 16 844 2.8 0.7 0.62 1.8
Underbark boiling otato 10 26 54 7 443 0.4 0.4 0.23 1.2
Palm cabbage, crude stem 216 114 297 123 1470 4.0 2.0 0.40 0.9
Palm cabbage, cooked stem 249 130 318 141 1575 4.5 2.1 0.23 1.1
Crude shattering carrot 15 8 24 19 178 0.3 0.1 0.03 0.8
Cooked freezing carrot 21 7 19 43 115 0.4 0.2 0.05 0.9
Fresh entire tomato 6 14 30 11 273 0.6 0.1 0.09 0.6
Canned tomato juice 17 20 35 661 403 1.0 0.3 0.18 0.4
Attains (defrosting) 17 18 30 2 356 0.2 0.1 0.08 0.4
Attains 52 13 18 0 237 0.1 0.1 0.06 1.2
Apple (skin) 10 6 10 1 159 0.3 0.1 0.06 0.6
Banana (peeling) 7 32 22 1 451 0.4 0.2 0.12 1.1
Roasted beef (cans) 5 21 176 50 305 1.6 3.7 0.08 —
Roasted veal (cans) 6 28 234 68 389 0.9 3.0 0.13 —
Roasted chicken breast 13 25 194 62 218 0.9 0.8 0.04 —
Roasted chicken drumstick 10 20 156 77 206 1.1 2.4 0.07 —
Cooked salmon 6 26 234 56 319 0.5 0.4 0.06 —
Canned salmon with bone 203 25 277 458 231 0.9 0.9 0.07 —
Minerals 243
The contents of minerals in plant-derived foods are subject to the influences of soil, water
and fertilizer management, antagonistic effect among minerals and climate. As shown in
Table 7-6, the contents of some minerals in black glutinous rice of three different provinces in
China differ greatly.
The contents of minerals in animal-derived foods depend on feed, animal health status
and environment, in which, the mineral content of feed is the most important determinant. As
shown in Table 7-7, the supplementation of trace elements in feed markedly increases the
contents of K, Ca, and P in milk.
Processing method, water used, processing equipment, and food additives also change the
contents of minerals in foods.
Table 7-8 lists the effects of four processing methods on the mineral contents of instant
fiddlehead. It could be seen that the four treatments slightly increase the contents of Ca, but
more or less decrease the contents of other minerals, of which, salting-out dehydration plus
blanching leads to the highest loss of Mg, Mn, and Zn, and salting-out dehydration without
blanching causes most Fe and Cu losses.
Table 7-9 illustrates the loss of some minerals in spinach after blanching. K and Na suffer
the highest loss after blanching, but the Ca content is nearly not affected. Hence, minerals in
free state, such as K and Na, are lost easily during bleaching, but minerals occuring in
insoluble state (such as Ca) are not lost.
Table 7-6. Contents of some minerals in black glutinous rice sampled from three
provinces in China (mg/100g)
producing area Zn Cu Fe Mn Ca Mg
Hunan 19.48 1.779 17.18 15.46 27.59 12.27
Zhejiang 19.47 2.549 20.13 24.25 59.48 12.00
Guizhou 17.64 0.702 24.97 25.36 32.00 11.42
244 Dongfeng Wang, Lina Yu, Haiyan Li et al.
Table 7-7. Effect of trace element supplementation in cattle feed on the minerals content
of milk (mg/100g)
Fe Cu Zn Mn K Na Ca Mg P
Experimental group 0.122 0.032 0.417 0.008 81.60 83.70 144.0 11.00 98.60
Control group 0.137 0.007 0.442 0.010 68.39 85.34 77.67 10.06 82.09
Table 7-8. Effect of different processing methods on some trace elements content in
instant fiddlehead (mg/100g dry weight)
Processing methods Ca Mg Fe Mn Cu Zn
Before processing 62.5 238.0 32.0 8.1 27.4 9.5
(1) 80.0 140.9 30.6 7.3 22.4 7.1
(2) 80.1 169.5 21.1 7.3 20.3 7.0
(3) 80.6 127.0 27.6 5.1 20.2 5.7
(4) 88.0 157.3 20.7 7.7 15.5 7.9
Note: (1) natural dehydration plus blanching; (2) natural dehydration without blanching; (3) salting-out
dehydration plus blanching; (4) salting-out dehydration without blanching.
g/100g
Mineral Loss (%)
Not steam blanching Steam blanching
K 7.9 3.0 56
Na 0.5 0.3 43
Ca 2.2 2.3 0
Mg 0.3 0.2 36
P 0.6 0.4 36
Nitrite 2.5 0.8 70
Fluctuati Fluctuati
Processing method Cu Processing method Cu
on (%) on (%)
Material 0.21 0.00 Potato mesh 0.10 -52.38
Water boiling 0.10 -52.38 French frying potato crisp 0.27 +28.57
Baking 0.18 -14.29 Fast potato 0.17 -19.05
Potato chip 0.29 +37.20 Peeling potato 0.34 +61.90
The effect of processing method on Cu content in potato shown in Table 7-10. Cu content
is slightly increased in the frying potato crisp and peeling potato.
Minerals 245
Minerals in foods can migrate from packaging materials. The contents of some minerals
in canned liquid and solid foods are given in Table 7-11. The contents of Al, Sn and Fe in
solid foods are evidently increased because solid foods repeatedly collide with the packing
material.
REFERENCES
[1] Capasso, C; Carginale, V. Solution structure of MT-nc, a Novel Metallothionein from
the Antarctic Fish Notothenia coriiceps. Structure, 2003, 11, 435-443.
[2] ESHA Research. The Food Processor Plus, ESHA Research, Salem, OR, 1992.
[3] Ji, L; Huang, J; Mo, T. Bioinorganic Chemistry an Introduction (Second), Guangdong:
Zhongshan University Press, 2001
[4] Kan, JQ. Food Chemistry. Beijing: China Agricultural University Press; 2008.
[5] Liu, Y. An idea on trace elements as nutrients of organism. Journal of Peking University
(Natural Science), 1986, (3): 121.
[6] Nagy, L; Szorcsik, A. Equilibrium and structural studies on metal complexes of
carbohydrates and their derivatives. Journal of Inorganic Biochemistry, 2002, 89, 1-12.
[7] Sigel, H; Sigel, A. Metal Ions in Biological Systems. 1st edition. New York: Marcel
Dekker, 1995.
[8] Tang Renhuan. On the Biological Element Spectrum in Organism. Acta Scientiarum
Naturalium Universitatis Pekinensis, 1996, 32, 790-803.
[9] U. S. Department of Agriculture (1976-1986). Composition of Foods. Agriculture
Handbook Nos.8-1 to 8-16. Human Nutrition Information Service, USDA, Hyattsville,
MD.
[10] Yang, P. Introduction of Bioinorganic Chemistry, Xi‘an: Xi‘an Jiaotong University
Press, 1991.
In: Food Chemistry ISBN: 978-1-61942-125-7
Editors: D.Wang, H. Lin, J. Kan et al. © 2012 Nova Science Publishers, Inc.
Chapter 8
FOOD FLAVORS
ABSTRACT
The special tastes or aromas of foods are contributed by abundant small-molecular
weight compounds and these compounds significantly affect the acceptability of foods by
consumers. This chapter firstly concerns the major tastes and their perception by human
beings. Then, the major flavor compounds in various foods, including fruits, vegetables,
and meats are elucidated in detail. Besides, reactions that contribute to the formation of
flavors during food processing and storage are also presented in detail in this chapter.
Foods should not only meet the needs of consumers on nutrition, but also provide
desirable flavors so that consumers can enjoy the foods. Flavor is an important aspect that
determines food quality, and affects the intake and absorption of nutrients in foods.
Flavor is an overall integrated perception of all contributing senses (smell, taste, sight,
feeling, and sound) at the time of food consumption. The evaluation and preference to
flavors differ significantly among individuals, areas, and ethnics. Flavor together with
nutritional value and security determine consumers‘ acceptance of foods.
The flavor of food is contributed by multiple compounds in addition to
environmental factors. The development of modern analysis techniques, such as
chromatography and mass spectrometry, provides great convenience for further study of
food flavor. However, since food flavor is a physiological perception, neither qualitative
nor quantitative methods can accurately measure or describe a food flavor yet.
248 Xiaoxiong Zeng and Guaoqing Huang
Food Taste
A taste is a feeling caused by the stimulation of food compounds on taste receptors in the
mouth. Taste buds are the most important taste receptors in the mouth, followed by free nerve
endings. Taste buds locate on the surface of the tongue and the back of the oral cavity. Each
taste bud is the cluster of approximately 30-50 taste cells and taste receptors are distributed on
the membranes of these cells. Each taste bud is connected to the oral cavity through a hole on
the top. When foods are ingested, the taste compounds get contact with the corresponding
receptors in the taste cells through the hole and consequently a taste is perceived. Free nerve
ending acts as a micro-receiver and can identify different chemical substances. It is scattered
in the entire oral cavity and surrounded by sacs.
Different parts of the tongue are sensitive to different tastes. Each of the primary tastes is
associated with a specific area in the tongue. The tip of the tongue is most sensitive to sweet
and salty tastes, while sour seems to register more strongly on the sides of the tongue. Far to
the rear of the tongue are most of the receptors for bitter tastes.
The sensitivity to a taste is often described by threshold, which is the lowest
concentration required for eliciting a sensation. Threshold values are usually determined
using individuals representative of the general populations, and each panelist indicates
whether or not the compound can be detected. The concentration range where at least half
(sometimes greater) of the panelists can detect the compound is designated as the flavor
threshold. Table 8-1 lists the threshold values of some taste compounds.
Three kinds of threshold value are proposed based on measurement methods. Absolute
threshold value, also called sensory threshold value, is the lowest level of a taste compound
that can be perceived. It is determined by tasting a series of diluted taste compound solutions.
Differential threshold value is the smallest change in taste compound concentration that
consumers can detect. Terminal threshold value is the minimum concentration of a taste
compound, whose further increase does not enhance the perception. In this chapter, all
thresholds value mentioned refer to the absolute threshold value, except special instructions.
Taste classification.
Different taste classifications have been proposed due to the differences in culture and
dietary habits. In Japan, the primary tastes include sweet, sour, bitter, salty and pungent. In
European and American countries, six primary food tastes are identified, including sweet,
sour, bitter, salty, pungent, and astringent. In India, up to eight tastes are recognized as
primary tastes and they are sweet, sour, bitter, salty, pungent, insipid, astringent and
abnormal. In China, the original standard specifies only five primary tastes, including sweet,
sour, bitter, salty and pungent, but the astringent and delicious tastes are added later. From the
physiological point of view, only the sweet, sour, bitter and salty tastes can be perceived by
taste receptors. The pungent taste is the pain feeling when pungent substances stimulate oral
mucosa, nasal mucosa, skin and trigeminal nerve. The astringent taste is the response of
tactile nerves to protein aggregation. Both the tastes affect the flavor of foods independently.
The presence of delicious compounds enhances the sensation of other tastes. In European and
American countries, the delicious taste is excluded from the primary tastes.
Food Flavors 249
The perception of tastes is affected by many factors. In addition to dietary habits, health
status, age and other individual factors, taste perception is also affected by the following:
Temperature: the optimum temperature for taste sensation is between 10-40 °C and taste
receptors are the most sensitive at 30 °C. When the temperature is lower than 10 °C or higher
than 50 °C, the sensation becomes dull. It can be seen from Table 8-1 that the salty taste is the
most sensitive to temperature variation and the sour taste of citric acid is the least sensitive.
Solubility: the intensity of a taste is related to the solubility of the taste compound,
because taste receptors or free nerve endings are stimulated only by dissolved compounds.
Threshold (%)
Taste compounds Taste
25 °C 0 °C
Quinine sulfate Bitter 1.0×10-4 3.0×10-4
Sucrose Sweet 0.1 0.4
Sodium chloride Salty 0.05 0.25
Citrate Sour 2.5×10-3 3.0×10-3
Generally, taste compounds that dissolve quickly are perceived in a very short time and
the sensation disappears very fast. For example, sucrose is readily soluble. Its sweetness is
perceived rapidly after ingestion, but the sensation lasts only a short time. In contrast, the
sweetness of saccharin is perceived slowly, but the sensation can last for a relative long time.
Presence of other taste compounds: Interactions might occur between different taste
compounds.
a. Enhancing: the presence of a taste compound could enhance the intensity of another
taste. For example, table salt in concentration 0.017% enhances the sweetness of
sucrose solution (15 %).
b. Modification: the presence of a taste compound might change the taste of another
compound. For example, water tastes sweet if table salt or quinine has been
perceived before.
c. Elimination: the presence of a taste compound reduces or eliminates the intensity of
another taste. For example, any one of sucrose, citric acid, table salt, and quinine can
reduce the taste intensity of the other three compounds. In wines or beverages, the
sweetness of sugars weakens the sour taste and vice versa.
d. Multiplication: when two taste compounds are present at the same time, the intensity
of the tastes increases significantly. For example, the mixture of sodium glutamate
and 5‘-inosinic acid has markedly improved delicious taste than alone and maltol
significantly enhances the sweet taste in beverages and candies.
e. Adaptation: adaptation refers to the gradual decline of taste intensity with prolonged
stimulation. The time required for the recovery of taste sensation varies with tastes.
The time needed for recovery of sour taste sensation after adaptation is 1.5~3 min
and that for sweetness, bitterness, and salty is 1~5 min, 1.5~2.5 min and 0.3-2 min
respectively.
250 Xiaoxiong Zeng and Guaoqing Huang
The interactions between tastes are very complicated and are affected by both
psychological and physicochemical factors. The mechanisms involved are not well
understood yet to present.
Sweet Taste
Sweetness is the most popular taste for consumers. It improves the palatability and
certain properties of foods. The intensity of sweetness is expressed in relative sweetness by
using 10 % sucrose solution as reference. Table 8-2 lists the relative sweetness of several
sweeteners.
The mechanism of sweet taste can be explained by the AH/B through proposed by Robert
Shallenberger and Terry Acree in 1963. It is supposed that the initial event in the perception
of sweetness is the hydrogen bonding of a stimulant to receptors on the tongue. Each sweet
compound possesses an electronegative atom A (usually N or O) covalently connected with a
hydrogen atom (AH). Hence, the AH can be hydroxyl (-OH), imino (-NH) or amino (-NH2)
group. AH functions as the proton donor. The sweet compound contains another
electronegative atom B (usually N, O, S, or Cl), which is 0.25-0.4 nm away from the AH
group and acts as the proton receptor. The sweetness receptor contains the AH/B unit. When
the AH/B unit of a sweet compound binds to the AH/B unit in the receptor through hydrogen
bonding, the taste nerve is stimulated and the sweet taste is perceived. Figure 8-1 shows the
AH/B structure of chloroform, saccharin and glucose.
This theory has been successfully used to explain the sweet sensation of many
compounds. However, this theory has some limitations. It can not explain why the sweet
intensities of sugars and D-amino acids that contain the AH/B structure differ significantly
and why the optical isomers of amino acids have different tastes.
Relative
Sweetener Sweetener Relative sweetness
sweetness
β-D-fructose 1.0-1.75 D-tryptophan 35
α-D-glucose 0.40-0.79 glycyrrhizic acid 200-250
α-D-galactose 0.27 saccharin 200-700
β-D-mannose 0.59 Naringin dihydrochalcone 100
Sweet receptor
Figure 8-2. Schematic showing the relationship between AH/B and γ sites in the saporous sweet unit for
β-D-fructopyranose [1].
To solve these problems, Kier extended the AH/B theory. He proposed that each sweet
compound also contains a lipophilic region γ in addition to the AH/B structure. The lipophilic
region might be methylene (-CH2-), methyl (-CH3) or phenyl (-C6H5) groups. All the three
active units (AH, B and region γ) must be arranged correctly in space so that the units can
contact with receptor molecules. The relationship between the three groups can be illustrated
in Figure 8-2.
Bitter Taste
The bitter taste is unpleasant on its own, but its combination with other tastes can provide
foods with special flavor, such as in tea, coffee, beer, and balsam pear. Strychnine is the
bitterest substance (threshold 0.0016 %) ever found and quinine is often used as reference in
the assessment of bitter intensity of other substance.
The sensation of the bitter taste is similar to that of the sweet taste. Bitter compounds
posses the AH/B entity and can interact with receptors through hydrogen bonding. The
difference is that the proton donor (AH) in bitter compounds are –OH, –C(OH)COCH3, –
CHCOOCH3, or –NH and the proton donor (B) is –CHO, –COOH, or –COOCH3. In addition,
the distance between AH and B is 0.15 nm, which is much less than that in sweet compounds.
Naturally occurring bitter compounds are alkaloids, terpenoids, and glycosides in plants
and bile in animals.
Caffeine, theobromine, theophylline: caffeine, theobromine and theophylline are
derivatives of purine and are important bitter substances in foods. Caffeine occurs in tea,
coffee and cacao, and theophylline is found in cacao and tea (Figure 8-3). All the three
alkaloids can stimulate the central nervous system.
Naringin and neohesperidin: naringin and neohesperidin are main bitter taste compounds
in citrus fruits and are mainly distributed in the peel of the fruits. Both the two compounds are
flavanone glycosides and are water soluble. The bitterness of naringin is related to the l→2
glycosidic bond between rhamnose and glucose. Enzymatic hydrolysis of the linkage yields
products without bitterness (Figure 8-4).
252 Xiaoxiong Zeng and Guaoqing Huang
R1 N N R3 R1=R2=R3=CH3 caffeine
R1=H R2=R3=CH3 theobromine
R1=R2= CH3 R3= H theophylline
O N N
R2
Enzyme
R3
COOH
R1=R2=OH R3=H chenocholic acid
R1=R3=OH R2=H deoxycholic acid
R1=R2=R3= OH cholic acid
R1 R2
Figure 8-6. Structures chenocholic acid, deoxycholic acid and cholic acid.
Bitter substance in beer: the bitter taste of beer is contributed by the bitter substances
originally contained in hops and those generated during brewing. The major bitter substances
in beer are α-acids, such as humulone, cohumulone, adhumulone. Hops are often added as the
mashed malted barely (or malt extract) is boiled in water. During this boiling process the
modestly bitter α-acids undergo thermal isomerization to form extremely bitter iso-α-acids.
(Figure 8-5).
Bile acid: bile acid is an extremely bitter fluid secreted by the liver of most vertebrates. It
is involved in the digestion of lipids in the small intestine and the adsorption of fat-soluble
vitamins. The major bitter compounds in bile acid are chenocholic acid, deoxycholic acid, and
cholic acid (Figure 8-6). If bile acid leaks from gallbladder during the processing of livestock,
poultry and aquatic products, the bitter taste cannot be removed even after repeated washing.
Food Flavors 253
Sour Taste
The sour taste is produced by hydrogen ion of organic acid, inorganic acids and acidic
salts. Moderate sour intensity yields pleasant sensation and enhances appetite. Generally, the
intensity of the sour taste is positively related to the concentration of hydrogen ion in
solutions. When the H+ concentration is too high (pH <3.0), the sour taste becomes
intolerable and sour intensity changes can no longer be perceived. The sensation of the sour
taste is affected by counter ion species and the buffering capacity of food medium. For
example, the sour intensities of five common acids in the same pH are in the following
decreasing order: acetate acid > formic acid > lactic acid > oxalate acid > hydrochloride yield.
Anions decide the characteristics of the sour taste, which is why the sour taste of sour
compounds differs.
Acidulants are important additives in food processing. The compounds not only impart
foods with desired sour taste, but also inhibit the growth of microorganisms. The most
commonly used acidulant in food industry is acetic acid, followed by citric acid, lactic acid,
tartaric acid, gluconic acid, malic acid, fumaric acid and phosphoric acid. Acetic acid is the
major active component of vinegar. Citric acid is the most widely used acidulant in food
industry. Malic acid is used to mask the lingering bitterness of synthetic sweeteners. Gluconic
acid-δ-lactone can produce gluconic acid upon heating and is hence a slow-acting acidulant. It
can be used as leavening agent in biscuit processing and curing agent in tofu preparation.
Phosphoric acid is mainly used in the production of cola-type beverages.
Salty Taste
The salty taste is contributed by neutral salts and it is an indispensable and the most
fundamental taste in foods. This taste is the compromise of the effects of dissociated anions
and cations. Cations produce salty taste, while anions suppress the sensation of salty taste and
elicit other undesirable tastes. Whether an inorganic salt is bitter or salty depends on the
diameters of cations and anions. If the sum of the diameters of cation and anion of a
compound is less than 0.65 nm, the salt tastes salty; otherwise, the salt tastes bitter. For
example, the sum of the diameters of Mg2+ and Cl- is 0.85 nm and MgCl2 tastes quite bitter.
L-sodium
L-sodium glutamate
glutamate (MSG) (MSG) Inosine-5‘-monophate
Inosine-5'- (5‘-IMP).
monophosphate (5′-IMP)
Sodium chloride is the only substance known to evoke a purely salty taste in any
concentration that is suprathreshold. The optimum concentration of NaCl in liquid foods is
0.8-1.2 %. Because excessive intake of NaCl can cause negative impacts on health, the
development of NaCl substitutes has attracted much attention. For example, a mixture of 20
% of KCl and 80 % NaCl has been developed as a low-sodium salt.
Delicious Flavor
The delicious flavor is a very complex sensation. The flavor enhances the appetite of
consumers and makes foods tasted more delicious. When the concentration of a delicious
254 Xiaoxiong Zeng and Guaoqing Huang
compound in foods is higher than threshold value, it evidently increases the delicious taste of
the food, and enhances the original flavor of the food even its concentration is lower than its
threshold value. Hence, delicious compounds are also known as flavor enhancers.
Delicious compounds can be divided into amino acid, nucleotide and organic acid types
and their typical representatives are L-sodium glutamate (MSG), 5‘-inosine monophosphate
(5‘-IMP), and sodium succinate respectively. MSG is the first discovered and commercially
available flavor enhancer. It occurs widely in nature and is abundant in kelps. 5‘-IMP is
widely found in chickens, fishes and broths and 5‘-IMP in animals is mainly generated by the
degradation of ATP in muscles. 5‘-Guanosine monophosphate (5‘-GMP) is the major
delicious component in mushrooms. Sodium succinate has been identified in poultry,
livestock and mollusks and the highest content is detected in shellfishes. It is also present in
low levels in fermented products, such as soy sauce, sauce, and yellow rice wine. Aspartic
acid and its sodium salt are the main delicious substances in bamboo shoots, though their
intensities are lower than that of MSG. The combination of IMP, GMP and MSG
significantly enhance the delicious taste of MSG. For instance, the delicious intensity of the
mixture containing 1 % IMP, 1 % GMP, and 98 % MSG is four times of that of MSG alone.
Pungency
Certain compounds found in some spices and vegetables cause characteristic hot, sharp
and stinging sensations that are known collectively as pungency. Pungent compounds
enhance the appetite and increase the secretion of digestive juice of consumers and they are
indispensable condiments in daily life. Based on sensation, natural pungent compounds are
divided into hot, aromatic and irritative types.
Hot compounds: pungent compounds of this type are odorless and can cause the burning
feeling in mouth. The pungent compounds in chili, black pepper and zanthoxylum belong to
this type.
Chili.
Capsaicinoids are the vanillyl amides of monocarboxylic acids with varying chain length
(C8~C11) and capsaicin is the active component in chili pepper. The contents of capsaicin in
chili peppers vary significantly with species. The contents of capsaicin in red chili, horn red
chili, Sam chili, and Uganda chili are 0.06 %, 0.2 %, 0.3 %, and 0.85 %, respectively.
Capsaicin
Black pepper.
high pungency intensity. The liability of black pepper to light and storage is due to the
isomerization of piperine isomers.
Pipirine
The main pungent compound in Chinese prickly ash is suberosin and it also an amide
compound.
Aromatic compounds: pungent compounds of this type are volatile and aromatic.
Ginger.
Zingiberols are the main active components responsible for the pungency of fresh ginger.
The carbon chain length on the lateral side of hydroxyl in the side chain on the ring is
different (n=5-9). When fresh ginger is dried, zingiberols are converted to more pungent
gingerols through dehydration. When ginger is heated, the side chain of zingiberols breaks to
produce zingerone, which is a moderate pungent compound.
The main pungent components in the two species are eugenol and isoeugenol
respectively.
Eugenol Isoeugenol
Irritative compounds: in addition to tongue and oral mucosa, compounds of this type are
also irritative to nose and eyes.
256 Xiaoxiong Zeng and Guaoqing Huang
The pungency and irritability of these materials are contributed by mustard oil that is
generated through the hydrolysis of sinigrin. It is the collective of isothiocyanate. The
following active substances have been identified in mustard, radish, and horseradish:
Disulfides are the major pungent and irritative substances in welsh onion, garlic, leek,
and onion. The pungent components of garlic are generated by the decomposition of alliin
and include diallyl disulfide and allyl propyl disulfide. The pungent components in leek and
onion are also sulfur-containing compounds. These substances are converted to sweet thiol
compounds when heated. This is why cooked onion and garlic taste sweet other than pungent.
Astringency
Astringency is the sensation of the aggregation of proteins in oral mucosa. Tannins and
polyphenols are major components in foods that cause astringency. Besides, some salts (such
as alum), aldehydes, organic acids (such as oxalic acid), and quinine acid are sometimes also
involved in astringency sensation. Mature fruits taste less astringent than immature fruits,
because polyphenols are decomposed, oxidized, or polymerized during maturation. Tea also
contains polyphenols, but their contents vary with processing methods. Red tea is less
astringent than green tea, because polyphenols are oxidized during fermentation. Astringency
is a characteristic taste of red wine. To obtain an acceptable astringency, measures must be
taken to reduce the contents of polyphenols in wines.
Fruits
The characteristic aromas of fruits are mainly contributed by esters, aldehydes and
terpenes, followed by alcohols, ethers and volatile acids. The contents of these compounds
increase gradually as fruits get mature. Table 8-3 lists the aromatic compounds in some fruits.
Vegetables
Generally speaking, the intensity of the aroma of vegetables is weaker than that of fruits.
However, some vegetable, such as onion, garlic, leek, and onion, possess unique and strong
aromas.
Food Flavors 257
Fresh vegetables.
Many fresh vegetables have the smell of soil. This aroma is generated by methoxy alkyl
pyrazines, such as 2-methoxy-3-isopropyl pyrazine in fresh tomato and pee, 2-methoxy-3-
isobutyl pyrazine in green pepper, and 2-methoxy-3-sec-butyl pyrazine in red beet root. These
compounds are synthesized from the precursor leucine. The biosynthesis pathway of pyrazine
compounds in plants is shown in Figure 8-7.
enzyme
leucine
2-methoxy-3-isobutyl
pyrazine
Figure 8-7. Biosynthesis pathway of methoxy alkyl pyrazines in plant tissues [3].
acetone alkyl
garlic alcohol ammonia
1-allyl-1-subsurfuracid
S-propionaldehyde-S-oxidate
Figure 8-9. Reactions involved in the formation of garlic flavor compounds [5].
Mushroom.
The aroma precursor of mushrooms is lenthionine acid. The precursor can be hydrolyzed
by S-alkyl-L-cysteine sulfoxide lyase to produce the aromatic lenthionine (Figure 8-11). In
addition, benzyl isothiocyanate, phenethyl isothiocyanate, and benzaldehyde cyanohydrin are
also involved in the aroma formation of mushroom.
Other vegetables.
The major aromatic compounds in cucumber are carbonyl substances and alcohols and its
characteristic aroma is contributed by 2-trans-6-cis-nonadienal, trans-2-nonene aldehyde and
2-trans-6-cis-nonadienol. Besides, 3-cis-hexenal, 2-trans-hexenal, and 2-trans-nonnenal also
affect the aroma of cucumber. These flavor compounds are synthesized from linoleic acid and
linolenic acid.
More than 80 kinds of volatile compounds have been identified in tomato, in which, 3-
cis-hexenal, 2-trans-hexenal, β-ionone, hexanal, β-damascenone, 1-penten-3-one, 3-methyl
butyraldehyde, are major active compounds for tomato aroma. In heated products such as
260 Xiaoxiong Zeng and Guaoqing Huang
ketchup, the aroma changes due to the formation of dimethyl sulfide, the increase of β-
ionone, β-damascenone and the decrease of 3-cis-hexenal and hexanal.
Potato contains only trace amounts of aromatic compounds. Pyrazines, including 2-
isopropyl-3-methoxy-pyrazine, 3-ethyl-2-methoxy-pyrazine and 2, 5-dimethoxy-pyrazine, are
the major active components in fresh potato. Volatile compounds in cooked potato are
carbonyl compounds (including saturated and unsaturated aldehydes, ketones and aromatic
aldehydes), alcohols (C3~C8 alcohols, linalool, neroli and geraniol), sulfur compounds
(mercaptan, sulfide and thiazole) and furan compounds.
A large variety of terpenes have been identified in the volatile oil of carrot, mainly
including γ-bisabolene, caryophyllene, and terpinolene. cis-γ-Bisabolene, trans-γ-bisabolene
and hypoxanthine contribute to the characteristic smell of carrot.
Green tea does not undergo fermentation during processing and exhibits the typical
roasted and fresh smell. The first step of green tea processing is water removing and enzymes
are deactivated in this step. Hence, most aromatic components of green tea are original from
fresh leaves and only a few are formed during processing.
The main volatile components in fresh tea leaves are leaf alcohols (3-cis-hexenol, 2-cis-
hexenol) and leaf aldehydes (3-cis-hexenal and 2-cis-hexenal), which have a strong flavor of
grass. During processing, part low boiling point substances, such as leaf alcohols and leaf
aldehydes, are evaporated, while part leaf alcohols and leaf aldehydes are isomerized to trans-
leaf alcohols and trans-leaf aldehydes. These products have the faint scent and are the main
body of the aroma of green tea. The smells of high boiling point aromatic compounds, such as
linalool, benzyl alcohol, phenylethanol, and acetophenone, get exposed with the volatilization
of low boiling point substances. Linalool is an important active component and accounts for
10 % of total aromatic components in green tea. These high boiling point compounds have
pleasant smells and are important aromatic substances of green tea.
The characteristic aroma of teas harvested right before or after Ching Ming Festival is
contributed by disulfide ether and leaf alcohols and the aroma disappear gradually during
prolonged storage.
Semi-fermented tea.
Oolong tea is the representative of semi-fermented tea and its major aromatic components
include leaf alcohol, cis-jasmone, jasmine lactone, methyl jasmonate, nerolidol, benzyl
alcohol cyanohydrin, and ethyl acetate.
Food Flavors 261
CH2COOCH 3 HO CH CN
CH 2CH=CHCH 2CH3
OH
O O
O O
Red tea
Red tea undergoes fermentation during processing and has strong aroma. During
processing, tremendous reactions occur to produce hundreds of aromatic components. Hence,
red tea has obviously different aroma from green tea. Alcohols, aldehydes, acids and esters
are major constituents of the aroma of red tea and violet ketone plays important role in the
formation of the characteristic aroma.
O O
O
O2 +
Cis-theaspirane β-carotene β-ionone β-damascenone
Carotenoids, amino acids, and unsaturated fatty acids are the aroma precursors for red
tea. During processing, β-carotene is oxidized and decomposed to ionone (Figure 8-12),
which is further oxidized dihydroaclinidiolide and theaspirone.
Unsaturated fatty acids in tea, especially linolenic acid and linoleic acid, undergo
enzymatic oxidation during processing to produce C6-C10 aldehydes and alcohols. Meanwhile,
the fatty acids are also esterified by alcohols to yield esters with different aromas, such as
benzyl acetate, ethyl phenylacetate, methyl benzoate, and methyl salicylate. These
compounds have important effects on the aroma of tea.
Amino acids are also decomposed by enzymes to produce aldehydes, alcohols, and acids.
These compounds also contribute to the aroma of red tea.
enzyme
Pregnenolone 5α-male-16-en-3-one
Aromatic compounds in cooked meats are generated in three ways: lipid oxidation and
hydrolysis; Maillard reaction between amino acids or proteins and reducing sugars; and
further decomposition or recombination of flavor compounds. The aroma compositions of
cooked meats vary with the cooking temperature and processing methods. Cooked pork
contains reduced volatile compounds (mainly aldehydes, ketones, carboxylic acids and sulfur
compounds). Some non-volatile compounds, including free amino acids, peptides,
carbohydrates, vitamins and nucleotides, are important aroma precursors of livestock and
poultry meats. When heated, the precursors undergo various chemical reactions to yield
characteristic aromas.
When fat-containing beef is cooked, abundant volatile compounds are produced,
including fatty acids, aldehydes, ketones, alcohols, ethers, furan, pyrrole, lactones, aromatic
hydrocarbons, sulfur compounds (thiazole, thiophene, alkyl sulfur, sulfide, disulfide
compounds) and nitrogenous compounds (oxazole, pyrazine). To present, more than 600
volatile compounds have been identified in cooked beef, of which acidic compounds have
only minor effect on the aroma. Instead, thiophenes, furan, pyrazine compounds and pyridine
compounds contribute largely to the characteristic aroma of cooked beef. The composition of
the characteristic aroma of cooked pork is similar to that of beef, except that the contents of γ-
or δ-lactones converted from 4 (or 5)-hydroxyl fatty acid precursors are higher than in cooked
beef. Besides, cooked pork contains more unsaturated carbonyl and furan compounds than
cooked beef. Because mutton contains less free fatty acids and unsaturated fatty acids than
beef or pork, cooked mutton with less carbonyl compounds. The characteristic aroma of
cooked chicken meat is provided by sulfide and carbonyl compounds, in which, carbonyl
compounds, such as 2-trans-4-cis-decadien-1-al, are the most important active components.
The aroma of boiled meats is provided mainly by neutral compounds, such as sulfides,
furan-type and benzene-type compounds, while that of roasted meats is contributed mainly by
basic compounds, such as pyrazine, pyrrole, pyridine, and carbonyl compounds. However,
regardless of the processing method, sulfur compounds are the most important active
components for meat aroma. If sulfur compounds are removed, cooked meats will lose their
aroma. The content of hydrogen sulfide significantly affects the aroma of cooked meat. When
the content is too high, the odor of rotten egg is perceived; however, when the content is too
low, the aroma intensity is reduced. Smoked meats have unique aroma and tastes. The smoke
used contains phenols, formaldehyde, acetaldehyde, acetone, cresol, fatty acids, alcohols,
pyromucic aldehydes, and guaiacol, in which, fatty acids, phenols, and alcohols play
important role in the formation of the unique taste and aroma of smoked meats.
Lipids play an important role in the formation of the aroma of livestock meats. When
tallow is heated, it is decomposed and generates abundant compounds, including esters,
hydrocarbons, alcohols, carbonyl compounds, lactones, pyrazine and furan compounds, which
Food Flavors 263
are important active components of beef aroma. The same decomposition products have also
been detected in heated lard. When pork is cooked at temperatures lower than 100 °C, flavor
compounds derived from fat accounts for more than 50 % of total aroma compounds.
Aquatic Products
Generally, fresh marine fishes and freshwater fishes have only light odor and the odor is
mainly provided by volatile carbonyl compounds and alcohols, including aldehyde (C6, C8,
and C9), ketones and alcohols (such as 1-octene-3-one, 2-trans-nonyl aldehyde, cis-1-5-
octadiene-3-one and 1-octene-3-ol). These compounds are generated from the oxidation of
unsaturated fatty acids by lipoxygenase. As the freshness decreases, the compositions of the
odor change gradually and a characteristic fishy smell is perceived. This smell is caused by δ-
amino-valeraldehyde, δ-amino-valeric acid and hexahydropyridine compounds in fish skin
mucus, which are synthesized from basic amino acids. δ-Amino-valeraldehyde and δ-amino-
valeric acid have strong fishy smell. Because fish blood also contains δ-amino-valeraldehyde,
fish blood also smells fishy.
Volatile sulfur compounds are always detected in degraded marine fishes, such as
hydrogen sulfide, methyl mercaptan, dimethyl sulfide and diethyl sulfide. These compounds
are also involved in the unpleasant odor of marine fishes.
Marine fishes might exhibit the smell of oxidized fish oil or cod liver oil during storage
due to the oxidation of polyunsaturated fatty acids. Linolenic acid, arachidonic acid and
docosahexaenoic acid are the main unsaturated fatty acids in fish oil, their auto-oxidation
decomposition products can cause unpleasant odor. The smell of the oxidation products
depends on the degree of oxidation. In the early phase of oxidation, the products have the
smell of cucumber. As the oxidation proceeds, the smell of cod liver oil appears.
Food Flavors 265
Lipid Oxidation
Lipoxygenase occurs widely in plants and catalyzes the oxidation of polyunsaturated
fatty acids. The produced peroxides are then decomposed by lyase to yield aldehydes,
ketones, alcohols and many other flavor compounds. Hexanal, synthesized by linoleic acid as
precursor (Figure 8-18.), is the flavor compound of apple, strawberry, pineapple, and bananas.
Lipid oxidation can also generate undesirable flavors. For example, the oxidation of linoleic
acid leads to the formation of the characteristic beany flavor of soybean. 2-trans-Hexenal and
2-trans-6-cis-nonadienol are the characteristic aroma compounds of tomato and cucumber,
and both the compounds are synthesized with linolenic acid as precursor (Figure 8-19).
Among the flavor compounds generated in the lipoxygenase-catalyzed pathway, C6
compounds has the fragrance of grass, C9 compounds generate aroma similar to that of
cucumber and watermelon, and C8 compounds possess the smell of mushroom or violet. C6
and C9 compounds are generally aldehydes and primary alcohols and C8 compounds are often
ketones and secondary alcohols.
The pleasant aroma of mature pear, peach, apricot and other fruits is generally
contributed by the β-oxidation products of long-chain fatty acid (C8-C12).
linoleic acid
lipoxygenase
peroxidelyase
hexanal
+lipoxygenase
+aldehyde
++--yde lyase
lyase
oxygen acid
Figure 8-19. Lipoxygenase catalyzed formation of aldehydes from long-chain polyunsaturated fatty
acids [10].
266 Xiaoxiong Zeng and Guaoqing Huang
enzyme eugenol
enzyme
enzyme p-cresol
cinnamyl
alcohol
lignin polymer
3-methoxy-4-hydroxybenzaldehyd(vanillin)
Figure 8-22. Volatile compounds produced in the synthesis of shikimic acid [12].
In the synthetic pathway of shikimic acid, aromatic compounds (phenylalanine and other
aromatic amino acid) can be produced from intermediate product in the pathway. Besides
aromatic amino acid, the pathway can also form other volatile compounds related to essential
oil. Aromatic components which are formed by fumigation of food, some of them are also
formed from compounds in the shikimic acid pathway as precursors, such as vanillin.
Cinnamyl alcohol is an important aroma component in cinnamon perfume. Eugenol is the
main flavor and pungent ingredients in clove. Some important flavor compounds in shikimic
acid pathway are showed in Figure 8-22.
Terpenoids Synthesis
Terpenoids are important aromatic compounds of citrus fruits. Terpenoids containing two
or more isoprene units are nonvolatile and do not directly involve in aroma sensation.
Sesquiterpenes neral and ngcuka ketone are the characteristic aroma components of orange
and grapefruit respectively. Citral and limonene are monoterpenes and possesses the unique
smell of lemon and sour orange respectively. The enantiomers of terpenes may exhibit quite
different smells. For example, l-carvone [4(R)-(-) carvone] has a strong aroma of spearmint,
while d-carvone has the characteristic aroma of sweet wormwood (Figure 8-23).
268 Xiaoxiong Zeng and Guaoqing Huang
Non-Enzymatic Reactions
Maillard Reaction
The Maillard reaction can yield a large number of aromatic compounds and their contents
and proportion vary with substrate type, heating duration, and temperature. When the reaction
occurs in a low temperature for a short time, aromatic l actones, pyran compounds and furan
compounds as well as Strecker aldehydes are produced. When the reaction proceeds in high
temperatures for a long time, pyrazine, pyrrole and pyridine compounds with baking aroma
are formed.
Pyrazine compounds are important flavor compounds in all bakery foods and thermally
processed foods. It is generally believed that pyrazine compounds are generated through the
Strecker degradation between amino acids and α-dicarbonyl compounds, which are the
intermediates of the Maillard reaction (Figure 8-25). Small sulfides formed in the Maillard
reaction also influenced the flavor of foods. For example, methionic aldehyde is the
characteristic aroma compound of boiled potatoes and cheese biscuits.
Methionic aldehyde is unstable and can be easily decomposed into methane thiol and
dimethyl disulfide, resulting in the increase of low molecular weight sulfides.
The thermal degradation produces H2S and NH3 are also involve in the flavor formation
through Maillard reaction. For example, H2S, NH3, and acetaldehyde are the thermal
degradation products of cysteine. They can react with hydroxy ketones formed in the Maillard
reaction to generate thiazoline, which has the flavor of cooked beef (Figure 8-26).
Food Flavors 269
Figure 8-24. Formation of volatile compounds in the heterolactic fermentation of citric acid and
glucose.
Figure 8-25. Formation of an alkyl pyrazine and small sulfur compounds through the Maillard reaction
[13].
cysteine
3-hydroxyl-2-butanone
2,4,5-trimethyl-3-thiazoline
Figure 8-26. Formation of a thiazoline through the reaction between the thermal degradation products
of cysteine and carbonyl compounds [13].
270 Xiaoxiong Zeng and Guaoqing Huang
Degradation of vitamin.
Fat oxidation.
REFERENCES
[1] Shallenberer, RS; Acree, TE. Molecular theory of sweet taste. Nature, 1967, 216, 480-
482.
[2] DeTaeye, L; DeKeukeleire D; Siaeno E; Verzele M. Recent developments in hop
chemistry. In European Brewery Convention Proceedings. Amsterdam: European
Brewing Congress, 1977; 153-156.
[3] Morgan, ME; Libbey, LM; Scanlan, RA. Identity of the musty-potato aroma compound
in milk cultures of Pseudomonas taetrolens. Journal of Dairy Science, 1972, 55, 666
[4] Whitfield, FB; JH. Last Vegetables. In: Maarse, H. Volatile Compounds in Foods and
Beverages. New York: Marcel Dekker, 1991; 203-269.
[5] Shankaranarayana, ML; Raghaven, B; Abraham, KO; Natarajan, CP. Sulphur
compounds in flavours. In: Morton, ID; Macleod, AJ. Food Flavours, Part A,
Introduction. Amsterdam: Elsevier Scientific, 1982; 169-281.
Food Flavors 271
[6] Govindarajan, VS. Pungency: the stimuli and their evaluation. In: Boudreau, JC. Food
Taste Chemistry. Washington DC: American Chemical Society, 1979; 52-97.
[7] Hiraider, M; Miyazaki, Y; Shibata, Y. The smell and odorous components of dried
shiitake mushroom, Lentinula edodes I: relationship between sensory evaluations and
amounts of odorous components. Journal of Wood Science, 2004, 50, 358-364.
[8] Gower, DB; Hancock, M Bannister, LH. Biochemical studies on the boar pheromones,
5a-androst-16-en-3-one and 5a-androst-16-en-3a-ol, and their metabolism by olfactory
tissue. In: Cagan, RH; Kare, MR. Biochemistry of Taste and Olfaction. New York:
Academic Press, 1981; 7-31
[9] Hebard, CE; Flick, GJ; Martin. Occurrenceand significance of trimethylamine oxide and
its derivatives in fish and shellfish. In: Martin, RE; Flick, GJ; Ward, DR. Chemistry and
Bilchemistry of Marine Products. Westport: AVI Publishing, 1982; 149-304.
[10] Blank, I; Lin, J; Vera, FA; Weli, DH; Fay, LB. Identification of potent odorants formed
by autoxidation of arachidonic acid: structure elucidation and synthesis of (EZZ)-2,4,7-
tridecatrienal. Journal of Agricultural and Food Chemistry, 2001, 49, 2959-2965.
[11] Tressl, R; Holzer, D; Apetz, M. Biogenesis of volatiles in fruit and vegetables. In:
Maarse, H; Groenen, PJ. Aroma Research: Proceedings of the International Symposium
on Aroma Research, 1975 in Zeist, the Netherlands. Wageningen: Centre for
Agricultural Publishing and Documentation, 1975; 41-62.
[12] Wittkowski, R; Ruter, J; Drinda, H; Rafiei-Taghanaki, F. Formation of smoke flavor
compounds by thermal lignin degradation. In: Teranishi, R; Takeoka, GR; Guntert, M.
Flavor Precursors: Thermal and Enzymatic Conversions. Washington DC: American
Chemical Society, 1992; 232-243.
[13] Mussinan, CJ; Wilson, RA; Katz, I; Hruza, A; Vock, MH. Identification and some
flavor properties of some 3-oxazolines and 3-oxazolines and 3-thiazolines isolated from
cooked beef. In: Charalambous, G; Katz, I. Phenolic, Sulfur, and Nitrogen Compounds
in Food Flavors. Washington DC: American Chemical Society, 1976; 133-145.
In: Food Chemistry ISBN: 978-1-61942-125-7
Editors: D.Wang, H. Lin, J. Kan et al. © 2012 Nova Science Publishers, Inc.
Chapter 9
FOOD ADDITIVES
ABSTRACT
Food additives are substances intentionally added by manufacturers to foods to
preserve flavor or enhance taste and appearance. A substantial amount of food additives
with different functions have been widely used in the food industry and these compounds
contribute largely to the development of the industry. Due to the increased concern on
food safety and the rapid development of analysis techniques, the definition of food
additive has evolved greatly. This chapter firstly describes the evolution of the definition
of food additives. Then, various food additives are introduced briefly according to their
classification and the functions, properties and related aspects of important additives are
described one by one.
1. INTRODUCTION
1.1. Definition
Food additives are regulated substances and therefore defined in law. The definition of
food additives was firstly proposed by the FAO/WHO Joint Expert Committee for Food
Additives (JECFA) in 1955 as ―non-nutritive substances added intentionally to food,
generally in small quantities, to improve its appearance, flavor, texture, or storage properties‖.
This definition covered a rather narrow range and did not include flavorings and nutrients.
Since then, the definition evolves gradually and various definitions have been proposed by
different countries or organizations.
According to the Chinese Hygienic Standards for the Use of Food Additives (GB2760-
2007), food additives refer to ―artificially chemosynthetic or natural substances to be added to
foods in order to improve food quality and color, flavor and taste, and meet the need of
274 Linwei Liu and Shiyuan Dong
1.2. Classification
According to origin or source, food additives are divided into natural and artificial ones.
Food additives are also classified by functions in most cases. In China, food additives are
subdivided into 21 categories, including acidulant, anticaking agent, antifoaming agent,
antioxidant, bleaching agent, bulking agent, chewing gum base, coloring agent, color fixative,
emulsifier, enzyme preparation, flavor enhancer, flour treatment agent, coating agent, water
retention agent, nutrition enhancer, preservative, stabilizing and coagulating agent, sweeter,
thickener and others.
Among the 1500 kinds of food additives approved for use in China, more than 700 kinds
are spices and essence oils.
To guarantee food safety, use of food additives is strictly regulated by national and
international laws. According to the Chinese Hygiene Standards for Use of Food Additives
(GB2760-2007), the use of food additives must comply with the following principles:
1. Food additives must be nontoxic, do not generate toxic compounds upon
decomposition and do not cause chronic poisoning symptoms after long-term intake of dose
allowed.
2. Food additives do not destroy the nutritional components of foods, reduce food quality,
or generate toxic compounds upon decomposition.
3. Food additives can not be applied for the purpose of adulteration or for shielding the
facts of food spoilage and food deterioration.
Food Additives 275
4. Food additives cannot be applied for the purpose of concealing the quality deficiency
caused by the food itself or by processing.
5. The application ranges, dosages, and residues of food additives must comply with
related national standards and regulations, and try to minimize the using amount to bring
about the desired result.
6. Processing aids must be removed after processing, except those with allowed residues.
2. ACIDULANTS
2.1. Functions
Acidulants or acidity regulators are some acids and their salts, which serve a variety of
functions shown as the following:
(1) Flavoring to provide a desired taste and serve to intensify, enhance, blend of modify
the overall flavor of the product.
(2) Reduction of the pH to prevent or retard the growth of microorganisms and the
germination of spores, and to increase the lethality of the process.
(3) Maintainer or establishment of pH by serving as buffering agents. Usually a
combination of free acids and salts are used.
(4) Chelation of metal ions (Cu, Fe) to assist in minimizing lipid oxidation, reducing
color changes and controlling texture in some fruits and vegetables.
(5) Alteration of the structure of foods including gels made from gums (pectin,
carrageenan), and proteins.
(6) Interaction with proteins and emulsifiers to modify the structure of foods such as
doughs, alter the heat stability of proteins, and to serve as an emulsifier in processed cheese.
(7) Modification of sugar crystallization in hard candy manufacturing.
2.2. Acidulants
The usual use of acidulants in food are acidic, phosphoric, citric, malic, succnic, tartaric,
lactic, gluconic, glycolic, fumaric and adipic acid. The pKa or pKa1 of them are 4.75, 2.1,
3.08, 3.4, 4.2, 3.2, 3.86, 3.60, 3.03 and 4.43, respectively. Their structures are shown in
Figure 9-1:
The differences between acidulates are flavor, acidity, metal chelating and antimicrobial
activity, solubility, hydroscopicity and cost. Citric, malic, tartaric and gluconic acids have
similar taste which compliant with making beverage and candy. But for cola drink, using
phosphoric acid is more suitable. Fumaric and acitic acid have good antimicrobial activity,
and acetic acid (vinegar) is an important condiment and functional agent for Chinese food,
mayonnaise and pickles. Tartaric acid is often used to make leavening (bulking agent) owing
to its lower solubility.
276 Linwei Liu and Shiyuan Dong
Gluconolactone can be used to make Doufu and also used as a ingredient for making the
leavening because it can change to gluconic acid gradually in hot water.
Lactic acid has special taste, which compliant with many dairy products and fermented
food, such as yoghourt and alcohol. Phosphoric, citric, malice, succinct and tartaric acids are
metal chelating agents, they can be used as antioxidant synergist.
3. SWEETENERS
3.1. Type and Functions
There are two types of sweeteners: caloric (nutritive) and noncaloric (non-nutritive). The
caloric sweeteners provide about 4 calories per gram. The noncaloric varieties provide zero
calories.
Caloric sweeteners provide sweet flavor and bulk when added to food. They also
maintain freshness and contribute to product quality. Caloric sweeteners act as a preservative
in jams and jellies, and a flavor enhancer in processed meat. They provide fermentation for
breads and pickles, bulk to ice cream, and body to carbonated beverage. Some caloric
sweeteners are rich in natural resources, e.g., sucrose and fructose. Some are mainly made by
processing sugar or other small molecule compounds, e.g., molasses and sugar alcohols.
Sugar alcohols are low glycemic sweetener that is safe for diabetics, and helps manage
healthy glucose levels, and does not promote tooth decay.
Non-caloric sweeteners are used in place of caloric sweeteners in some foods. They do
not provide calories, but they do provide the sweet taste. Most non-caloric sweeteners are
chemically sythenic. Some of them, e.g., saccharin, acesulfame K and sucralose are more
stable than sugar to high temperature and other conditions of food processing, e.g., they do
not go in for non enzyme browning. Almost all of them can use in the diet for diabetics and
obesity patients.
Food Additives 277
This sweet enhancer is derived from cornstarch and is a mixture of 55% fructose and
45% sucrose. Starches are treated with enzymes that convert glucose to fructose, which
results in a sweeter product. The sweeters are used in many mass-produced foods, including
soft drinks, baked goods, jelly, syrups, condiments (like ketchup), fruits and desserts.
Sugar alcohols belong to polyols family which has many functions in food, such as
increasing viscosity, modifying sugar crystallization, being water binder, plasticizer,
cryoprotectant, and non-cariogenic sweetener. In China and many other countries, xylitol,
maltitol, sorbitol and mannitol are allowed to add into food.
Xylitol is odorless and a white crystalline powder with a pleasant and sweet taste, and its
energy value is 16.72 kJ/g. It has the same sweetness and bulk as sucrose with one-third fewer
calories and no unpleasant aftertaste. It quickly dissolves, produces a cooling sensation in the
mouth and reduces the development of cavities. Xylitol occurs naturally in many fruits and
vegetables and is even produced by the human body during normal metabolism. It is
produced commercially from plants such as birch and other hard wood trees and fibrous
vegetation, or from xylose hydrogenation. It can be used into any food with the amount as the
required of food making because its safety level is high.
Maltitol (4-O-α-glucopyranosyl-D-sorbitol) has 75-90% of the sweetness of sucrose and
its food energy value is 8.8 kJ/g. It is used to replace table sugar because it has fewer calories,
and does not promote tooth decay and has a somewhat lesser effect on blood glucose. Maltitol
is made by hydrogenation of maltose obtained from starch. It is especially used in production
of sweets: sugarless hard candies, chewing gum, chocolates, baked goods, and ice cream. Its
similarity to sucrose allows it to be used in syrups with the advantage that crystallization is
less likely. Maltitol may also be used as a plasticiser in gelatine capsulesand as a
humectant.http://en.wikipedia.org/wiki/Maltitol - cite_note-1#cite_note-1 Maltitol does not
brown and caramelize after liquifying by exposing to intense heat. It is somewhat more
slowly absorbed than sucrose which makes it somewhat more suitable for people with
diabetes than sucrose. It can use with quantity stipulated by use standard for different food
categories.
Sorbitol, also known as glucitol, is a sugar alcohol that the human body metabolises
slowly. It is obtained by the reduction of glucose changing the aldehyde group to an
additional hydroxyl group. It also occurs naturally in many stone fruits and berries from trees
of the genus sorbus. It provides dietary energy 2.6 kJ per gram. and is often used in diet foods
including diet drinks and ice cream, mints, cough syrup, and sugar-free chewing gum.
Sorbital sometimes is used as a sweetener and humectant in cookies. Ingesting large amounts
of sorbitol can lead to abdominal pain, gas, and mild to severe diarrhea. In China, the
maximum level of use to each food is 5.0 g/kg.
Mannitol is also used as a sweetener for diabete patient. Since mannitol has a positive
heat of solution, it is used as a sweetener in "breath-freshening" candies, the cooling effect
contributing to the fresh feel. The pleasant taste and mouth feel of mannitol also make it as a
popular excipient for chewable tablets. It can be used a little in food coating for flavor.
278 Linwei Liu and Shiyuan Dong
3.4. ISO-Maltulose
There are several noncaloric sweeteners, such as saccharin, aspartame, acesulfame K, and
sucralose and their chemical structures are shown in Figure 9-2:
(1) Saccharinhttp://en.wikipedia.org/wiki/Saccharin - cite_note-1#cite_note-1 is a
colorless, crystal and artificial sweetener. The basic substance, benzoic sulfimide, has
effectively no calories and is many times sweeter than sucrose (about 300-700 times as
sucrose) [1], but has an unpleasant bitter or metallic aftertaste, especially at high
concentrations. In countries where saccharin is allowed as a FD, it is used to sweeten products
such as drinks, candies, medicines, and toothpaste. In China, the maxium usage quantity of
saccharin for food is 0.15 g/kg. Many studies have been performed on saccharin, some
showing a correlation between saccharin consumption and increased frequency of cancer in
rats (especially bladder cancer) and others finding no such correlation. No study has ever
shown a clear causal relationship between saccharin consumption and health risks in humans
at normal doses, though some studies have shown a correlation between consumption and
cancer incidence.
(2) Aspartame is 200 times sweeter than sugar in typical concentrations. Aspartame has a
caloric value of 17 kJ per gram, so the minimum quantity of aspartame which needs to
produce a sweet tast is so small that its caloric contribution is negligible. Therefore, it is a
popular sweetener for those trying to avoid calories from sugar. The taste of aspartame is not
identical to that of sugar. Blends of aspartame with acesulfame K taste more like sugar, and to
be sweeter than either substitute used alone.
Like many other peptides, aspartame could be hydrolyzed into its constituent amino acids
under conditions of high temperature or pH. This makes aspartame undesirable as a baking
sweetener.. At room temperature, it is the most stable at pH 4.3, so that it is reasonably stable
in soft-drinks. In the powdered beverages, the amine in aspartame can undergo Maillard
reaction with the aldehyde groups present in certain aroma compound. The safety of
aspartame has been studied thoroughly, and the scientific evidence indicates it is safe at
current level of consumption as a non-nutritive sweetener.
(3) Acesulfame K, also known as cesulfame potassium, is a white crystalline powder. It is
180-200 times sweeter than sucrose with a slightly bitter aftertaste, especially at high
concentrations.
Food Additives 279
4. PRESERVATIVES
4.1. Definition
Preservatives or antimicrobial agents play an important role in today's supply of safe and
stable foods. Preservative means any substance which is capable of inhibiting, retarding or
arresting the process of fermentation, retarding acidification or other deterioration of food or
masking any of the evidence of putrefaction. Preservatives work by preventing the growth of
280 Linwei Liu and Shiyuan Dong
microbes (fungi, bacteria) or by killing the microbes. Food preservatives, low toxicity, are
commonly used in food processing. They should not pose significant health effects on
consumers during normal consumption.
The choice of antimicrobial agent has to be based on the antimicrobial spectrum of the
preservative, the chemical and physical properties of both food and preservative, the
conditions of storage and handling, and the assurance of a high initial quality of the food to be
preserved.
Many preservatives have broad bacteriostasis spectrum, but some others can only affect
on some species of microorganism. Salts of acids, such as sodium acetate, calcium citrate,
sodium benzoate, calcium propionate, and sodium nitrite all have antimicrobial properties.
Sulfur dioxide can be derived from a various sulfur additives such as bisulfite, and produce a
multitude of effects in food. Most preservatives only have antimicrobial effects at certain
range of pH because their states can be changed with the change of pH. Some preservatives
are unstable in high temperature, and some are dissoluble in water or oil. Therefore, the user
must know those properties before using them. Table 9-1 shows properties of some common
preservatives.
The latter is used more often because benzoic acid is sparsely soluble in water, and
sodium benzoate is more soluble. The undissociated form on benzoic acid is the most
effective antimicrobial agent. The optimum pH range ranges from 2.5 to 4.0, which makes it
an effective antimicrobial in highly acidic foods. Benzoic acid and sodium benzoate are
widely used in fruit drinks, cider, carbonated beverages, sauce, jams and pickles with 1.0 g/kg
or less as the ML for different foods.
4.4.4. Sulfites
Sulfur dioxide and sulfites have been used as preservatives serving both as antimicrobial
substance and antioxidant. Instead of sulfur dioxide solutions, a number of sulfites, such as
sodium bisulfite, sodium metabisulfite, sodium sulfite, potassium bisulfite, sodium hydrogen
sulfite, sodium hyposulfite and potassium metabisulfite can be used. When dissolved in
water, they all yield active SO2 (see the following equations)[3]. The most widely used of
these sulfites is potassium metabisulfite.
282 Linwei Liu and Shiyuan Dong
SO2(gas) ↔ SO2(aq)
SO2(aq) ↔ H2O + H2SO3
H2SO3 ↔ H+ + HSO3-
HSO3- ↔ H+ + SO32-
2HSO3- ↔ S2O52- + H2O
All of these forms of sulfur are known as free sulfur dioxide. Meanwhile, the bisulfite ion
(HSO3-) can react with aldehydes, dextrins, pectic substances, proteins, ketones, and certain
sugars to form addition compounds, which are known as bound sulfur dioxide.
Sulfurous acid inhibits molds and bacteria to a lesser extent yeasts. For this reason, SO2
can be used to control undesirable bacteria and wild yeasts in fermentations without affecting
the SO2- tolerant cultured yeasts. The antiseptic activity of SO2 highly depend on the pH. The
lower the pH, the greater the antiseptic action of SO2. The amount of SO2 added to foods is
self-limiting because the product may develop an unpleasant off-flavor at concentration from
200 to 500 ppm. The use of SO2 is not permitted in foods that contain significant quantities of
thiamine, because this vitamin is destroyed by SO2.
Because SO2 is volatile and easily lost to the atmosphere, the residual levels may be
much lower than the amounts originally applied. In China, the ML of sulfites are calculated
by means of the residual levels in the finished food. Different food has different maxium
residual quantity. For example, the maximum residual quantities for fresh and dried fruits
processed are 0.05 g/kg and 0.2 g/kg, respectively.
4.4.5. Natamycin
Natamycin (Figure 9-3) is a naturally occurring antifungal agent produced by
Streptomyces natalensis. Natamycin has a very low solubility in water; however, it is
effective at very low levels. Natamycin has been used for decades in the food industry as a
hurdle to fungal outgrowth in dairy products, meats, and other foods. It has a neutral flavor
impact, and less dependence on pH for efficacy. It may be applied by spraying a liquid
suspension, by dipping the product in an aqueous suspension, or by mixing it into the product
in a powdered form along with cellulose on whole, shredded, or soft cheeses.
4.4.6. Nisin
Nisin is an antimicrobial polypeptide, with a molecular weight of 3500, produced by
some strains of Lactococcus lactis. Nisin-like substances are wide products from lactic acid
bacteria.
http://upload.wikimedia.org/wikipedia/commons/a/a3/Natamycin.svg
These inhibitory substances are known as becteriocins. Nisin can be used as a processing
aid against gram-positive organisms. It has been effectively used in preservation of processed
cheese. It is also used in the heat treatment of nonacid foods and in extending the shelf life of
sterilized milk [6].
5. ANTIOXIDANTS
5.1. Definition and Classification
Food antioxidants in the broadest sense are all of the substances that have some effects on
preventing or retarding oxidative deterioration that leads to rancidity, loss of flavor, color and
nutritive value of foodstuffs in foods.
Antioxidants can be classified into a number of groups: (1) Primary antioxidants which
can terminate free radical chains reactions and function as electron donors including the
phnolic antioxidants, butylated hydroxyanisole (BHA), butylated hydroxytoluene (BHT),
tertiary butyl hydroquinone (TBHQ), propylgallate (PG), natural and synthetic tocopherols
and so on. (2) Oxygen scavengers which can remove oxygen in a closed food system. Most
widely used compounds are Vitamin C, and related substances, ascorbyl palmitate, and
erythorbic acid (the D-isomer of ascorbic acid). (3) Chelating agents or sequestrants. They
remove metallic ions, especially copper and iron, that are powerful pro-oxidants. Citric acid is
widely used for this purpose. Amino acids and ethylene diamine tetraacetic acid (EDTA) are
examples of chelating agents. (4) Enzymatic antioxidants which can remove head space
oxygen dissolved, such as glucose oxidase. Superoxide dismutase can be used to highly
remove oxidative compounds from food systems. (5) Natural antioxidants which are present
in many spices and herbs. Rosemary and sage are the most potent antioxidant spices.
Primary antioxidants are mostly phenolic compounds. They can react with free radicals,
which scavenge the active radicals and change themselves into lower active radicals. The
lower active radicals can react each other or with other radicals until becoming stable
molecules. That is why they can terminate free radical chains reaction, which is the main
oxidation process of lipids. Phenolic compounds are a mixture and in combination with a
chelating agent because different antioxidants have the synergistic effect. This kind
antioxidant should be added into food before serious oxidation has occurred and used with
small quantity. Otherwise, it may act as a pro-oxidant. For example, phenolic radicals can
promote ROOH decomposition to produce ROOO.
ROO AH 2 ROOH AH
ROO AH ROOH A
AH AH A AH 2
Chelating agents which have ability to bind metal ions have contributed significantly to
stabilization of food color, aroma and texture because traces of heavy metal ions can act as
284 Linwei Liu and Shiyuan Dong
catalysts for lipid oxidation. Many natural constituents of food can act as chelating agents, e.
g., carboxylic acids (oxalic, succinic), hydroxy acids (lactic, malic, tartaric, citric),
polyphosphoric acids (ATP, pyrophosphates), amino acids, peptides, proteins and porphyrins.
Both ascorbic acid and glucose plus glucose oxidase and catalase can deplete O2 in food
system. When they react with oxygen, ascorbic acid becomes to dehydroascorbic acid, and
glucose becomes to gluconic acid, and H2O2, another product of the oxidation of glucose, can
be broken down to water by catalase. When the oxygen has been depleted completely, the
food oxidation will stop. However, owing to VitC, oxidation is based on a complex
mechanism with some active substance giving birth to the midway of the reaction, adding less
quantity of VitC will prooxidant.
The common used antioxidants in food are tocopherols, ascorbic acid, ascorbyl palmitate,
sodium isoascorbate, tert-butylhydroxyanisole (BHA), di-tert-butylhydroxytoluene (BHT),
tertiary butyl hydroquinone (TBHQ), propylgallate (PG), tea polyphenols, antioxidant of
glycyrrhiza, and so on. The structures of some of the antioxidants are shown in Figure 9-4.
Tocopherols and ascorbic acid are two vitamins, and their use in food have no danger but
expensive. Tocopherols and ascorbic acid, which are supplyed either natural or synthetic
equivalents, are less restricted in food using. In China, they can be used in food with any
quantities as the needs for food process. Ascorbyl palmitate, a derivative of ascorbic acid, has
good solubility in oil, so as to be a wide use as antioxidant which contains abundant oil or fat.
Sodium isoascorbate has almost the same function as ascorbic acid except it is not a vitamin
and cheaper than ascorbic acid. The use standard of FDs of China permit those antioxidant to
be added into many food with ML being 0.2-0.5 g/kg.
BHA, BHT and PG have been used, with powerful antioxidant function, for many years
in most countries. The first two are typical lipophilic artificial antioxidants and the last one
has some polarity. The first two are very stable during food process, but PG is unstable at
high temperature and discolour in presence of iron and metal complexes. The use of these
synthetic antioxidants is very restricted. The ML of them in most food categories is 0.1 g/kg
according to hygienic standards for uses of FDs in China.
TBHQ is more stable and less volatile than BHA at high temperature. TBHQ gives
excellent antioxidant potency to oils and fats.
It can maintain freshness and quality of crude oils during long distance transportation,
and can offer protection to fried foods, thus enhancing their storage life and freshness. The
highest level of TBHQ permitted in the GSFA (USA) is 1 g/kg for frozen fish, fish fillet, and
fish products, and in the FDs use standard (China) is 0.2 g/kg for edible oils and fats, fried
food, curing meat class, and dried fishes. It is often used in conjunction with BHA, BHT and
PG to provide a synergistic antioxidant effect.
Tea polyphenols, antioxidant of glycyrrhiza and antioxidant of bamboo leaves are natural
antioxidants being extracted from tea, liquorice and bamboo. Tea polyphenols are water
soluble. Antioxidant of glycyrrhiza is unsoluble in water but in ethanol and ethyl acetate. The
antioxidant of bamboo leaves is soluble in ethanol. They are phenols substance, such as
catechins, flavonoids and phenolic acids. The ML of TP, AG and ABL in the FDs use
standard (China) are 0.3, 0.2 and 0.5 g/kg, respectively.
Rosemary extract is another natural antioxidant. The active ingredients are ursolic acid,
rosmarinic acid, conorsic acid, and conorsol. The ML of it in the FDs use standard (China) is
0.3 g/kg.
EDTA is abbreviation of disodium ethylene-diamine-tetraacetate, a famous chelating
agent in analysis chemistry. Phytic acid (inositol hexaphosphoric acid), orthophosphoric acid,
pyrophosphoric acid, triphosphoric acid, hexameta-phosphoric acid, tartaric acid, citric acid,
gluconic acid, and their salts are also good chelating agents. All of those chelating agent have
certain ability of antioxidant. In the use standard of FDs of China, the ML of EDTA and
phytic acid are 0.07 and 0.2 g/kg repectivesly. The orthophosphoric acid, pyrophosphoric
acid, triphosphoric acid, hexameta-phosphoric acid are classified also as water retention
reagents which can be use with high levels as 3-5 g/kg. The other chelating agents meationed
above can be used in food without level limits.
The purpose of emulsifiers and stabilizers is mix together of different ingredients that
normally would not mix, namely fat and water. This mixture of the aqueous and lipid phases
is then maintained by stabilizers. For example, these additives are essential in the production
of mayonnaise, chocolate products and fat spreads. The manufacture of fat spreads (reduced-
fat substitutes for butter and margarine), has made a significant contribution to consumer
choice and dietary change, which would be impossible without the use of emulsifiers and
stabilizers. Other reduced and low-fat versions of a number of products are similarly
dependent on this technology.
In addition to this function, the term stabilizers is also used for substances that can
stabilise, retain or intensify an existing colour of a foodstuff and substances that increase the
binding capacity of the food to allow the binding of food pieces into reconstituted food.
Some emulsifier and a few stabilizers used in food are synthetic compounds, while many
of them are natural substances. Hygeian use of these additives need to be known and
controlled their negative effects on people health. Although almost each of them is generally
recognized as safe (GRAS), some of them still strict the level of use. Moreover, the increasing
awareness of problems with food allergy and intolerance has led to the requirement to state
the source of certain emulsifiers on food labelling. For example, lecithin derived from soya is
286 Linwei Liu and Shiyuan Dong
not suitable for an individual with an allergy to soya, so labelling of the source of the
ingredient is vital to aid in consumer choice in products safe for individuals with specific
dietary requirements.
When two immiscible liquids, e.g., oil and water are mixed by stirrer throughly together,
there are great interface appearing between them. Because the surface tension of the interface
send up the free energy of the system greatly, the system, named as disperse system, is high
unstable and will separate water and oil quickly.
Emulsifier, an amphiphilic substance, has usually a hydrophilic head and a hydrophobic
tail. When emulsifier moleculars are adsorbed to the interface, the head and the tail will point
into the water and oil respectively, which will decrease the surface tension and increase
stability of the disperse system. If water, oil and emulsifier are mixed together, the disperse
system will formed much easier than before. That is why emulsifier has the funtion to make
and stablize emulsion and other disperse system.
Stabilisers may have a little emulsifier's function or not, but they can enhance the stability
of disperse system by other effects. It may increase the viscosity of the system, which
decrease the thermal motion speed of the droplets so as to retard their aggregation. It may be
adsorptive as the second layer on the first adsorptive layer on the surface of the droplets,
which increase the steric restriction to aggregation.
Addition from the fundamental function, emulsifier has other useful functions for food.
Formation or deformation of foaming also need emulsifier to be an accelerant for forming or
deforming the airtight film on the bubble. Another function is wetting effect, which means
moisten the solid surfaces. Solid material is mixed with an emulsifier or its surface is spread
with emulsifier, the surface then becomes hydrophilic. For example, chewing gum is apt to
stick to teeth. We can prevent adhesion by wetting the surface of chewing gum by adding
emulsifier. Emulsifier can act on starch and protein, which is important also. When emulsifier
combine with the amylose helix structure, the α-starch can not change to β-starch, which
prevent degradation of starch in bread and other millet cake, so that extending shelf life of
bread products. When making sponge dough, emulsifier can modify gluten molecules and
enhance its film-forming power, resulting in good spreadability and improvement of working
efficiency. Thus, easy-rising bread can be obtained. Emulsifiers stabilise the emulsion in low-
fat spreads providing the right stability and mouthfeel and reduce spattering in frying
margarine also.
When an emulsifier will be used for a purpose, knowing its classification is important
because different classes of emulsifier have different properties, function and safety. For the
student to learn the basical knowledge, the concept of HLB (hydrophile-lipophile balance)
should be understood. The Hydrophilic-lipophilic balance of a surfactant is a measure of the
degree to decide whether it is hydrophilic or lipophilic, determining by calculating values for
the different regions of the molecule, as described by Griffin in 1949 and 1954.
Griffin's method for non-ionic surfactants as described in 1954 works as follows:
HLB = 20Mh / M
Where, Mh is the molecular mass of the hydrophilic portion of the Molecule, and M is
the molecular mass of the whole molecule, giving a result on an arbitrary scale of 0 to 20. An
HLB value of 0 corresponds to a completely hydrophobic molecule, and a value of 20 would
correspond to a molecule made up completely of hydrophilic components.
The HLB value can be used to predict the surfactant properties of a molecule:
purposes. In China, those emulsifiers are extensively used in dairy, pasta, butter, and coffee
drinks, with ML from 5 g/kg to production need.
(2) Acetic acid esters of monoglycerides.
Acetic acid esters of monoglyceride, also called as acetylated monoglyceride, are an
emulsifier in which acetic acid is bound with monoglyceride. It has little emulsifying activity
but there are many characteristics and application fields as follows: Soft acetylated
monoglyceride is able to expand by more than 8 times with tension. It is an extremely stable
oil of which peroxide value does not increase even when heated at 97.7 °C for 1000 hours.
The combination of liquid acetylated monoglyceride and hydrogenated fats can improve the
quality of fats, for example, margarine characterized with small temperature changes and
wide plasticizing range, can be produced with them. It is a liquid characterized by being less
oily even at low temperatures and available as a solvent, lubricant, etc. Although it has no
function as a good emulsifier, it is usable for foaming fats and oils by itself or in combination
with other emulsifiers because of its stable alpha-crystal structure. Practically, it is used as
powdered foaming agents, solvents, plasticizers for gums and coating agents for food.
All the stabilizers, thickeners and gelling agents are known and described as food
hydrocolloids implying that functional properties are obtained by mixing them with water.
They are macromolecules, such as carbohydrate polymers, proteins and their modified forms,
which are water soluble. These additives include traditional materials such as starch,
cellulose, gums, obtained from many land plants, and gelatin, an animal by-product, and
microbial polysaccharides of xanthan, gellan and pullulan, and their modified forms. Even at
low concentrations, they are able to increase a system's viscosity, to form gels and to stabilize
emulsions, suspensions or foams. These compounds are also active as crystallization
inhibitors and are suitable for aroma encapsulation, which is often needed for dehydrated
food.
7.2. Classification
Raw material origin has been used to classify hydrocolloids, for example as seaweed
extracts, seed gums, fermentation products, plant exudates, animal gelatin or microorganic
gums. Their general functional properties may also be used to classify them as thickeners,
stabilizers or gelling agents. The resourceful plant polysaccharoses, like starch and cellulose,
are derived by some chemical methods are classified modify polysaccharoses. Natural
292 Linwei Liu and Shiyuan Dong
stabilizers, thickeners and gelling agents coming from plants can be classified based on their
sources shown in Table 9-4.
The following is a brief overview of the key functional properties for gelling agents,
stabilizers or thickeners used. These ingredients need to be added to commercially-produced
food to maintain their structure and physical properties during processing. For example, fruits
such as strawberries, raspberries and cherries need the addition of a small amount of pectin to
form a jam. Nutritional properties are relatively new and nutraceutical or health-enhancing
properties are even more recent. Further work is sure to advance the use of hydrocolloids
beyond modification of the rheology of foods.
this and xanthan gum is the typical hydrocolloid to supply this functionality. For beverage
with pulp suspended, like orange juice with pulp particle, precipitation can be prevented by
adding suitable amount agar to crate a small yield point which is big enough to stop the pulp
settling during the shelf-life and small enough to keep the beverage's flow property like
normal drink.
7.3.4. Gelation
One of the key texturising aspects of hydrocolloids is the ability to gel and solidify fluid
products. For example, in gelled milk desserts, even low levels of carrageenan will form a
solid milk gel. Other classic gelling agents are pectin, gelatin and agar. However, others will
form a gel under specific conditions. Certain grades of alginates form gels with calcium ions.
Xanthan and locust bean gum alone do not gel, but their combination display synergy and
form a strong cohesive gel. Methyl cellulose and hydroxypropylmethyl cellulose are unusual
in forming solutions that reversibly thicken or gel when heated. The food industry has a
myriad of gelling applications ranging from soft, elastic gels to hard and brittle gels.
The following agents are widely used in food industry. Almost every one is permitted to
be used in any food categories, except those special mentioned in appropriate level, based on
the need of production according to the Chinese GB 2760.
7.4.2. Agar
Agar is extracted from red seaweed (Rhodophyceae) and has been used in foods for more
than 350 years. Agar consists of a mixture of agarose and agaropectin. Agarose is a linear
polymer, made up of the repeating monomeric unit of agarobiose. Agarobiose is a
disaccharide including D-galactose and 3, 6-anhydro-L-galactopyranose. Agaropectin is a
heterogeneous mixture of smaller molecules that occur in lesser amounts. Agar is insoluble in
cold water and hydrates when boiled. Cooling solutions below about 40 °C produce very firm
brittle gels which can be melted by heating above 85 °C. Food applications include water
294 Linwei Liu and Shiyuan Dong
dessert gels, aspics, confectionery jellies, canned meats gels, a vegetarian gelatin substitute, a
thickener for soups, and as a clarifying agent in brewing.
7.4.3. Alginates
Alginates are derived from various species of brown seaweed found off the coasts of the
North Atlantic, South America and Asia. They are produced as a range of salts, but sodium
and potassium alginate are predominantly used in foods. It is a polysaccharide, consisting
primarily of D- and L-galactose units. About every tenth D-galactopyranose unit contains a
sulphate ester group. Calcium, magnesium, potassium or sodium cations are also associated
with the polysaccharide. It is insoluble in cold water and soluble in boiling water. Sodium or
potassium alginate hydrates in cold or hot water to give viscous solutions. The controlled
interaction between sodium or potassium alginate and calcium salts gives cold-setting gels
that are shear irreversible and heat stable. Control is affected using citrate or phosphate
sequestrants, or by processing at temperatures above about 70 °C and cooling. Typical food
applications include reformed foods such as onion rings and olive fillings, cold-setting bakery
cream fillings and heat-stable bakery and fruit fillings.
7.4.4. Carrageenan
Carrageenan is obtained from red seaweeds. Different species provide a number of
carrageenan extracts. Carrageenan is a hydrocolloid consisting mainly of the ammonium,
calcium, magnesium, potassium and sodium sulphate esters of galactose and 3, 6-
anhydrogalactose polysaccharides. These hexoses are alternatively linked -1, 3 and -1, 4 in
the copolymer. The relative proportions of cations existing in carrageenan may be changed
during processing to the extent that may become predominant. Depending on the source of
seaweed, the functional components are kappa-carrageenan, iota-carrageenan or lambda-
carrageenan, each of which is characterized by the content of sulphate groups and gelling
properties. Carrageenan is soluble in water of about 80 °C, forming a viscous, clear or slightly
opalescent solution that flows readily. It is insoluble in ethanol.
Kappa carrageenan and furcellaran form thermally reversible firm, brittle gels. Iota
carrageenan gives soft, elastic gels. Kappa carrageenan interacts synergistically with
polymannans, such as locust bean gum and konjac, to give strong cohesive gels. Blends of
kappa with iota carrageenan or polymannans are used to give a range of gel textures used in
injected meats, canned meats and water dessert gels..
Hybrid (kappa/iota) carrageenan is particularly suitable for firm, creamy textures in dairy
desserts. Lambda carrageenan is non-gelling but thickens in drinks and dairy desserts. A
specific interaction between kappa carrageenan and kappa casein is widely used to stabilise
dairy products including milk beverages, ice cream mixes and processed cheese products.
7.4.8. Gelatine
Gelatine is a protein material obtained from animal connective tissue using hydrolysis in
acidic (type A) or basic (type B) solution followed by hot water extraction. Gelatine hydrates
readily in warm or hot water to give low-viscosity solutions that have good whipping and
foaming properties. Concentrated solutions containing up to 40 % gelation are made for use
in confectionery. After cooling, the network of polypeptide chains associates slowly to form
clear, elastic gels that are syneresis free. The thermoreversibility of gelatine gels gives them
unique properties: the melting point is below 37 °C so they melt in the mouth to give smooth
textures with excellent flavour releasing. Gelatine is used in a wide range of food,
pharmaceutical and photographic applications. Food products include jelly candies and
aerated confectionery, yogurt and other cultured desserts, dairy desserts and creams, low-fat
spreads, canned meat products, water dessert gels and decorative aspics.
7.4.10. Pectin
Pectin is a polysaccharide that is naturally present in most land plants, although
commercial pectin is primarily extracted from citrus peel and apple pomace. Two forms of
commercial pectin are available: high methyl- and low methyl-esterified pectin; and two
versions of the latter exist: a conventional and an amidated form. High methyl-esterified
pectin forms gels in high soluble solids and acidic systems, whereas low methyl-esterified
pectin forms gels in a much broader pH and soluble-solids range, but requires the presence of
divalent cations for gelling. As a consequence, each type has its own particular function.
Nevertheless, general attractive features include excellent flavor release, good processing
characteristics and stability at low pH. Its traditional and major function is to act as a gelling
agent in foods, but, nowadays, it also serves as a thickening and stabilizing agent. The
application of pectin is diverse and covers fruit-based products, dairy products, acidified milk
drinks and other beverages, confectionery, bakery products, various fine foods and spreads.
Additionally, pectin is used in the pharmaceutical industry. Finally, increasing consumer
awareness of healthy life-style habits and the emerging trend to produce functional foods
increases the significance of the status of pectin as a water-soluble dietary fiber.
7.4.16. Others
Polydextrose, propylene glycol alginate, fenugreek gum, sesbania gum, tamarind seed
polysaccharide gum, sodium carboxymethyl starch, ablmoschus manihot gum, artemisia gum,
gleditsia sinensis lam gum, linseed gum, polyglycerol esters of fatty acid, hydroxypropyl
starch phosphated distarch phosphate, methyl cellulose and ethyl cellulose are other
thickeners, stabilisers and gelling agents used in food in China. They are used in some
appointed food categories with limited amount as ML in GB2760.
298 Linwei Liu and Shiyuan Dong
Phosphoric acid (other names: orthophosphoric acid.) can only be obtained pure in the
crystalline state and slowly undergoes dehydration to diphosphoric acid. Phosphoric acid is
added to food to enhance the antioxidant effects of other compounds present, and also as an
acidity regulator. Typical products include carbonated beverages, processed meat, chocolate,
fats and oils, beer, jam and sweets. Phosphoric acid is a highly acidic ingredient in cola
drinks.
(1) Monosodium phosphate is a sodium salt of phosphoric acid. It is added to food to act
as an antioxidant synergist, a stabiliser and a buffer. Typical products include processed meat
products, processed cheese products. It is also used in bread, rolls, buns, artificial sweetened
fruit jelly, canned potatoes, canned sweet peppers, and canned tomatoes and as a jelling agent.
No food safety problems have been shown to occur with this chemical at the levels commonly
used in foods, but high intakes may upset the calcium/phosphorus equilibrium.
(2) Disodium phosphate is a sodium salt of orthophosphoric acid and is used as an
antioxidant synergist, stabiliser and buffering agent in food. It is also used as an emulsifier in
Food Additives 299
Sodium triphosphate is beside potassium triphosphate, one of the polyphosphates that are
allowed as FDs. It is used in food for soften water, as emulsifying salt for process cheese or
for the preparation of cooked sausages, surimi or fish fingers. It has antimicrobial function
also.
300 Linwei Liu and Shiyuan Dong
9. COLORANTS
Dyes and pigments used in the food are known collectively as food colours, or more
tersely, simply as colours. They are added to foods to make it more attractive to the purchaser
or consumers or to replace natural colours lost during the food processing. Canned
strawberries, for example, would be grayish-brown if colours are not added and canned peas
would be brownish green without colouring with green colorant.
In China, only 56 colorants are permitted for use as FDs. Most of them are natural, and
include saffron, cochineal, carotenes (and the closely related xanthophylls) and anthocyanins.
Other permitted colorants include synthetic or semi-synthytic coumpound, such as carotene
structure identical, sodium copper chlorophyllin and erythrosin, and inorganic substances,
such as the white pigment titanium dioxide and finely divided aluminum, silver and gold
which are used in cake decoration.
The list of permitted colours includes 9 synthesis dyes and 47 natural pigments or
extracts. Most of them are used in foods with strictly limits. For example, colouring matter
must not be added to raw meat, fish, poultry, fruit, cream, milk, honey, vegetables, wine,
coffee, tea and condensed or dried milk in most countries. Also, by agreement with the
manufacturers, colours are not used in foods made for babies and infants. The 9 synthesis
colours use in China are amaranth, ponceau 4R, erythrosin, new red, lemon yellow, indigo
blue, sunset yellow, brilliant blue and crimson. Sodium copper chlorophyllin is a semi-
synthesis colour which is also permitted in China. The 47 natural colours are β-carotene
(zymotechnics), bect-root red, turmeric yellow, curcumin, safflower yellow,
http://www.chinaadditives.com/Carthamus-Red.htm lac dye, cowberry red, papika extract
include capsorubin and capsanthin, chilli orange, caramel, carthamus yellow, gardenia
yellow, coreopsis yellow extract, wild groundnut red, broomcorn red, maize yellow include
zeaxanthin and crtotixabthin, radish red, cacao husk pigment, ang-kak, monascorubin,
vinespinach red, black currant red, neutral mustard red, gardenia blue, hippophae
rhamnoides(sea backthern) yellow, hibiscus sabaariffa(roselle) red, acorn husk brown, NP red
(NP), tanoak brown, mulberry red, natural amaranth, cherokee rose brown, wide jujube skin
extract, peanut underwear red, grape skin red, uguisukagnra color, spirulina blue, vegetable
carbon black, pale butterflybush flower yellow, gromwell red, theaflavin, tea green pigment,
citrus yellow, bixin, cochineal red and iron oxide red or black.
All of the 9 synthesis colours and most of natural colours used in China are water soluble
and purchased in a powder format that exhibits coloring solutions when they are dissolved.
Therefore, their using are very easy.
Aluminum lake pigments, made of aluminum and colorants, are water insoluble material
but oil dispersible (but generally not oil soluble) and thus can be mixed with oils and fats.
They can also be dispersed in other carriers such as propylene glycol, glycerin and sucrose
(water and sugar). Aluminum lake pigments are used in a variety of applications: (1) To color
a fat based product, such as chocolate or compound coatings. For these, we produce a
concentrated dispersion in a high quality and very stable vegetable oil. The dispersion is
added directly to the chocolate to dye it accordingly. (2) For "hard panning" (to dye the
outside of a product such as a gum ball or a pill). In this case, we produce a dispersion usually
using sucrose (sugar and water) that is applied to the candy or food as it is being tumbled and
dried. Multiple layers are applied to produce the desired shade.(3) Lakes tend to resist
bleeding. Dyes have a tendency to "bleed", or migrate from one part of the product to another.
This can be a problem in candy canes or any product where there are defined borders such as
Food Additives 301
the food with desired stripes. While Dyes are normally used in hard candy, lakes are
sometimes substituted if bleeding is a problem.
Flavourings, or flavors, spices and essence, are substances or food flavor additives used
to give taste and/or smell to food. There are different types of flavourings, such as natural,
natural-identical or artificial flavouring substances, flavouring preparations of plant or animal
origin, processing flavourings which evolve flavour after heating and smoke flavourings. The
expression "natural flavouring" may only be used for flavouring substances or flavouring
preparations which are extracted from vegetable or animal materials. Generally, different
flavors are specially formulated for various food items to make them more delightful.
Flavorants contains many flavour compounds. Only the Generally Recognized As Safe
flavour compounds can be used as food flavor additives. Flavour compounds often classify
into 18 groups, shown in Table 9-5. Each of the 18 groups contains substances that have
similar chemical structure at least partly, but have not similar odors mostly.
REFERENCES
[1] Salant, A. Nonnutritive sweeteners. In: Furia, TE. Handbook of Food Additives.
Cleveland: CRC Press, 1972.
[2] Luo, AS; Chun, Z; Luo, AX; Fan, YJ; Ge, SR. The survey and progress of the food
preservative. China Food Additives, 2005, 55-57.
[3] Wedzicha, RL. Chemistry of Sulphur Dioxide in Foods. 1st edition. London: Elsevier,
1984.
[4] Chichester, DF, et al. Antimicrobial food additives. In: Furia, TE. Handbook of Food
Additives. Cleveland: CRC Press, 1972.
[5] Zsolt, F, et al. A synthetic and in silico study on the highly regioselective Diels-Alder
reaction of the polyenic antifungal antibiotics natamycin and flavofungin. Tetrahedron
Letters, 2010, 51, 4968-4971.
[6] Ma, LR; Zhang, ZL; Li, H. New type food preservative-NISIN. Journal of Hebei
Academy of Sciences, 2001, 18, 180-182.
[7] Griffin, WC. Classification of Surface-Active Agents by HLB. Journal of the American
Oil Chemists' Society, 1949, 311.
Food Additives 303
[8] Ren, P; R, YW; Wang, LD. Properties of Plant Gum and Its Application in Food
Industry. Food Research and Development, 2004, 39-44.
In: Food Chemistry ISBN: 978-1-61942-125-7
Editors: D.Wang, H. Lin, J. Kan et al. © 2012 Nova Science Publishers, Inc.
Chapter 10
TOXICANTS IN FOODS
ABSTRACT
Microorganisms, plants and animals have evolved multiple defense systems against
predators. Among the systems, the chemical defense system is of special interest for the
food industry. Some of these compounds are toxic to specific microorganisms, insects,
birds, and mammals, but most of those are toxic to humans and can give rise to chronic or
acute symptoms of poisoning. Though some of the compounds occur in very low
concentrations, the compounds have a cumulative harmful effect if they constitute a part
of the normal diet over a prolonged period. Besides, food materials might be
contaminated by exogenous toxins. Intrinsic toxins and contaminants have been
recognized as the major components that affect food safety. This chapter introduces the
occurrence and properties of the most important toxicants in foods, including allergens,
toxic glycosides, toxic amino acids, lectins, saponins, toxins in aquatic organisms,
various antinutrients, heavy metals, pesticide residues, dioxins, veterinary and fish drug
residues, benzopyrenes as well as heterocyclic amines. Besides, measures for preventing
the generation of some toxicants are proposed.
1. INTRODUCTION
According to structure and biological effects on human body, toxicants in foods are
divided into toxic substances, harmful substances, and antinutrients. A toxic compound shows
its toxicity even in a very low dose, and a harmful substance is toxic only when its content
exceeds a certain threshold. An antinutrient may interfere in or inhibit the absorption of other
nutrients in foods. The definitions of these terms, however, are subject to changes due to the
306 Wang Dongfeng, Guoqing Huang and Shuhui Wang
improvement of analysis techniques and the availability of more data on their biological
effects. It has been found that some toxicants are beneficial in certain contents and some
substances are toxic or hazardous only in certain cases. For example, phenols in foods are
often recognized as antinutrients since they inhibit the adsorption of proteins. However,
phenols have the anti-oxidation and free radical scavenging capabilities and can be used as
natural antioxidants in foods. In addition, some well-known nutrients may be risky to certain
individuals, such as lactose, which may be deleterious to lactose-intolerant individuals.
According to origin, hazards in foods can be divided into inherent toxicants (or
endogenous toxicants) and contaminants (or exogenous toxicants). Endogenous toxicants are
metabolites produced via biosynthesis by food organisms under normal growth or metabolites
produced via biosynthesis by food organisms that are stressed. Contaminants refer to
toxicants that directly contaminate foods, toxicants that are absorbed from the environment by
food-producing organisms, toxic metabolites produced by food organisms from substances
that are absorbed from the environment, and toxicants that are formed during food preparation
[1].
It should be noted that all chemicals are potentially toxic, and that the dose alone
determines whether or not a toxic effect occurs. Indeed, toxicant (or toxin) is recently defined
as a ―substance that has been shown to present some significant degree of possible risk when
consumed in sufficient quantity by humans or animals‖ [2]. For example, pure water drunk to
excessive can induce an electrolyte imbalance and lead to death, which is called the ―water
toxicity‖ that is due in part to decreased renal capacity to excrete water [3]. The innumerable
308 Wang Dongfeng, Guoqing Huang and Shuhui Wang
naturally occurring chemicals in food are potentially capable of inducing toxic effects, but
few are ordinarily present in sufficient concentrations to actually show toxic effect [2, 4].
Hence, we should distinguish between ―toxic substance‖ and ―toxic effect‖. The most
frequently occurring toxicants in foods are listed in Table 10-1~10-3.
A substantial number of toxic substances have been isolated and identified This chapter
concerns only the most important toxicants that have been identified in foods.
2. ENDOGENEOUS TOXICANTS
Endogeneous toxicants include any substances produced by food materials (either plants
or animals) that are harmful to human beings. Lectins, saponins, and toxic peptides mentioned
above are endogenous toxicants.
2.1. Allergen
An allergen refers to any substance that can cause an allergy. Most immune responses of
caused by food components are IgE-mediated immediate allergic reactions. Upon exposure to
allergens, the lymphatic system of human body acts to avoid or alleviate the adverse effects.
Most antigens can be metabolized to monosaccharides, amino acids and lower fatty acids
after antigen-antibody reactions. However, complete-antigens, which are characteristic of
both immunogenicity and immunoreactivity, can cause immune reactions.
The intake of allergen-containing foods can cause allergic symptoms, such as pruritus,
functional gastrointestinal disorder and fever. Many foods have been found to contain
allergens, but the sensitivity to these foods varies with local diet, environmental factors and
possibly genetics. Epidemiological investigations reveal that the incidence of food-induced
allergy in infants and children is higher than that in adults and the incidence decreases as age
increases.
Food allergens share the following characteristics:
1. Allergens are present in most foods, such as milk, eggs, and soybean, of which, milk
and egg are the most important source of allergens. Though allergens occur widely in foods,
90% of food allergies are induced by only a small number of foods.
2. Only few food components are allergenic. For example, up to 23 types of
glycoproteins have been identified in white egg, but only ovalbumin, conalbumin, and
ovomucin are allergic.
3. The allergenicity of foods is subject to change after processing. For example, heat
treatment inactivates most allergens and the increase of acidity or the presence of digestive
enzymes reduces the allergenicity of foods.
4. Sensitive consumers could suffer allergic cross reactions. Some proteins contain the
same antigenic determinant and these proteins can cause allergic cross reactions. For instance,
at least 50% of patients allergic to cow‘s milk also react to goat‘s milk and patients allergic to
chicken eggs might be allergic to the eggs of other birds.
Toxicants in Foods 309
Plant Content
Cabbage 3~6
Savoy 18~31
Brussels sprout 10
Cauliflower 4~10
Kidney bean, turnip <1
Kohlrabi 2~3
Colza 2.5
Swedish turnip 9
Lettuce, Spanish, onion <1
2.2.2. Glucosinolates
Glucosinolates are quite stable. They are the precursors of isothiocyanates and are present
in much higher levels than their hydrolyzates in fresh plants. Glucosinolates can produce a
large variety of products when exposed to myrosinase as shown in Figure 10-2. In the case of
fresh plants chewing or tissue injury during cultivation, harvest, transport, and processing due
to scratching or freezing-thawing, glucosinolates get contact with myrosinase (EC 3.2.3.1)
and are hydrolyzed to toxic isothiocyanates.
Glucosinolates and their enzymatic hydrolyzates are water soluble. During cooking, more
than a half of the compounds are released to water, but the specific loss caused by processing
varies with vegetable species.
Myrosinase can be activated by Vc. Many facts have proved that myrosinase is inactive
in the absence of Vc. The activation is not due to the reducing property of Vc, instead due to a
nucleophilic group provided by Vc. Vc improves the Vmax and Km of myrosinase on its
substrates [6].
Toxicants in Foods 311
Toxic amino acids are rare amino acids that do not participate in protein synthesis, such
as homoserine, jenkolic acid, and 5-hydroxytryptophan. Toxic amino acids are usually the
structural analogs of protein amino acids and exert their toxicity as antimetabolites. Non-
proteinic amino acids are present in plants in quite low levels and certain non-proteinic amino
acids are found only in specific plants. For example, theanine is found only in the Camellia
family and the highest content is recorded in tea seeds, reaching 1% of dry weight; 5-
hydroxytryptophan is present only in the pea family and its content in Griffonic seeds
amounts to 14% by dry weight.
It should be noted that not all non-proteinic amino acids are toxic. Some rare amino
acids, such as theanine and alliin, can impart foods with special characteristics and healthy
functions. A summary of some unusual amino acids in food plants is given in Table 10-6.
2.3.1. Classification
Up to hundreds of non-proteinic amino acids have been identified in animals and plants
and most of them are the intermediate or final products of certain metabolisms in animals and
plants. Toxic amino acids can be divided into two categories according to their toxicity:
Table 10-6. Some toxic amino acids commonly occurring in plant foods and forages [7,8]
2.3.2. Toxicity
Toxic amino acids are not essential for human body and can interfere with the normal
amino acid metabolism. Djenko sickness is a disorder of the urinary tract and most cases are
caused by the intake of djenko bean, which contains the toxic djenkolic acid. In some legume
species, the contents of djenkolic acid can reach 1~2% and its content in black varieties is as
high as 3~4%. Djenkolic acid shares a similar structure with cysteine and thus can interfere in
the metabolism of this essential amino acid.
2.4. Lectins
2.4.1. Classification
Lectins occur widely in plants, animals, and microorganisms. Exogenous lectins are also
known as vegetable haemagglutinin. They are sugar-binding proteins or glycoproteins of non-
immune origin and can lead to selective red blood cell agglutination in human blood. Lectins
can reversibly bind to specific monosaccharides or oligosaccharides. Most lectins contain
more than one sugar-binding site for cross connection with oligosaccharides. The molecular
weight of lectins ranges from 91 kDal to 130 kDal. Lectins are natural antigen of red blood
cells and are heat stable. Some lectins are highly toxic to experimental animals. For example,
when mouse are orally fed with 80 mg/kg garlic lectin for consecutively 7 days, both the
appetite and body weight are significantly reduced.
Vegetable hemagglutinin is firstly discovered in castor seeds. To present, a large number
of lectins with different properties have been identified. According to structure, lectins are
divided into merolectin, hololectin, chemerolectin, and superlectin. Based on the specificity to
sugars, lectins can be of the fucose type, the galactose/N-acetyl galactosamine type, the N-
aceytl glucosamine type, the mannose type, the sialic acid type, or the glycoconjugate type.
According to the origin, lectins can be divided into legume-derived lectins, mannose-binding
lectins, chitin-binding lectins, type-2 ribosome-inactivating proteins (RIP), and lectins derived
from other crops. According to the agglutination to red blood cells, lectins can be categorized
as specific and non-specific lectins. Based on evolution and structure correlation, lections can
be divided into 7 families. Table 10-7 lists the structure, sugar specificity, and distribution of
the 7 families in crops.
Based on reported researches, Peumans W J divided the lectins that have been identified
in crops into 5 categories: (1) legume lectins. Legume lectins are a family of structurally
related lectins that occur exclusively within the legume family. In Spite of their structural and
evolutionary relationships, legume lectins exhibit a wide range of carbohydrate-binding
specificities. (2) Monocot mannose-binding lectins. Monocot mannose-binding lectins occur
in at least five different families (Amaryllidaceae, Alliaceae, Araceae, Liliaceae and
Orchidaceae). They all have a similar molecular structure and sugar-binding specificity. (3)
chitin-binding lectins.
Toxicants in Foods 313
to lectin poisoning. Experiments have proved that when mouse are fed lectin-containing crude
soybean powder, the mouse will suffer either enterocyte breakdown, leading to intestine
malfunction, or reduced activity of hydrolytic enzymes in stomach and intestine, leading to
decreased nutrient adsorption and inhibited growth.
2.5. Saponins
Saponins are a complex group of compounds and consist of saponin, sugar, uronic acid or
other organic acids. Most saponins are white and amorphous powders and tastes bitter and
spicy. Saponins are insoluble in nonpolar solvents but are soluble in water-containing polar
solvents. Saponins can irritate the mucous coat of digestive tract and lead to local hyperemia,
316 Wang Dongfeng, Guoqing Huang and Shuhui Wang
Saponins are widely distributed in plants as well as in some marine animals. The reports
on saponins-induced food poisoning are emerging in recent years. For example, poisoning
caused by the ingestion of improperly cooked kidney bean is quite common in China and
saponins have been confirmed as a cause of the poisoning. One of the most intensively
studied saponins is tea saponins and their structure, composition, and physiological-
biochemical properties have been well elucidated. The following describes the structure,
properties, and toxicity of saponins by taking tea saponins as an example.
Molecular
Ligand Melting point (°C) Empirical formula
weight
R1-barrigenol 303~308 506 C30H50O6
Theasapogenol B 284~288 490 C30H50O5
Theasapogenol D 285~286 474 C30H50O4
A1-barrigenol 285~287 490 C30H50O5
Toxicants in Foods 317
R1-barrigenol Theasapogenol B
Theasapogenol D A1-barrigenol
TTX is an extremely toxic natural toxin and is roughly 100 times more poisonous than
potassium cyanide. The LD50 (i.v.) to mice is 8.7μg/kg.
2.6.5. Actinotoxins
Actinotoxins are toxin derived from extracts of the tentacles of sea anemones. To present,
more than 60 kinds of cytolysin toxins have been isolated from sea anemones. Cytolysins are
substances or antibodies raised by microorganisms, plants or animals that are specifically
toxic to individual cells. The molecular weights of sea anemone-derived cytolysins range
from 15000 to 20000 and can selectively bind to the lipids on cell membranes, causing pain,
inflammation, and muscular paralysis. The most intensively studied actinotoxin is the
cytolysin isolated from anthoplerin. The molecular weight of the cytolysin is 17000 and is
characterized by a long hydrophobic β-sheet section and 5 short hydrophobic β-hydrophobic
sections in the N terminal, in which, 60%-70% of amino acids are hydrogen bonded and form
a transmembrane structure. The C terminal is highly hydrophilic and locates on the outside
surface of membrane, which forms a transmembrane channel.
Figure 10-9. Structures of OA and DTX-1, and DTX-2. OA: R1=CH3, R2=H, R3=H, DTX-1: R1=CH3,
R2=CH3, R3=H, DTX-2: R1=H, R2=CH3, R3=H.
2.6.6. Conotoxins
Conotoxins (CTXs) are a group of neurotoxic peptides isolated from the venom of the
marine cone snail, genus Conus. CTXs are highly poisonous to human body and the
selectivity varies with the living habits of cone snails. Among the CTXs identified, that
isolated from Conus gegraphus Linnaeus is the most poisonous.
The structures of more than 100 CTXs have been elucidated. A majority of CTXs
characterized from venoms so far are 12–30 amino acids (AA) in length and contain one or
more disulfide bonds. CTXs are initially translated as propeptide precursors, approximately
80–100 AA and the biologically active toxins are produced by proteolytic cleavage from the
precursors. Conotoxins can act on a wide range of targets and are highly tissue specific. CTXs
have been used as probes in the classification and identification of ion channels and receptors.
CTXs are potential drugs or leading compounds for new drug development.
Toxicants in Foods 321
2.6.7. Cyanotoxins
Cyanotoxins are produced by cyanobacteria (also known as blue-green algae). The
mechanisms of cyanobacterial toxicity currently described and understood are very diverse
and range from hepatotoxic, neurotoxic and dermatotoxic effects to general inhibition of
protein synthesis. Cyanotoxins fall into three broad groups of chemical structure: cyclic
peptides (including microcystins and nodularins), alkaloids (including neurotoxic anatoxins
and saxitoxins, cytotoxic cylindrospermopsin and demethoxy-cylindrospermopsin, and
dermatotoxic aplysiatoxins and lyngbyatoxin) and lipopolysaccharides.
The nutritional status of plants and animals are closely associated with the environment
and fertilizer or feed. When minerals in the environment and fertilizer or feed are deficient or
excessive, the minerals in the corresponding foods are also in shortage or excess. Plants and
animals accumulate both essential and harmful minerals and finally affect the mineral
contents of top predators in the food chain. For example, the Keshan disease and kashin-beck
disease suffered by residents in Se-deficient areas are possibly due to Se deficiency in foods.
If the human body intakes excessive minerals, especially heavy metals, poisoning occurs. The
world-famous Minamata disease is a result of Hg pollution.
In addition to water and air, the contents of heavy metals in human body are mainly
affected by their contents in foods. When human beings consume foods derived from plants
or animals with strong heavy metal accumulation capabilities, the metals will exceed
thresholds and cause potential harm on human body.
Living bodies do not show deficiency for non-essential metals, such as Be, Hg, Pb, and
Sb. However, once the contents of these metals exceed certain thresholds, toxicity symptoms
appear.
1. Heavy metals disrupt the functional groups of bioactive molecules. For example,
Hg(II) and Ag (II) can bind to the –SH of cysteine residues in enzymes and interrupt the
enzymatic reactions mediated by the –SH group.
2. Heavy metals replace the metal cofactors in biomolecules. The activity of
metalloenzymes is closely associated with metals. Due to the different macromolecule-
binding stability of metals, a metal with a higher stability constant replaces another metal
with lower stability constant and consequently inactivate the metalloenzyme.
3. Heavy metals change the conformation or higher-order structures of biomolecules. For
example, polynucleotides are units for genetic information storage and transfer. Heavy metals
can bind to the units and change their structures. This is why heavy metals readily cause
cancer and teratogenesis.
Proteins, phosphatides, some sugars and nucleonic acids can provide atoms for
coordinating with metal ions, such as the nitrogen atom in imidazole (histidine), NH2 (lysine),
purine and pyrimidine bases in DNA and RNA, oxygen atom in the hydroxyl group (serine,
tyrosine), COO- (glutamic acid and aspartic acid), PO43- (phospholipids, nucleic acids), and
sulfur atom in –SH (cystine) and SR (methionine, CoA). The three atoms are good ligands for
metals.
In metal activated enzymes, the prosthetic metals often bind loosely to the enzymes. The
metals can be easily replaced by other metals and the functions of the enzymes are destroyed
as a result. In metalloenzymes, metals bind tightly to the enzymes and their replacement by
other metals is difficult. However, during enzyme synthesis, metal replacement may occur
readily.
Cell wall, cell membrane, and organelle membrane are the main barrier of metal intake.
Generally, lipophilic metal ions with less charge can permeate the barriers easier. For
example, CH3Hg+ has a higher permeability than Hg2+ and the permeability of (CH3)2Hg is
greater than CH3Hg+. Based on these facts, it can be deduced that M2+ coordinated with a
organic ligand can enter cells easier than its hydrate form [M2+(H2O)n].
Metals can change the permeability of cellular membranes by initiating lipid peroxidation
and the changes vary with the affinity of metals to the ligands on membrane surface. The
peroxidative degradation of lipids in cell and organelle membranes is lethal to life systems.
For example, the increase of permeability and hemolysis of red cell has been related to the
peroxidative degradation of lipids. Lipid peroxidation is a special form of cell damage and
occurs mainly to polyunsaturated fatty acids in membranes. Under normal conditions, the
damage caused by low metal levels can be repaired by intracellular molecules such as vitamin
E and Se-containing glutathione peroxidase.
Toxicants in Foods 323
Pesticides are the collectives of pure or mixture compounds derived from organisms or
other natural substances for the prevention, diminish, or control of diseases, insects, grasses,
and other harmful organisms that adversely affect agriculture and forestry or for regulating
the growth of plants and insects. Based on purposes, pesticides are subdivided into
insecticides, fungicides, herbicides, nematicides, acaricides, rodenticides, defoliants, and
plant growth regulators, of which, insecticides, fungicides, and herbicides are the most widely
used. According to chemical composition and structure, pesticides can be organophosphorus,
carbamate, organochlorine, pyrethroid, organoarsenic, or organomerurial.
Hydrolysis
Due to the presence of polar P=O or P=S bond in phosphoryl compounds, the P atom
posses valid positive charge and is highly electrophilic. Hence, substitution reactions occur
easily to electrophilic reagents. The hydrolysis susceptibility of organophosphorous pesticides
to alkaline, neutral and acidic conditions is related with their structures. Hydrolysis leads to
the breakdown of the P-O-C or P-S-C bond and activity loss.
All phosphate pesticides contain the phosphate bond P-O-C. Two electrophilic centers (P
and C) exert effects in the hydrolysis of the bond. According to the Lewis‘s acid-base theory,
P serves as a hard acid and C serves as a soft acid. The hard base –OH attacks the P atom with
priority and breaks the P-O linkage. The soft base H2O attacks the C atom with priority and
lead to the breakdown of the O-C linkage.
324 Wang Dongfeng, Guoqing Huang and Shuhui Wang
Phosphorylation
The substitution reaction between phosphoryl compounds and nucleophilic agents may
yield two types of products. If the P atom is attacked, a phosphoryl compound is produced; if
the α-C atom is attacked, an alkyl product is yielded, as shown in Figure 10-5.
The phosphorylation reaction is essentially the nucleophilic substitution reaction occurred
in the P atom. The H atom connected to O, S, and N of nucleophilic reagents can be
substituted by phosphoryl group to yield new phosphoryl products. The phosphorylation
reaction is important for the preparation of natural phosphoryl compounds and their
biochemical aspects. The inhibition of esterase and the toxicity against animals by
organophosphorous pesticides are attributed to the phosphorylation reaction.
Figure 10-5. Substitution reactions between phosphoryl compounds and nucleophilic agents.
Alkylation
As mentioned above, when a nucleophilic agent attacks the α-C of the phosphate group,
the alkyl group is detached from the phosphate and the phosphate anion and alkylated
compound are generated. Many nucleophilic reagents can react with phosphoryl compounds
for alkylation. For example, amine compounds and sodium iodide have been used in the
production of demethylated derivatives of organophosphorous pesticides. Many sulfide
compounds, such as dithiophosphates, dithiocar-bamates, thiol, thioether, thiocyanates, and
thiourea are dealkylation agent of phosphates.
Oxidation and reduction
The nitro group in the benzene ring of parathion, fenitrothion, and ethyl-p-nitrophenyl
can be easily reduced to amine and the reducing products are no longer effective.
3.2.3. Pyrethroids
Pyrethroids are high-efficay and low-toxicity insecticides and acaricides. Pesticides of
this category include deltamethrin, prallethrin, cyphenothrin, and cyhalothrin. The effective
doses of pyrethroids are less than 10 gram per hectare. In environment, pyrethroids are
destroyed mainly by photo degradation (leading to isomerization, ester linkage breakdown,
and dehalogenation), followed by hydrolysis and oxidation. However, insects can evolve
resistance to pyrethroids in a short time. Hence, pyrethroids are often used together with other
pesticides to reduce the resistance issue.
Pyrethroids are divided into two groups based on their chemical structure and action
mechanism. Group I pyrethroids do not contain the cyano group. Commonly used group I
pyrethroids include allethrin, bifenthrin, tetramethrin, ethofenprox, and permethrin. Group I
326 Wang Dongfeng, Guoqing Huang and Shuhui Wang
3.2.4. Carbamates
Pesticides of this category include tricarnam, aldicarb, bufencarb, carbofuran, methomyl,
and propoxur. Carbamates are characterized by quick action, high selectivity, low toxicity to
homothermal animals, fishes, and human, easy degradation by soil microorganisms, and less
accumulation in organisms. Carbamates exert their toxicity as cholinesterase inhibitors, which
is similar to that of organophosphorous pesticides. After carbamates are hydrolyzed, the
activity of cholinesterase can be partially restored.
The term dioxin is commonly used to refer to a family of toxic chemicals that all share a
similar chemical structure and a common mechanism of toxic action. This family includes 7
of the polychlorinated dibenzo dioxins (PCDDs), 10 of the polychlorinated dibenzo furans
(PCDFs) and 12 of the polychlorinated biphenyls (PCBs). Dioxin is defined by World Health
Organization (WHO) and United Nations Environment Program (UNEP) as persistent organic
pollutants (POPs). POPs are chemical substances that persist in the environment,
bioaccumulate through the food web, and pose a risk of causing adverse effects to human
health and the environment. Due to the similarities in biochemistry and toxicological
properties, some halogenated aromatic hydrocarbons, such as polychlorinated diphenyl ethers
(PBDEs), polychlorinated naphthalene (PCNs), polybrominated dibenzodioxin/furan
(PBDD/Fs), polybrominated biphenyls (PBBs), and other halogenated aromatic hydrocarbon
mixtures are also classified as dioxin-like compounds.
3.3.1. Dioxins
Dioxins are a group of planar aromatic hydrocarbons that are substituted by multiple
chlorides and share similar structure and physic-chemical properties. Dioxins are oxygen
containing chlorinated tricyclic aromatics. Seventy five PCDDs and 135 PCDFs have been
defined as dioxins. The most intensively studied toxic dioxins are 17 congeners, whose –H
atoms in positions 2, 3, 7, and 8 are substituted by chloride. 2,3,7,8-Tetrachlorodibenzo-p-
Toxicants in Foods 327
dioxin (TCDD) is the most toxic dioxin among all known congeners (oral LD50 1µg/kg bw).
TCCD is highly carcinogenic and can interfere in endocrine in extremely low concentrations.
Dioxins are the by-product of combustion and various industrial processes. The sources of
environmental dioxins include chlorphenols used in wood preservation and blood fluke
prevention, combustion, defoliant, insecticides preparation, paper bleaching, and automobile
exhaust.
Thermal stability.
PCDD/Fs are extremely heat stable. The lowest temperature for degradation is 800 °C
and substantial degradation occurs in 1000 °C and higher temperatures.
PCDD/Fs can exist in both the gaseous phase and bind to particles. The two key
parameters, the congener‘s vapor pressure and the ambient air temperature, govern the
partitioning between gaseous phase and particle.
Fat solubility
PCDD/Fs are extremely lipophilic. The log of the distribution coefficient between octane
and water reaches up to 6. Hence, PCDD/Fs transfer and accumulate through the food chain
mainly via lipids.
Environmental stability
328 Wang Dongfeng, Guoqing Huang and Shuhui Wang
PCDD/Fs are resistant to physical, chemical, and biochemical degradations and can
persist in environment. UV light can rapidly destroy PCDD/Fs. However, PCDD/Fs in air are
absorbed on gasoloid particles and hence quite resistant to UV degradation. In soil, PCDD/Fs
are stable against physical, chemical, and biological degradation and the average half life
reaches 9 years.
3.3.4. Toxicity
PCDD/Fs are extremely toxic. In contrast to common acute toxicants, death occurs
several weeks post PCDD/Fs intake. After ingestion, the body weight of animals decrease
sharply in the early phase, accompanied by emaciation syndromes, including significant
muscle and fat tissue reduction. The uptake of sublethal dose leads to body weight loss and
the effect is dose dependent.
In experimental animals, sublethal dioxin induces thymic atrophy by reducing the number
of lymphocytes in thymic cortex. According to published researches, human thymus is also
sensitive to dioxins. A characteristic symptom of dioxin poisoning is chloracne [12].
Chloracne can cause skin accretion or hyperkeratosis [13] and pigmentation [14].
Dioxins are hepatoxic. Dioxins in high levels cause liver enlargement and subsequent
degeneration and necrosis in experimental animals. Besides, dioxins have reproductive
toxicity and carcinogenicity. It is reported that dioxins stimulate the hydroxylation of
dihydrotheelin and decrease the dihydrotheelin concentration in blood. Dioxins can change
the morphology of testis and affect the formation of sperm. The strong carcinogenicity of
2,3,7,8-TCDD has been evidenced in rodents and the minimum dosage for liver cancer in
mice is as low as 10 pg/kg body weight.
The veterinary drug residues in foods include both original drugs and their in vivo
metabolites. Original drugs and their metabolites might covalently bind to intrinsic molecules
as bound residues. The main veterinary drug residues include antibiotics, sulphonamides,
furanes, coccidiostats, hormones and anthelmintics, of which, antibiotics and hormones are
the most important healthy risks for human body.
Penicillins
Penicillins refers to group of compounds containing the penicillin core and includes
penicillin F, penicillin G, penicillin X, penicillin K and dihydropenicillin F. The penicillin
core structure is shown in 10-7. Table 10-14 lists the structures of the R side chain of
common penicillins and some properties.
Penicillins are monoacid and can form salts with potassium, sodium, calcium, magnesium
and many other ions. Penicillins are readily soluble in organic solvent such as alcohols,
ethers, and esters. Penicillin salts are readily soluble in water. Free penicillins and their salts
are quite unstable in aqueous solutions and are liable to heat treatment, but crystallized
penicillins and their salts are quite stable and can be stored for several years in room
temperature.
Toxicants in Foods 329
The antibacterial potency of penicillins is related to the stability of the lactan ring, in
which, the peptide bond can be broken by acids, bases, heavy metals or penicillin enzymes,
causing activity loss. Figure 10-8 and Figure 10-9 illustrate the hydrolysis of penicillins under
acidic and alkali conditions.
Molecular
Melting
Trivial name Chemical name Side chain R weight of
point (°C)
sodium salt
CH3-CH2-
Penicillin F 2-pentene penicillin 334.2 204~205
CH=CH-CH2-
CH3-(CH2)5-
Penicillin K n-heptylpenicillin 364.3
CH2-
CH3-(CH2)3-
Dihydropenicillin F n-Amyl penicillin 336.3
CH2-
Streptomycin
Chloramphenicol
Tetracyclines
Tetracyclines are amphoteric. Tetracyclines and their salts are yellow or light yellow
crystals and are extremely stable in dried state. They are soluble in diluted acid and alkaline
solutions, slightly soluble in water and lower alcohols, and insoluble in ethers or petroleum
ether.
Thyroxine
Thyroxine stimulates the metabolism of sugars, proteins, lipids and salts, promotes
growth and tissue differentiation, and significantly affects the central nervous system,
circulatory system, hematopoiesis and muscular work of organisms.
Female hormones
Female hormones include hormones secreted by the ovarian follicle before ovum
maturation such as estradiol and progesterone secreted by corpus luteum. The structures of
common female hormones are shown in Figure 10-13.
Male hormones
Testosterone is the most important male hormone in human body. It is secreted by the
interstitial cells of testicle. Testosterone can be metabolized to androsterone, which can be
further converted to dehydroepiandrosterone (DHEA). The structures of these compounds are
given in Figure 10-14.
Among the male hormones mentioned above, testosterone is the most active and its
activity is 5 times higher than that of androsterone. DHEA is the least active and its activity is
only one-third of that of androsterone.
Although female and male hormones have different functions in human body, they share
quite similar structure. Both female and male hormones are derived from cholesterol and can
be converted to each other.
metabolic enhancers (hormones), Chinese herbal medicines, biological products, and others.
According to preparation methods, fishery drugs are divided into chemical drugs, biological
drugs, biochemical drugs, and feed additives.
4. ANTI-NUTRIENTS IN FOODS
The nutritional values of animal- and plant-derived foods are determined by the
nutritional composition of their edible parts. However, to meet the requirements for growth,
propagation, and protection against invasions of microbes and predators, animals and plants
have evolved effective protection systems, such as morphology change and chemical
secretion. Besides, the accumulation of proteins or protein complexes in seeds or other edible
parts is another measure against external attacks, such as enzyme inhibitor, amylase inhibitor,
and sugar-binding proteins. These compounds are collectively termed anti-nutrients. If anti-
nutrients are present in high levels, the adsorption and utilization of nutrients in foods will be
affected.
Phytic acid is contained mainly in the seed, stem, and root trunk of plants and the highest
content is found in the seed of legumes and the bran and embryo bud of cereals. Phytic acid
can react with Ca, Fe, Mg, Zn, and other elements to form insoluble products and reduce their
bioavailability. In addition, phytates also form complexes with proteins. Phytic acid occurs
widely in plant-derived foods and is a main anti-nutrient that affects mineral absorption.
Each phytic acid molecule has 12 dissociable protons, of which, 6 protons are highly
acidic (pKa=1.84) and are completely dissociated in water, 2 protons are weak acidic groups
334 Wang Dongfeng, Guoqing Huang and Shuhui Wang
(pKa=6.3) and the rest 4 protons are extremely weak acidic groups (pKa=9.7). Phytic acid can
complex with most metals and the stability of the complexes is closely associated with the
acidity of foods and the properties of metals. For example, the stability of some essential
metal-phytic acid complexes in pH 7.4 is Cu2+ > Zn2+ > Co2+ > Mn2+ > Fe3+ > Ca2+. The
complexes of phytic acid with proteins, Ca2+, and Mg2+ are water-soluble, whereas those with
most heavy metals are only slightly water soluble.
Due to the high contents in plant-derived foods, phytic acid can bind to endogenous Zn,
Cu, and other metals in pancreatic juice and bile that are secreted by organs to small intestine.
Hence, phytic acid not only affects the bioavailability of food-derived trace elements, but also
hinders the re-adsorption of endogenous trace elements.
Phytic acid has strong chelating capability. Each phytic acid molecule contains six
negatively-charged phosphate groups and can complex with proteins as well. When the
medium pH is lower than the pI of a protein, the protein carries positive charges. Due to
strong electrostatic interaction, the protein binds to negatively-charged phytic acid and
insoluble complex is formed. When the medium pH is higher than the pI of a protein, the free
carboxyl groups and the unprotonated imidazolyl in histines are negatively charged. In this
case, the protein forms a ternary complex with phytic acid by using Ca2+, Mg2+, or Zn2+ as the
bridge. The formation of the ternary complex reduces the solubility of proteins and
consequently decreases protein digestibility. For example, casein completely dissolves in pH
2 medium. If phytic acid is added, casein is nearly completely precipitated. The same effect
also applies to proteins extracted from corn, sunflower seed, soybean meal, and rice bran.
However, after phytic acid is degraded by phytase, the solubility of the proteins increase
tremendously and some even exceed the original values, such as the proteins derived from
fine rice bran and rapeseed.
Chemical property
Oxalic acid is also termed ethane diacid and is widely present in plant-derived foods.
Pure oxalic acid is colorless crystal and is readily soluble in water but not soluble in ether or
other organic solvents.
Oxalic acid is another strong metal chelator found in plant-derived foods. When oxalic
acid binds to alkaline earth elements, the solubility of the metals is significantly reduced. For
example, calcium oxalate is nearly insoluble in water (Ksp=2.6×10-9). Hence, oxalic acid
significantly reduces the bioavailability of some minerals. It should be noted that formation of
complex with some transition metals can significantly improve their solubility. For example:
20
Fe3 3C2O4 [Fe(C2O4 )3 ]3 ( Kf=1.06×10 )
Toxicity
Intake of excessive oxalic acid leads to urethral calculus and reduces the bioavailability
of essential minerals.
Toxicants in Foods 335
4.2. Polyphenols
Polyphenols are widely distributed in plant-derived foods, but their species and contents
vary significantly. Due to the presence of multiple hydroxyl groups, polyphenols are
susceptible to oxidization and are natural antioxidants in foods. Besides, polyphenols have
free radical scavenging, bacterostasis, and cancer prevention functions. Hence, polyphenols
are known as functional components in foods. However, polyphenols can complex with some
essential trace elements, precipitate proteins, and inhibit the activities of certain enzymes. In
this sense, polyphenols are natural anti-nutrients.
the most chemically active among polyphenols. Polyphenols are unstable and are easily
destroyed by high pH, high temperature, and high oxygen concentrations. Besides, oxidases,
oxidants, and metal ions also affect polyphenol stability.
Antinutritional effect
Toxicity
Figure 10-17. Relationship between catechin content and protein adsorption in fermented sorghum
products [16].
When positions 3‘ and 4‘ in ring B of flavones are connected with –OH, the flavones can
easily form quinoid oxidates by enzymatic and automatic oxidation. The quinoid oxidates can
complex with GSH, as shown in Figure 10-19.
Trypsin inhibitor (LT1), chrymotrypsin inhibitor, and α-amylase inhibitor are major
digestive enzyme inhibitors. These inhibitors are evolved by plants and animals as defensive
measures against predators. The presence of these inhibitors affects the digestion and
adsorption of nutrients and even threatens the health of consumers. For example, the intake of
uncooked or under-cooked soybean products can cause nausea, vomiting, and other
symptoms.
338 Wang Dongfeng, Guoqing Huang and Shuhui Wang
4.3.1. Properties
Protease inhibitors are widely present in microbes and the tissues of plants and animals.
Legume seeds have higher protease inhibitor contents than other sources. Protease inhibitors
derived from legume seeds are divided into the Kunitz type and the Bowman-Birk type.
Kunitz protease inhibitors have relatively higher molecule weights of about 20000 Dal and
specifically bind to trypins. Bowman-Birk protein inhibitors have lower molecule weight of
about 9000 Dal and two binding sites. Hence, Bowman-Birk protease inhibitors can bind two
serine proteases, trypins, or chymotrypsins at the same time. Kunitz protein inhibitors are
sensitive to heat treatment, but Bowman-Birk protein inhibitors are quite heat resistant.
Protein inhibitors of difference sources are quite similar in amino acid composition. That
is, cystine has the highest content, followed by aspartic acid, arginine, lysine, and glutamic
acid in sequence. The high content of cystine facilitates the formation of intra-molecular
disulfide bonds, which make the inhibitors heat and acid resistant.
The action mechanism of protease inhibitors against target enzymes is well elucidated in
recent years. The interactions can be divided into three types:
Complementary type: Inhibitors bind to the recognition and binding sites of target
enzymes and block the activity center by hydrogen bonding with active groups. For example,
trypsin inhibitor takes effect in this way.
a)
"SH
"TO "TO
b)
Figure 10-21. (a) Stereoview of the Ca-atom backbone of STI (a) and LTI (b). Only the positions of
Arg63 and Asn11 are indicated in the structures.
(b)
Interaction between Arg62 (P1) of LTI and S1 residues of trypsin (shown in pink color) [18].
Associated type: Inhibitors do not occupy the recognition sites of target enzymes. Instead,
the inhibitors associate with target enzymes for hydrogen bonding with the active groups of
target enzymes and block the substrate binding site. The interactions between thrombin
inhibitors, such as hirudin, and their substrates are of this type.
Covered type: Inhibitors cover the areas close to the active center of target enzymes as
linear molecules to prevent the contact between active center and substrate. For example,
papain inhibitor is of this type.
The high temperature used in roasting and frying can cause oxidization or polymerization
of some compounds in foods, especially lipids. Lipid oxidation and thermal denaturation
Toxicants in Foods 341
significantly affect the flavor, color, shelf life, and safety of lipid-containing foods. Many
diseases have been associated with lipid oxidation and their thermal products.
5.1.4. Benzo(α)Pyrene
Benzo(α)pyrene is a polycyclic aromatic compound that is often found in smoked and
roasted foods. This chemical is present in very low level in common conditions. However,
after foods are roasted or smoked, its content increases significantly. Benzo(α)pyrene is now
recognized as one of the most carcinogenic, teratogenic, and mutagenic substances in the
world.
Physicochemical properties
(α)P has the most significant effect on food safety among PAHs. To date, a total of more than
two hundred kinds of PAHs and PAH derivates have been identified and many of them are
extremely carcinogenic and mutagenic. Figure 10-24 shows the structures of some common
PAHs. Of the PAHs, 3,4-benzo(α)pyrene is the most widely distributed and is highly
carcinogenic. 3,4-Benzo(α)pyrene is often regarded as the representative of PAHs.
Figure 10-23. Structure of PCBs. (left) PCB; (right) chlorinated dibenzofuran (X can be substituted
by chlorine).
Toxicity
incidence of cancer and shortened incubation period. In the case of mice, injection of 4-12 μg
benzo(α)pyrene induces cancer and the half carcinogenic dosage is 80 μg.
The carcinogenicity of PAHs is associated their chemical structures. Carcinogenicity is
only observed in PAHs with four to seven benzene rings. PAHs with less than four or more
than seven rings are not carcinogenic. Population and epidemiological investigations indicate
that benzo(α)pyrenes and other PAHs can be absorbed through respiratory tract, digestive
tract, and skin. B-(α)P can cause gastric cancer, lung cancer, or skin cancer in human. Iceland
has the third highest incidence of gastric cancer and the reason has been associated with
smoked foods in the diet of Iceland residents. Besides, the incidences of gastrointestinal tract
and respiratory tract cancers are three times higher than those of inland populations. The
carcinogenic incubation period of benzo(α)pyrene in human beings ranges from 20 to 25
years.
5.1.6. Acrylamide
Acrylamide is carcinogenic and can cause nerve damage. A food can be contaminated by
acrylamide if the food is processed by frying or roasting. Acrylamide has been identified in
carbohydrate-rich foods that are processed in temperatures higher than 120 °C for a long time,
such as fried potato chips. The contents of acrylamide in fried foods often exceed 1000μg/kg.
In overcooked fried potato chips, the acrylamide level reaches up to 12800 μg/kg.
Acrylamide is a simple molecule with molecular weight (CH2CHCONH2) of 71.09.
Acrylamide melts in 87.5 °C and boils in 125 °C. Acrylamide is the block for polyacrylamid
synthesis. Acrylamide is a white crystal. It is soluble in water, methanol, ethanol, acetone,
dimethyl ether, and trichloromethane, and is insoluble in heptane or benzene. Acrylamide is
stable in acidic medium, but is degraded in alkaline solutions. Self-polymerization occurs
easily in the melting temperature or when exposed to UV light.
344 Wang Dongfeng, Guoqing Huang and Shuhui Wang
Content in foods
According to published reports, nearly all foods contain acrylamide. The acrylamide limit
of WHO in tape water is 0.5 μg/kg (1993). However, investigations reveal that the acrylamide
contents in foods that are rich in carbohydrates and processed by frying or roasting are much
higher than the allowed value in tap water. For example, the average content of acrylamide in
fried potato chip (slice) is 1000 μg/kg and that in infant biscuit is 600-800 μg/kg.
Acrylamide is mainly found in foods that are processed in temperatures higher than 120
°C. High contents of acrylamide have been detected in most fried potato chips, part bread,
cocoa powder, apricot kernel, coffee, and biscuits.
Generation pathway
(1) Amino acids are degraded in high temperatures and the degradation products react
with reducing sugars to produce acrylamide;
(2) The primary reaction product N-glucoside of the Maillard reaction plays important
role in acrylamide formation;
(3) α-Dicarbonyl compounds react with amino acids to release acrylamide;
Toxicants in Foods 345
(4) Strecker degradation facilitates the formation of acrylamide, because aldehydes are
generated during the degradation;
(5) Free radicals might also involve in acrylamide formation;
(6) More than one pathway might contribute to acrylamide formation.
In addition to intrinsic formation during food processing, acrylamide might come from
other sources. Acrylamide can immigrate from polyacrylamide-based packaging materials to
foods or from flocculating agent.
Toxicants in Foods 347
Temperature: Acrylamide is produced only in temperatures higher than 120 °C. When the
equimolar (0.1 mol) mixture of asparagine and glucose is incubated, acrylamide is detected in
temperatures higher than 120 °C and its content increases during temperature elevation until
170°C. When the temperature is further increased, acrylamide content tends to decrease and
no acrylamide is detected when the temperature exceeds 185°C.
Heating duration: When glucose is incubated with asparagines, glutamine, or methionine
for 5~60 min, differences in acrylamide formation are found. The highest acrylamide content
is detected in the asparagines-glucose mixture, but the content decreases after 5 min. In the
glutamine-glucose system, the acrylamide content peaks within 10 min and then remains
constant in subsequent incubation. In the case of the methionine-glucose system, the
acrylamide content increases during prolonged incubation 30 min after the onset of the
reaction, but reaches a constant level in subsequent heating.
Carbohydrate species: When glucose, fructose, or lactose is incubated with asparagines,
high acrylamide contents are detected in all the three systems, indicating that carbohydrate
species plays less role in acrylamide formation. The carbonyl groups generated by lipid
oxidation stimulate acrylamide formation.
Amino acid species: When carbohydrates and amino acids are heated separately, no
acrylamide is produced. However, when the two compounds are heated together, acrylamide
formation is detected. Asparagine is the most susceptible to acrylamide formation with
carbohydrates among all the amino acids. When asparagine is heated with glucose, the
acrylamide content produced is hundreds to more than 1000 folds higher than that of the
glutamine-glucose or methionie-glucose mixture. This is why fried potato chips have high
acrylamide contents.
Water content: The formation of acrylamide seems to be a surface reaction and the water
contents of foods significantly influence acrylamide formation. High water contents facilitate
the flow of reactants and products and consequently lead to more acrylamide formation.
However, too high a water content causes diluted reactants and reduces the reaction rate. This
phenomenon is quite similar to the Maillard reaction.
5.2.1. Properties
Nitrates can be converted to nitrites in mammals and nitrites can further react with
amines, amino compounds, and amino acids to yield N-nitroso compounds. Nitrates are not
poisonous, but nitrites and N-nitroso compounds are toxic to mammals. Hence, the
conversion to nitrites and N-nitroso compounds must be considered in the safety evaluation of
nitrates.
Nitrites are oxidized to nitrates in the presence of reductants and reducants can be used to
decrease nitrites accumulation and conversion. It has been proposed to add nitrites and Vc or
Ve simultaneously in cured meats to reduce nitrite residue.
R1
N N O
N-nitroso compounds share the R2 structure. Chemically, N-nitroso
compounds can be divided into N-nitrosamines and N-nitrosamides. According to volatility,
N-nitroso compounds can be classified as volatile and non-volatile N-nitroso compounds.
348 Wang Dongfeng, Guoqing Huang and Shuhui Wang
In N-nitroso compounds, if groups R1 and R2 are the same, the compounds are
symmetric; otherwise, the compounds are asymmetric. R1 and R2 can be alkyl groups, such as
N-nitrosodimethylamine (NDMA) and N-nitrosodiethylamine (NDEA), aromatic
hydrocarbons, such as N-nitrosodiphenylamine (NDPhA), naphthenic bases, such as N-
nitrosopyrolidine (NPRY), N-nitrosomorpholine (NMOR), N-nitrosopiperidine, and N-
nitrosopiperazine, and amino acids, such as N-nitrosoproline (NPRO) and N-nitrososarcosine
(NSAR).
Low-molecular weight nitrosamines are yellow liquid in room temperature, and most
high-molecular weight nitrosamines are solid. Most nitrosamines are insoluble in water,
except some N-nitrosamines, such as NDMA, NDEA, and some N-nitroso amino acids. All
N-nitrosamines are soluble in organic solvents and are stable against spontaneous hydrolysis.
N-nitrosamines can be converted to carcinogenic compounds after being metabolized in
human body.
R1
N N O
The general structure of N-nitrosylamines is XCY , such as N-nitroso
formylamine, N-nitroso methylurea, N-nitroso ethylurea, N-nitroso urethane, N-nitroso-N‘-
nitro-methylguanidine.
N-nitrosylamines are unstable and can be directly decomposed to diazonium compounds,
which are carcinogenic and mutagenic by binding DNA.
5.3. Chloropropanols
With the increase of demand on flavorings, the soy sauce processing technique undergoes
large evolutions during recent years. Hydrolyzed vegetable proteins have been used in soy
sauce production to improve quality and reduce cost. If the hydrolysis condition is not well
controlled, toxic chloropropanols may be generated. Chloroproanols can cause cancers in
liver, kidney, and thyroid and affect fertility. Chloropropanols have turned to be another
hotspot in the food pollutant area in addition to dioxins.
Toxicants in Foods 349
5.3.2. Toxicity
Because chloropropanols reduce the number and activity of sperms and inhibit the
formation of male hormone, male contraceptives have been developed based on 3-MCPD.
Due to the potential carcinogenicity, sperm inhibition, and kidney toxicity, many countries
have set up limits for chloropropanol residue in foods.
During processing, storage, and transportation, foods must contact various containers,
utensils, and packaging materials. Some components in containers and packaging materials
might migrate or dissolve in foods and cause chemical pollution in foods. Hence, containers
and packaging materials are potential risks for food safety.
Many types of containers and packaging materials have been used in the food industry in
the history of China, such as bamboo wood, metals, glass, enamel, and ceramics. Years of
practice have proved that most of them are safe for human body. However, with the rapid
development of the food industry and chemical synthesis technologies, many new synthetic
materials, such as plastics, coatings, and rubbers, have emerged and gained wide applications
in food packaging. These synthetic materials contain potential toxicants and some can migrate
into foods and cause poisoning.
5.4.1. Plastics
Plastics are made from synthetic resins and supplementary materials. Plastics and
synthetic resins are polymerized from small blocks and the higher polymerization degree, the
more stability and the less possibility of block migration into foods. If a polymer is
synthesized from only one block, this polymer is a homopolyer; if two or more blocks are
used, the polymer is a copolymer.
Plastics that are currently allowed for food packaging include polyethylene (PE),
polypropylene, polystyrene, urea formaldehyde, and melamino-formaldehyde. These
materials are potential pollutants for foods. For example, polyvinyl chloride (PVC) is
nontoxic, but the monomer vinyl chloride and its degradation products are toxic. PVC can be
degraded by high temperature and UV light and the decomposition product can cause hepatic
hemangioma. Free formaldehyde may exist in urea formaldehyde and melamino-
formaldehyde plastics in case of incomplete reaction during production. Besides, urea
formaldehyde and melamino-formaldehyde can be degraded by high temperature and acidic
solutions to release formaldehyde and phenols. Formaldehyde is a protoplasmic poison and
can cause focal necrosis of liver cells and lymphocytic infiltration if orally ingested by
animals.
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INDEX
antagonism, 224 base, 31, 55, 72, 151, 209, 220, 225, 227, 272, 300,
antibiotic, 328 321
antibody, 306 beef, 108, 156, 157, 174, 179, 188, 199, 208, 210,
antigen, 306, 310, 311 238, 240, 260, 261, 266, 268, 269
antimony, 194 beer, 5, 92, 158, 162, 249, 250, 266, 295, 296
antioxidant, 61, 66, 67, 71, 126, 128, 131, 185, 189, Beijing, 7, 188, 189, 243
197, 199, 213, 215, 220, 272, 274, 279, 281, 282, beneficial effect, 102
283, 296, 297, 333, 334 benefits, 7, 28, 272, 291
antitumor, 74 benzene, 62, 201, 206, 260, 266, 315, 317, 323, 328,
appetite, 251, 252, 310 333, 339, 340, 341, 347
apples, 71, 264, 307 benzoyl peroxide, 184
aquaculture, 316 beriberi, 192, 202
aqueous solutions, 34, 36, 51, 59, 85, 207, 210, 212, beryllium, 222
213, 236, 279, 315, 316, 326 beta-carotene, 193, 194, 196, 219
aqueous suspension, 84, 280 beverages, 51, 74, 75, 91, 100, 169, 247, 251, 266,
arabinogalactan, 291 276, 277, 279, 292, 293, 294, 296, 348
arginine, 67, 68, 140, 149, 177, 336 bile, 94, 101, 103, 249, 250, 332
aromatic compounds, 254, 256, 257, 258, 264, 265, bile acids, 103
266 bioavailability, 9, 68, 103, 178, 179, 180, 182, 207,
aromatic hydrocarbons, 194, 260, 324, 346 212, 224, 225, 227, 236, 237, 238, 239, 305, 331,
aromatic rings, 184 332, 333, 334
aromatics, 324 biochemical processes, 221
ARS, 135 biochemistry, xi, xii, 2, 3, 324
arsenic, 222, 225, 239 biological activity, 191, 237, 349
ascorbic acid, 38, 61, 62, 63, 70, 211, 213, 219, 281, biological stability, 5
282 biomass, 5, 173
aseptic, 179 biomolecules, 26, 32, 225, 239, 320, 334
Asia, 292, 295 biopolymer, 9
asparagines, 345 biopolymers, 34
asparagus, 74, 218, 257 biosynthesis, 44, 95, 212, 234, 255, 304, 333
Aspartame, 187, 276 biotechnology, xii
aspartate, 147 biotic, 174
aspartic acid, 140, 187, 320, 324, 336 biotin, 209, 210
assessment, 34, 249, 339 birds, 169, 303, 306
asthenia, 339 bladder cancer, 276
astringent, 46, 246, 254 bleaching, 184, 241, 272, 325
atmosphere, 4, 194, 280 bleeding, 298
atmospheric pressure, 71 blindness, 192, 194
atomic emission spectrometry, 349 blood, 40, 55, 94, 100, 101, 102, 149, 150, 192, 196,
atoms, 11, 13, 41, 45, 108, 109, 126, 210, 225, 229, 198, 199, 201, 202, 210, 236, 261, 262, 275, 276,
230, 231, 233, 237, 308, 320, 321, 324 305, 310, 316, 325, 326
ATP, 202, 208, 224, 227, 228, 229, 252, 282 blood plasma, 149
atrophy, 326 blood pressure, 102, 305
autolysis, 185 blood stream, 55, 236
autooxidation, 55 body fluid, 192, 233
awareness, 283, 294 body weight, 310, 326
boils, 341
bonding, 10, 11, 12, 15, 16, 17, 18, 23, 27, 50, 52,
B
76, 79, 87, 91, 92, 101, 116, 145, 146, 153, 154,
bacteria, 24, 74, 93, 94, 102, 173, 181, 185, 189, 156, 160, 165, 166, 168, 172, 248, 249, 288, 334,
200, 206, 209, 210, 212, 230, 231, 278, 279, 280 337, 338
bacterial fermentation, 276 bonds, 10, 11, 13, 14, 15, 40, 42, 43, 46, 58, 76, 77,
barriers, 320 85, 88, 98, 108, 109, 116, 124, 126, 127, 146,
147, 148, 151, 153, 155, 156, 159, 160, 166, 169,
172, 186, 230, 231, 237, 318, 336, 337
Index 355
bone, 150, 170, 221, 223, 224, 233, 240, 305 carboxylic groups, 87, 138, 139
bone growth, 223 carboxymethyl cellulose, 32, 293
bone marrow, 170, 233 carcinogen, 225, 236
bones, 296 carcinogenicity, 326, 341, 347
botanists, 2 cardiovascular disease, 100
bounds, 17 cardiovascular disease XE "cardiovascular disease"
brain, 300 s, 100
brain damage, 300 carob, 96, 293
branching, 77 carotene, 131, 193, 194, 195, 196, 219, 259, 298
breakdown, 58, 86, 124, 166, 184, 300, 313, 321, carotenoids, 191, 192, 194
323, 349 cartilaginous, 261
breast milk, 134, 180 casein, 32, 85, 91, 159, 162, 170, 171, 180, 184, 188,
bromine, 222, 322, 340 292, 332, 349
buns, 173, 296 catalysis, 7, 121, 323
burn, 116, 277 catalyst, 126, 132, 133, 134
by-products, 272 catalytic activity, 94, 126, 133, 152
category a, 112, 150
cation, 12, 87, 90, 164, 251
C
cattle, 242
Ca2+, 14, 39, 41, 81, 87, 90, 92, 98, 102, 164, 167, causal relationship, 276
178, 227, 235, 237, 332, 334 cauterize, 155
cabbage, 10, 200, 215, 218, 240, 304 cell membranes, 318
cacao, 249, 298 cell surface, 74
cadmium, 222, 348 cellulose, 32, 36, 40, 46, 49, 85, 86, 93, 94, 98, 100,
caffeine, 68, 249, 250 101, 102, 268, 280, 289, 291, 292, 293, 295
calcification, 196 central nervous system, 209, 249, 329
calcium, 39, 74, 91, 92, 95, 170, 188, 192, 196, 207, ceramide, 111
221, 222, 278, 279, 288, 291, 292, 294, 296, 297, cereal starches, 76
304, 307, 326, 332 cerebrovascular disease, 6
calculus, 239, 333 chain molecules, 54
calorie, 85, 86, 100, 277, 290 charge density, 154
cancer, 100, 276, 291, 320, 333, 339, 340, 341 cheese, 91, 96, 121, 141, 143, 158, 171, 177, 186,
cane sugar, 24 240, 266, 273, 279, 281, 292, 296, 297
capillary, 51, 168 cheilitis, 205
carbohydrate, xi, 40, 54, 55, 76, 84, 170, 181, 184, chemical industry, 82
207, 225, 226, 289, 310, 312, 333, 341, 345 chemical properties, 2, 9, 39, 158, 320, 324, 325, 341
carbohydrates, vii, xii, 1, 3, 5, 7, 32, 35, 36, 37, 46, chemical reactions, 6, 9, 20, 30, 31, 107, 139, 177,
50, 51, 54, 58, 63, 66, 73, 100, 102, 103, 172, 260
184, 202, 217, 225, 226, 229, 236, 243, 260, 268, chemical structures, 276, 341
342, 345 chemicals, 4, 11, 31, 121, 219, 278, 305, 324, 346
carbon, 28, 36, 37, 46, 49, 62, 63, 90, 92, 94, 102, chicken, 143, 174, 199, 240, 260, 306, 316, 330, 339
108, 109, 110, 111, 115, 116, 121, 122, 130, 131, children, 176, 178, 306, 330
132, 143, 145, 163, 203, 210, 215, 222, 229, 253, China, vii, ix, xi, xii, 1, 7, 9, 35, 107, 128, 137, 167,
261, 298, 315, 323, 328, 333, 340, 347 191, 221, 241, 243, 245, 246, 271, 272, 275, 276,
carbon atoms, 36, 37, 90, 108, 109, 143, 229, 328 277, 279, 280, 282, 283, 286, 287, 288, 289, 295,
carbon dioxide, 28, 36, 102, 163, 261, 323 298, 300, 303, 314, 316, 347
carbon tetrachloride, 92, 347 Chinese restaurant syndrome, 300
carbon-centered radicals, 215 chiral center, 37, 39
carbonyl groups, 49, 72, 181, 345 chitin, 74, 93, 94, 100, 310, 311, 312, 316
carboxyl, 36, 37, 44, 48, 52, 53, 84, 102, 138, 141, chitosan, 74, 93, 94, 95, 100, 101, 104, 295
165, 211, 225, 231, 232, 234, 235, 332 Chitosan, 93, 94, 104, 295
carboxylic acid, 108, 138, 143, 214, 225, 227, 260, chlorine, 222, 340, 347
264, 282 chloroform, 62, 86, 201, 206, 209, 212, 248, 315,
carboxylic acids, 138, 214, 260, 282 317, 328, 333
chlorophyll, 115, 230, 231, 237
356 Index
cholesterol, 74, 94, 100, 101, 105, 107, 174, 239, connective tissue, 150, 170, 293
291, 316, 330 constant rate, 161
cholic acid, 250, 251 constituents, vii, 17, 18, 19, 28, 32, 171, 172, 221,
choline, 111 224, 236, 259, 261, 268, 282, 287, 317
cholinesterase, 324 consumer choice, 283, 284
cholinesterase inhibitors, 324 consumers, 1, 3, 4, 5, 37, 55, 73, 130, 174, 176, 186,
chromatography, 245 202, 245, 246, 248, 252, 272, 278, 298, 306, 319,
chromium, 132, 222, 236 335
chromosome, 149 consumption, 55, 60, 173, 174, 192, 245, 276, 278,
chymotrypsin, 177, 183, 184, 305 313, 330
ciguatera, 317 containers, 29, 347, 348
civilization, 6 contaminant, 233
classes, 10, 13, 89, 90, 91, 221, 285, 321 contamination, 222, 348
classification, 35, 107, 191, 221, 246, 271, 285, 318 conversion rate, 174
cleaning, 1, 289 COOH, 138, 143, 187, 249
cleavage, 318 cooking, 83, 101, 130, 152, 173, 178, 183, 202, 211,
climate, 173, 241 220, 260, 289, 308, 341
clusters, 170 cooling, 29, 30, 45, 82, 91, 132, 169, 275, 292, 293,
CMC, 49, 85, 86 294
CO2, 66, 86, 93, 166, 210 coordination, 12, 224, 225, 226, 227, 229, 230, 231,
coatings, 86, 95, 298, 347 235, 237, 238
cobalamin, 231, 305 copolymer, 292, 348
cobalt, 212, 222, 231 copolymers, 58, 92
cocoa, 91, 112, 117, 118, 134, 289, 342 copper, 132, 150, 231, 233, 281, 298
cocoa butter, 112, 117, 118, 134, 289 cornea, 194
coconut oil, 117 corpus luteum, 329
coenzyme, 207, 208, 209, 212, 213 correlation, 33, 164, 276, 310
coffee, 21, 22, 54, 68, 104, 249, 286, 287, 288, 298, corrosion, 325
305, 342 cortex, 201, 207, 326
coherence, 159 cost, 48, 53, 272, 273, 346
collagen, 32, 150, 156, 170, 183, 309 covalent bond, 14, 17, 52, 146, 153, 183, 187
collisions, 31 covalent bonding, 52
colon, 73, 74, 101, 102, 108 covering, xi
color, 1, 2, 4, 5, 6, 7, 36, 37, 46, 55, 58, 59, 60, 63, crop, 173
69, 71, 94, 95, 115, 130, 156, 158, 161, 170, 184, crops, 76, 176, 234, 310, 311
191, 205, 219, 233, 271, 272, 273, 281, 298, 315, crude oil, 283
338, 339, 346 crust, 223
coma, 305 crystal growth, 46, 83, 96
combustion, 325 crystal structure, 85, 286, 287, 288
commercial, 33, 34, 74, 75, 86, 90, 95, 98, 134, 143, crystalline, 16, 22, 76, 77, 78, 117, 207, 275, 276,
172, 189, 219, 277, 282, 294, 321, 346 292, 296
complement, 94, 295 crystallization, 29, 30, 73, 79, 83, 97, 100, 117, 273,
complexity, 68, 103 275, 287, 289
compliance, 319 crystals, 13, 18, 28, 38, 46, 117, 118, 134, 207, 208,
composition, 2, 4, 5, 6, 18, 20, 22, 29, 30, 36, 55, 58, 212, 290, 315, 316, 325, 329
63, 65, 96, 101, 102, 104, 109, 111, 113, 114, cultivation, 241, 307, 308
115, 117, 124, 129, 133, 148, 156, 159, 164, 166, culture, 246
173, 174, 260, 293, 314, 316, 321, 331, 336 curcumin, 298
compression, 130 cuticle, 316
condensation, 39, 55, 58, 59, 62, 63, 65, 72, 124, cyanide, 47, 231, 317
129, 139, 180, 181, 182, 204 cyanide poisoning, 47
conduction, 324 cyanocobalamin, 212, 231
configuration, 10, 11, 37, 109, 110, 116, 124, 127, cyclodextrins, 39
143, 225, 333 cyclopentadiene, 321
conjugation, 116
Index 357
cysteine, 71, 140, 144, 166, 179, 184, 232, 256, 257, diabetes, 6, 100, 275
266, 267, 310, 320, 328 dialysis, 68, 151
cystine, 165, 166, 179, 182, 184, 233, 320, 336 diarrhea, 73, 196, 208, 275, 314, 317, 318
cytochrome, 223, 230, 324 dielectric constant, 156
cytoplasm, 316 diet, 6, 35, 107, 181, 183, 192, 194, 225, 238, 274,
275, 295, 296, 303, 306, 339, 341
dietary fiber, 37, 85, 86, 90, 100, 103, 105, 177, 291,
D
294
damages, 348 dietary habits, 1, 246, 247
D-amino acids, 248 dietary intake, 103
danger, 278, 282 diffraction, 78
DDT, 321 diffusion, 29, 30, 31, 33, 79, 81, 93, 125, 152, 153,
deacetylation, 93, 295 169, 185, 186
decay, 93, 274, 275 digestibility, 68, 157, 174, 176, 177, 178, 179, 184,
decomposition, 5, 6, 102, 116, 124, 125, 194, 203, 295, 332, 349
205, 207, 254, 259, 260, 261, 262, 268, 272, 281, digestion, 100, 102, 177, 180, 183, 189, 250, 295,
348 304, 334, 335
defecation, 101 digestive enzymes, 103, 182, 306, 334
defects, 13 dihydroxyphenylalanine, 177, 309
deficiency, 173, 191, 192, 194, 196, 197, 198, 201, dilation, 119
202, 205, 208, 209, 210, 212, 213, 214, 222, 224, dimethylsulfoxide, 317
238, 273, 319, 320 dioxin, 324, 325, 326, 349
deformation, 29, 51, 118, 165, 284 dioxin-like PCBs, 325
degradation, 5, 6, 56, 57, 65, 66, 68, 71, 129, 181, dipeptides, 140
182, 184, 194, 195, 196, 199, 202, 203, 204, 205, dipole moment of, 11
207, 208, 209, 210, 212, 214, 216, 219, 252, 262, discomfort, 102
266, 268, 269, 284, 320, 323, 324, 325, 326, 342, diseases, 6, 100, 185, 191, 210, 321, 339
344, 348 dislocation, 13
degradation rate, 203 disorder, 202, 208, 305, 306, 310
degumming, 131 dispersion, 17, 85, 154, 158, 169, 289, 292, 298
dehydration, 9, 21, 22, 36, 58, 59, 60, 61, 66, 86, dissociation, 11, 71, 87, 95, 138, 169, 209
143, 168, 179, 199, 241, 242, 253, 296 dissolved oxygen, 61
denaturation, 5, 6, 7, 137, 148, 151, 152, 153, 154, distillation, 7, 131, 288
156, 157, 159, 167, 168, 169, 172, 178, 180, 183, distribution, 15, 40, 44, 96, 107, 110, 112, 113, 114,
184, 187, 338 115, 117, 124, 133, 134, 135, 146, 159, 161, 174,
dendrites, 13 176, 221, 223, 289, 307, 310, 311, 325, 330
dental caries, 73 dizziness, 300, 304, 305
Department of Agriculture, 243 DNA, 95, 239, 320, 346
dephosphorylation, 217 docosahexaenoic acid, 262
depolarization, 324 donors, 11, 110, 128, 281
depression, 34, 83 dosage, 133, 326, 341
derivatives, 36, 37, 49, 76, 82, 86, 107, 110, 111, double bonds, 58, 108, 109, 111, 116, 121, 122, 124,
120, 138, 187, 197, 200, 208, 211, 220, 225, 226, 126, 127, 131, 132, 253
229, 243, 249, 269, 293, 299, 317, 322, 328, 333 double helix, 44, 45, 77
dermatitis, 205, 208, 210 dough, 86, 91, 96, 165, 166, 167, 171, 172, 185, 284,
desorption, 22, 23, 29 287, 288, 289, 296
destruction, 68, 151, 152, 183, 194, 205, 212, 215, drainage, 164
216 dressings, 83, 85, 86, 96, 97, 279, 290, 293, 294
detectable, 152 drinking water, 94, 224
detection, xii, 104 drugs, 305, 318, 326, 330, 331
detergents, 285 dry matter, 27
detoxification, 71, 213, 220 drying, 2, 21, 29, 33, 83, 169, 179, 184, 186, 196,
developing countries, vii 349
deviation, 113 DSC, 30, 156
dyes, 298
358 Index
dynamic mechanical analysis, 30 221, 232, 239, 256, 258, 259, 262, 264, 275, 305,
dyspepsia, 202 307, 313, 320, 327, 333, 336, 337, 338, 339, 346
dyspnea, 214, 305 EPA, 5, 109, 112
epidemiological investigations, 341
epidermis, 316
E
epinephrine, 107
edema, 202, 339 epithelial cells, 194, 304
egg, 24, 41, 44, 45, 72, 87, 108, 152, 156, 158, 159, equilibrium, 19, 29, 30, 138, 168, 262, 296
164, 178, 183, 196, 206, 212, 235, 261, 289, 306 equipment, 3, 162, 241
elastin, 32, 150, 170, 309 essential fatty acids, 107
electrolyte, 305 ester, 49, 52, 54, 90, 111, 120, 139, 140, 150, 187,
electrolyte imbalance, 305 194, 256, 264, 287, 288, 292, 322, 323, 333
electron, 11, 79, 128, 179, 233, 281, 324, 333 ester bonds, 150
electron pairs, 11 ethanol, 59, 62, 64, 91, 92, 93, 100, 142, 149, 165,
electrons, 11, 12, 225 171, 172, 194, 207, 209, 212, 213, 255, 266, 283,
electrophoresis, 138 288, 292, 293, 315, 317, 328, 333, 341, 347
elongation, 166, 324, 333 ethers, 49, 254, 260, 266, 324, 326, 329
elucidation, 269 ethyl acetate, 62, 255, 259, 266, 283, 315, 328
emergency, 3, 100 ethylene, 93, 281, 283
emission, 205 eukaryotic cell, 222
emulsifying agents, 82 evacuation, 101
emulsions, 91, 98, 119, 120, 125, 154, 158, 159, 160, evaporation, 183
162, 169, 288, 289, 291, 293 evidence, 16, 276, 277
enamel, 347 evolution, 271, 310
enantiomers, 37, 265 EXAFS, 226
encapsulation, 73, 289 excretion, 95
endocrine, 325 experimental design, 6
endosperm, 95, 171, 293 exploitation, 4
endothermic, 156 exposure, 17, 118, 121, 126, 153, 183, 194, 213, 234,
energy, 11, 12, 18, 31, 35, 37, 73, 86, 102, 107, 119, 279, 306, 323
120, 126, 128, 134, 153, 159, 162, 163, 170, 202, extraction, 7, 88, 101, 130, 168, 169, 172, 293
275, 276, 323 extracts, 289, 292, 298, 300, 318
energy consumption, 134 extrusion, 7, 83, 172
energy input, 159, 162, 163 exudate, 96, 98, 291
energy supply, 276
engineering, xii, 1, 4 F
enlargement, 304, 326
entanglement network, 32 families, 310, 311, 312
entropy, 188 fast food, 349
environment, 1, 16, 17, 102, 138, 146, 168, 216, 223, fat, 3, 5, 86, 91, 94, 100, 103, 107, 108, 111, 112,
241, 295, 304, 305, 319, 321, 323, 324, 325, 326 113, 114, 118, 119, 131, 133, 134, 156, 158, 159,
environmental conditions, 159, 168, 183 161, 172, 191, 192, 193, 194, 196, 197, 199, 239,
environmental effects, 32 240, 250, 260, 261, 282, 283, 284, 288, 289, 290,
environmental factors, 245, 306 292, 293, 295, 298, 317, 326
environmental stress, 151 fat soluble, 191, 194, 196, 197, 317
environmental stresses, 151 fatty acids, xii, 16, 78, 83, 94, 102, 107, 108, 109,
environments, 50, 212 110, 111, 112, 113, 114, 115, 116, 117, 120, 121,
enzyme, 4, 5, 7, 31, 44, 46, 47, 71, 128, 151, 152, 122, 124, 126, 127, 129, 130, 131, 132, 133, 134,
163, 177, 180, 185, 223, 224, 272, 274, 304, 320, 182, 256, 259, 260, 261, 262, 285, 287, 288, 306
323, 331, 335, 336, 349 FDA, 100, 103, 187
enzyme inhibitors, 128, 177, 335, 336, 349 feed additives, 331
enzymes, 4, 28, 47, 48, 55, 68, 72, 77, 82, 85, 87, 88, fermentation, 5, 90, 100, 165, 173, 184, 185, 189,
90, 120, 146, 150, 152, 153, 157, 165, 170, 176, 254, 258, 259, 266, 267, 274, 277, 289, 294, 295,
185, 191, 196, 205, 207, 208, 212, 214, 216, 217, 334, 349
Index 359
ferritin, 237 formula, 19, 37, 40, 41, 59, 75, 93, 141, 234, 314,
fertility, 346 316, 317, 340
fever, 306 free energy, 119, 120, 141, 159, 284
fiber, 35, 91, 100, 150, 170, 173, 291 free radicals, 26, 103, 121, 126, 128, 130, 182, 199,
fibers, 40, 100 205, 233, 281, 334
films, 159, 163, 164, 165, 188 free rotation, 42
filtration, 4, 117, 131 free volume, 31, 32
fish, 24, 68, 92, 108, 148, 157, 169, 173, 174, 177, freezing, 2, 6, 13, 20, 28, 34, 45, 83, 84, 117, 240,
178, 179, 180, 184, 185, 196, 204, 208, 212, 233, 308
234, 238, 261, 262, 269, 279, 283, 296, 297, 298, freshwater, 261, 316
300, 303, 316 friction, 152, 169
fish oil, 196, 262 fructose, 4, 36, 47, 48, 49, 50, 55, 57, 59, 60, 74, 75,
fission, 58 82, 181, 225, 248, 274, 275, 276, 345
fixation, 210 fruits, 4, 7, 18, 21, 24, 36, 55, 74, 87, 93, 95, 108,
flame, 179 195, 213, 219, 237, 245, 249, 254, 255, 263, 264,
flatulence, 73, 172 265, 273, 275, 279, 280, 290, 297, 304, 305
flavonoids, 45, 46, 283, 333, 334 functional food, 73, 86, 94, 294, 296
flavour, 54, 103, 187, 293, 299, 300 fungi, 74, 193, 233, 278
flaws, 58 furan, 124, 203, 214, 258, 259, 260, 261, 266, 268,
flexibility, 42, 52, 159, 160 324
flocculation, 120, 164
flora, 37, 75
G
flour, 10, 24, 86, 96, 165, 166, 167, 171, 172, 173,
177, 180, 184, 202, 216, 218, 219, 272, 288, 295, gallbladder, 251
296, 297, 300 gastroenteritis, 305
fluid, 51, 85, 113, 157, 164, 169, 250, 291, 294, 348 gastrointestinal tract, 194, 341
fluorescence, 67, 104, 202, 205, 340 gel, 44, 51, 52, 53, 81, 82, 83, 84, 86, 87, 90, 91, 92,
fluorine, 222 98, 100, 167, 168, 171, 291, 292, 294, 295, 296
foals, 105 gel formation, 296
foams, 154, 158, 159, 162, 163, 164, 188, 289, 293 gelatinization temperature, 76, 80, 81, 82, 83, 84
folate, 210 gelation, 81, 87, 88, 98, 151, 158, 159, 160, 167,
folic acid, 210, 211, 212, 215, 219 168, 293, 297
follicle, 329 genes, 145
food additive, vii, 5, 91, 241, 271, 272, 273, 284, genetic code, 145
300, 346 genetic information, 320
food additives, vii, 5, 91, 241, 271, 272, 273, 284, genetics, 306
300, 346 genitals, 198
Food and Drug Administration, 73 genomics, 7
food chain, 319, 325 genus, 96, 98, 275, 318
food industry, 1, 3, 4, 5, 6, 7, 39, 46, 48, 49, 73, 82, geometry, 40, 41, 42, 43, 44
85, 86, 87, 90, 91, 92, 93, 94, 97, 120, 132, 137, germination, 273
168, 171, 178, 180, 184, 187, 213, 251, 271, 278, gill, 316
280, 289, 291, 295, 300, 303, 347 ginger, 253
food poisoning, 314 gland, 233
food production, 287, 289 glass transition, 23, 30, 32
food products, 297, 300 glossitis, 210
food safety, xi, xii, 2, 46, 271, 272, 296, 303, 319, glucoamylase, 48, 82
340, 347 glucose, 36, 39, 40, 47, 48, 49, 50, 55, 59, 65, 66, 67,
food security, 3 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 82, 84, 86,
food spoilage, 272 97, 98, 100, 101, 181, 224, 225, 239, 248, 249,
food web, 324 266, 267, 274, 275, 276, 281, 282, 294, 295, 307,
foodborne illness, 317 328, 333, 345
force, 17, 95, 101, 146, 147, 163, 168, 169 glucose oxidase, 48, 72, 281, 282
formaldehyde, 182, 210, 261, 262, 348 glucoside, 45, 342
360 Index
hydroxyl, 36, 37, 39, 45, 46, 48, 49, 61, 62, 63, 67, inhibition, 5, 67, 68, 91, 93, 304, 305, 319, 322, 347,
79, 83, 88, 90, 95, 102, 110, 111, 115, 116, 129, 349
139, 165, 225, 231, 248, 253, 260, 264, 275, 320, inhibitor, 67, 177, 183, 331, 335, 336, 337, 338, 349
333, 334, 347 initiation, 46, 116, 121, 124, 126
hydroxyl groups, 36, 39, 45, 46, 49, 62, 63, 79, 83, injury, 304, 308, 316
88, 95, 102, 225, 333, 347 inositol, 38, 39, 111, 283, 328, 331
hygiene, 220, 272 insecticide, 241
hyperemia, 194, 313 insects, 73, 174, 303, 321, 323
hypersensitivity, 210 insertion, 44
hypertension, 100, 101, 277 insomnia, 305
hypothesis, 58 instant noodles, 173
hysteresis, 23 insulin, 147, 224
hysteresis loop, 23 integrity, 194, 221
intercellular adhesion molecule, 213
interface, 119, 120, 125, 153, 154, 159, 160, 162,
I
163, 164, 169, 185, 284
Iceland, 341 interference, 44, 304
ID, 268 international law, 272
ideal, 19, 94, 159, 176 interphase, 160
identification, 5, 6, 115, 139, 318 intervention, 58
illumination, 216 intestinal tract, 192
images, 3 intestine, 37, 55, 94, 102, 103, 185, 313
immune reaction, 306 invasions, 331
immune response, 306 inversion, 161
immunity, 181 investment, 173
immunogenicity, 306 iodine, 5, 129, 194, 222, 304
immunoglobulin, 180 ion channels, 318
immunoglobulins, 149 ionization, 153, 154, 168
immunomodulatory, 185 ionizing radiation, 153
immunoreactivity, 306 ions, 11, 14, 26, 70, 81, 87, 88, 91, 94, 98, 99, 102,
immunostimulatory, 74 138, 158, 164, 178, 188, 216, 225, 230, 233, 234,
impurities, 115, 116, 130, 131, 132, 133 237, 281, 291, 308, 326
in vitro, 349 Iran, 96
in vivo, 72, 113, 148, 208, 240, 326 iron, 60, 93, 150, 180, 212, 224, 230, 233, 237, 238,
incidence, 73, 102, 210, 276, 306, 330, 341 281, 282, 298, 304
incubation period, 341 irradiation, 184
India, ix, 107, 246 irreversible aggregation, 155
individual differences, 103 irritability, 178, 254
individuals, 102, 245, 246, 284, 304, 330 isoflavone, 333
induction, 67, 121 isoleucine, 140
induction period, 67, 121 isomerization, 7, 48, 58, 66, 75, 122, 194, 250, 253,
industrial processing, 179 323
industries, 74, 87, 95, 133, 325 isomers, 37, 39, 49, 113, 122, 124, 133, 135, 141,
industry, 4, 5, 7, 90, 173, 179, 188, 251, 271, 294, 195, 219, 248, 253, 287, 324, 328
295, 297, 316, 347 isoprene, 265
infants, 155, 178, 180, 298, 300, 306 isotherms, 22
infertility, 198 isotope, 13
inflammation, 192, 194, 208, 214, 314, 318
infrared spectroscopy, 225 K
ingestion, 75, 101, 102, 186, 247, 304, 305, 314,
316, 320, 326 K+, 14, 81, 90, 91, 98, 102
ingredients, 5, 7, 37, 53, 73, 82, 94, 158, 265, 283, kaempferol, 333
288, 289, 290, 294, 296, 300 keratin, 32
362 Index
ketones, 37, 58, 60, 66, 69, 124, 129, 181, 184, 187, liquid chromatography, 135, 219, 220
214, 256, 258, 259, 260, 261, 263, 264, 266, 280, liquid phase, 29, 117, 118, 119
308 liquids, 53, 119, 179, 284, 325
kidney, 177, 196, 206, 210, 218, 233, 236, 304, 307, lithium, 93, 222
312, 314, 330, 346, 347 liver, 36, 39, 40, 84, 94, 101, 170, 174, 196, 201,
kidney failure, 196 203, 206, 207, 208, 209, 210, 212, 223, 233, 236,
kinetic model, 104 250, 262, 304, 318, 326, 330, 346, 348
kinetics, 34 liver cancer, 326
liver cells, 348
liver damage, 318
L
livestock, 251, 252, 260, 261
labeling, 139, 300 loss of appetite, 196, 202, 214
lactase, 73 low temperatures, 18, 45, 72, 118, 129, 153, 157,
lactase deficiency, 73 286
lactic acid, 3, 66, 143, 173, 181, 185, 189, 202, 251, lung cancer, 341
280, 287, 288, 342 Luo, 300
lactobacillus, 74, 295 lutein, 131, 174, 194
Lactobacillus, 24, 74, 104 lymphatic system, 170, 306
lactoferrin, 180 lymphocytes, 326
lactose, 50, 66, 67, 70, 73, 75, 304, 345 lysine, 55, 66, 67, 68, 70, 71, 72, 140, 171, 179, 180,
lactose intolerance, 73 181, 182, 320, 336
lakes, 299 lysosome, 159
lamella, 164 lysozyme, 158, 161, 181
lanthanum, 225
large intestine, 100, 102 M
lead, 70, 121, 129, 164, 167, 168, 177, 178, 179,
183, 217, 218, 236, 275, 305, 307, 310, 313, 316, macromolecules, 9, 28, 37, 44, 52, 53, 68, 238, 289
319, 321, 324, 345, 348 magnesium, 39, 74, 150, 188, 222, 292, 326
leakage, 93, 316 magnitude, 23, 93, 225
leaks, 251 Maillard reaction, 27, 29, 39, 46, 55, 56, 57, 58, 61,
lecithin, 110, 111, 283, 286, 289 64, 65, 66, 67, 68, 71, 72, 104, 181, 182, 184,
legs, 317 214, 225, 260, 266, 267, 276, 342, 345, 349
legume, 76, 309, 310, 312, 336 majority, 3, 36, 46, 58, 107, 199, 222, 295, 318
lesions, 212 malaise, 307
leucine, 67, 68, 140, 255, 264 malt extract, 250
Lewis acids, 225 maltose, 36, 39, 50, 73, 275
ligand, 39, 46, 225, 237, 314, 320 mammal, 234
light, 63, 88, 91, 92, 94, 121, 126, 141, 161, 192, mammals, 107, 111, 169, 233, 303, 345
193, 194, 196, 197, 205, 206, 207, 209, 210, 211, management, 216, 241
253, 261, 279, 323, 329 manganese, 222
light scattering, 161 manipulation, 349
lignin, 85, 100, 269 mannitol, 45, 50, 275
linear molecules, 53, 338 manufacturing, 187, 272, 273
linear polymers, 166 marine fish, 185, 261, 262
linoleic acid, 67, 108, 109, 110, 111, 112, 113, 114, masking, 277
124, 126, 127, 133, 258, 259, 263, 264 mass, 21, 78, 161, 169, 245, 275, 285
lipases, 121 mass spectrometry, 245
lipid metabolism, 192 material surface, 180
lipid oxidation, 6, 26, 67, 103, 115, 121, 126, 128, materials, vii, 1, 3, 4, 5, 6, 21, 29, 32, 37, 65, 74, 76,
131, 184, 186, 199, 217, 260, 268, 273, 282, 339, 126, 131, 153, 158, 163, 165, 173, 174, 180, 182,
345 207, 216, 243, 254, 278, 289, 290, 299, 303, 305,
lipid peroxidation, 320 306, 344, 347, 348
lipoid, 182 matrix, 29, 53, 54, 61, 169, 170, 172
lipoproteins, 17, 150 matter, 16, 177, 298
Index 363
native starches, 76
O
natural compound, 187
natural food, 73 obesity, 101, 274, 277
natural polymers, 156 octane, 325
natural resources, 274 OH, 11, 13, 14, 17, 31, 46, 63, 67, 152, 212, 226,
nausea, 73, 177, 196, 314, 317, 318, 335 230, 248, 249, 321, 329, 333, 335
NCS, 254 oil, 4, 5, 10, 67, 86, 100, 112, 117, 118, 119, 120,
necrosis, 326, 348 125, 128, 131, 132, 159, 161, 162, 169, 172, 173,
negative consequences, 68 176, 177, 182, 184, 185, 198, 258, 262, 265, 278,
negative effects, 283 282, 284, 286, 287, 288, 290, 291, 298
nerve, 202, 246, 247, 248, 304, 305, 317, 324, 341 oilseed, 180
nervous system, 60, 202, 212 olefins, 308
Netherlands, 269 oleic acid, 108, 110, 111, 112, 113, 115, 124, 127
neurotransmitters, 324 oligomers, 74, 186
neutral, 46, 69, 90, 95, 98, 138, 150, 172, 186, 187, oligosaccharide, 4, 6, 36, 73, 74, 88
205, 206, 207, 211, 251, 260, 280, 294, 295, 298, olive oil, 112, 117
316, 321, 322 optical activity, 152
New Zealand, 277 oral cavity, 186, 246
NH2, 72, 138, 144, 187, 226, 248, 320 organ, 209
nickel, 132, 222 organelle, 320
nicotinamide, 206, 207, 208 organic compounds, 36, 192, 325
nicotinic acid, 206, 207, 208 organic food, 296
niobium, 222 organic solvents, 92, 107, 156, 317, 328, 332, 333,
nitrates, 345, 346 340, 346
nitrides, 257 organism, xii, 191, 223, 233, 234, 243
nitrite, 278, 341, 345, 346 organs, 170, 330, 332, 339
nitrogen, 3, 17, 58, 138, 139, 168, 172, 176, 222, ornithine, 140, 309
225, 231, 233, 320 oscillation, 180
nitrogen fixation, 233 osmotic pressure, 102, 221
nitrogen gas, 139 osteomalacia, 196
nitrosamines, 345, 346 osteoporosis, 296
nitroso compounds, 345, 346 ovum, 329
NMR, 64, 227, 233, 234 oxalate, 251, 332
non-diffusion-limited properties, 33 oxidation products, 61, 84, 103, 131, 211, 261, 262,
nonequilibrium, 29 263, 339
non-polar, 165 oxidation rate, 26, 124, 125
NPR, 346 oxidative reaction, 130
nuclear magnetic resonance, 119 oxidizability, 205
nucleic acid, 17, 150, 174, 210, 223, 225, 236, 239, oxygen, 6, 10, 11, 13, 26, 28, 31, 40, 41, 43, 45, 46,
320 61, 67, 93, 121, 122, 124, 125, 126, 127, 128,
nucleophiles, 71, 203 129, 152, 182, 184, 194, 196, 197, 199, 200, 205,
nucleoprotein, 150 209, 214, 215, 220, 222, 225, 236, 237, 268, 281,
nucleotides, 227, 236, 260 282, 316, 320, 324, 334
nucleus, 46 oysters, 317, 318
nuisance, 163
nutraceutical, 290, 291, 295
nutrient, 75, 100, 179, 216, 304, 313, 332 P
nutrients, vii, 1, 5, 6, 9, 37, 177, 179, 189, 191, 219,
243, 245, 271, 303, 331, 333, 335 pain, 73, 210, 246, 275, 300, 314, 317, 318
nutrition, vii, xi, xii, 1, 2, 3, 4, 5, 6, 7, 37, 63, 73, 75, palm oil, 112, 117
76, 100, 102, 130, 137, 149, 167, 176, 180, 237, palpitations, 300
239, 240, 245, 272, 319 pancreas, 22
nutritional status, 319 pantothenic acid, 206, 207, 217
parallel, 46, 77, 78, 146
paralysis, 202, 304, 318
Index 365
pasta, 30, 220, 286 physical properties, 39, 101, 172, 278, 290, 339
pasteurization, 178, 179, 209 physical structure, 22
patents, xii physicochemical properties, vii, 6, 53, 54, 76, 145
pathogens, 153 Physiological, 192, 194, 196, 197, 198, 201, 202,
pathways, 56, 107 205, 207, 208, 209, 210, 212, 213
PCBs, 325, 339, 340 physiological factors, 238
PCDD/Fs, 325, 326 physiology, 5
pellagra, 192, 207, 208 pigmentation, 326, 339
penetrability, 45 pitch, 40, 42
penicillin, 326, 327 plant growth, 223, 321
pepsin, 150, 180, 184, 185, 316 plants, 3, 35, 36, 37, 39, 87, 96, 100, 101, 108, 111,
peptide, 15, 137, 141, 145, 146, 148, 159, 168, 182, 112, 127, 130, 174, 176, 177, 196, 206, 208, 212,
184, 185, 186, 189, 225, 231, 327 230, 233, 234, 249, 255, 263, 275, 289, 290, 294,
peptide chain, 146, 148, 160, 168 303, 305, 306, 307, 308, 309, 310, 312, 314, 318,
peptides, 4, 36, 69, 141, 142, 177, 181, 182, 185, 319, 321, 331, 335, 336, 349
186, 229, 234, 236, 260, 276, 282, 306, 318, 319 plasticity, 107, 118, 119
perchlorate, 239 plasticizer, 9, 31, 275
peristalsis, 201 plastics, 347, 348
permeability, 316, 320, 324 platelets, 198
permit, 282 platinum, 132
permittivity, 14 poison, 348
pernicious anemia, 192, 210, 212 polar, 12, 16, 17, 23, 26, 31, 54, 80, 93, 141, 156,
peroxidation, 320 165, 168, 186, 313, 315, 317, 321
peroxide, 124, 128, 184, 199, 217, 286, 336, 339 polar groups, 12, 16, 17, 31, 80, 141
pesticide, 241, 303, 323 polarity, 120, 282, 317
petroleum, 328, 329 polarizability, 102
PGE, 285 polarization, 11
pH, 28, 31, 39, 49, 52, 53, 61, 66, 70, 71, 72, 81, 82, pollutants, 6, 324, 325, 348
84, 85, 87, 88, 92, 95, 99, 102, 104, 138, 143, pollution, 233, 316, 319, 347, 348
146, 153, 154, 159, 162, 163, 168, 171, 172, 178, polyacrylamide, 344
188, 202, 203, 204, 207, 211, 212, 214, 215, 236, polybrominated biphenyls, 324
251, 273, 276, 277, 278, 279, 280, 294, 323, 332, polychlorinated biphenyl, 324
334 polychlorinated biphenyls (PCBs), 324
pharmaceutical, 74, 293, 294 polycyclic aromatic hydrocarbon, 339, 348
pharmaceuticals, 82, 87, 295 polyether, 317, 318
phase diagram, 29 polymer, 2, 29, 30, 31, 34, 53, 63, 76, 77, 91, 93, 98,
phase inversion, 161 166, 291, 348
phase transformation, 119 polymer chain, 31
phenolic compounds, 61, 63, 281 polymer matrix, 31
phenylalanine, 140, 153, 187, 265 polymer systems, 30
phosphate, 39, 49, 52, 84, 144, 170, 192, 203, 208, polymeric materials, 21
209, 227, 228, 239, 292, 293, 295, 296, 297, 321, polymerization, 5, 6, 36, 40, 51, 58, 59, 62, 76, 82,
322, 331, 332 85, 87, 92, 123, 124, 129, 130, 153, 165, 166,
phosphates, 38, 83, 84, 92, 236, 238, 296, 321, 322 182, 287, 323, 333, 338, 339, 341, 348
phosphatidylcholine, 111 polymers, 23, 30, 31, 52, 58, 74, 82, 87, 141, 147,
phosphoinositides, 39 166, 181, 289
phospholipids, 74, 107, 110, 111, 120, 128, 130, 131, polymorphism, 107, 117
150, 167, 289, 320 polynucleotides, 320
phosphorous, 93 polypeptide, 145, 146, 148, 154, 159, 160, 280, 293,
phosphorus, 49, 77, 81, 83, 196, 221, 222, 228, 296 309
phosphorylation, 208, 322 polypeptides, 145, 166
photochemical degradation, 205, 220 polyphenols, xii, 61, 224, 238, 254, 282, 283, 333,
photosynthesis, 36, 233, 237 334
physical chemistry, 2 polyphosphates, 296, 297
physical interaction, 9, 17 polypropylene, 348
366 Index
polysaccharide, 5, 6, 36, 40, 41, 43, 44, 45, 50, 51, prothrombin, 128, 201
52, 53, 54, 55, 86, 87, 88, 91, 93, 97, 100, 103, protons, 332
183, 292, 293, 294, 295 pruritus, 306
polysaccharide chains, 53 pulp, 279, 291, 294
polysaccharides, 4, 9, 17, 31, 35, 36, 37, 40, 45, 46, pure water, 13, 14, 15, 18, 19, 92, 305
47, 49, 51, 52, 53, 73, 95, 96, 97, 99, 100, 167, purification, 168, 169
177, 183, 235, 268, 289, 291, 292, 295, 334 purity, 50, 82, 153, 288, 289
Polysaccharides, 36, 40, 42, 45, 48, 50, 51, 53, 97, PVC, 348
235 pyridoxine, 208, 209
polystyrene, 348 pyrimidine, 201, 227, 320
polyunsaturated fat, 115, 127, 262, 263, 320 pyrophosphate, 90, 202
polyunsaturated fatty acids, 115, 127, 262, 263, 320
polyuria, 196
Q
polyvinyl chloride, 348
ponds, 316 quality control, xii, 347
POPs, 324 quantification, 139
population, 173, 174 quantum yields, 121
porosity, 184 quercetin, 333
porphyrins, 229, 282 quinone, 199, 215
positive correlation, 166 quinones, 334
potassium, 91, 202, 222, 276, 279, 292, 294, 296,
297, 317, 326
potato, 27, 28, 76, 77, 78, 79, 80, 81, 83, 163, 195, R
204, 206, 218, 219, 240, 242, 258, 268, 304, 305,
307, 313, 339, 341, 342, 345 race, 110
poultry, 108, 251, 252, 260, 298 radiation, 126, 153, 194, 211
precipitation, 85, 138, 291, 334 Radiation, 153
precocious puberty, 330 radical formation, 153
predators, 303, 319, 331, 335 radical reactions, 121
predicate, 21, 28 radicals, 26, 67, 121, 182, 281, 334, 344
preparation, 5, 48, 54, 85, 101, 172, 251, 272, 297, radius, 14
304, 322, 325, 331 Raman spectroscopy, 227
preservation, vii, xi, 4, 5, 28, 272, 281, 325 rancid, 121, 346
preservative, 93, 219, 272, 274, 278, 300 rape, 178
prevention, 5, 83, 91, 121, 128, 291, 321, 325, 333 rape seed, 178
principles, 272 rare earth elements, 222
probability, 160 raw materials, 216
probiotic, 73, 349 RE, 269
probiotics, 94 reactant, 9, 26
professionals, 1 reactants, 26, 27, 31, 345
progesterone, 329 reaction center, 337
programming, 80 reaction mechanism, 58, 68
proliferation, 24, 73, 74, 94 reaction medium, 9
proline, 68, 139, 140, 149, 170 reaction rate, 25, 26, 28, 48, 179, 345
propagation, 102, 121, 174, 319, 331 reaction temperature, 69, 134
propylene, 254, 288, 295, 298 reaction time, 69, 181, 217
prostaglandins, 198 reactions, 2, 4, 5, 6, 7, 9, 20, 23, 26, 27, 31, 39, 46,
protease inhibitors, 178, 336, 337 55, 58, 59, 60, 61, 63, 65, 66, 68, 69, 70, 71, 107,
protection, 4, 5, 139, 150, 283, 331 121, 124, 127, 128, 129, 130, 133, 138, 165, 166,
protein components, 158, 171, 186 177, 181, 182, 184, 208, 209, 210, 212, 213, 217,
protein constituent, 172, 232, 233 219, 233, 236, 239, 245, 259, 281, 306, 320, 322,
protein folding, 17, 31 347
protein structure, 182 reactive oxygen, 71
protein synthesis, 139, 149, 223, 309, 319 reactivity, 13, 16, 69, 167, 236
proteolytic enzyme, 185 reagents, 139, 152, 283, 321, 322
Index 367
receptor sites, 11
S
receptors, 53, 140, 141, 186, 246, 247, 248, 249, 318
recognition, 337, 338 saccharin, 247, 248, 274, 276, 277
recombination, 31, 260 safety, vii, xii, 2, 4, 5, 6, 19, 34, 35, 63, 68, 85, 107,
recommendations, 173, 174 124, 130, 143, 224, 225, 275, 276, 277, 285, 339,
recovery, 247 345, 348
recrystallization, 29, 81 salinity, 316
red blood cells, 177, 310, 316 salmon, 240
red wine, 254 Salmonella, 24
reducing sugars, 55, 60, 69, 73, 177, 181, 260, 342 salt concentration, 149, 170, 294
refractive index, 115, 132, 339 salts, 9, 12, 16, 17, 39, 59, 60, 72, 81, 90, 91, 92, 98,
regenerate, 215 141, 142, 143, 163, 167, 168, 173, 184, 212, 251,
regulations, 273, 319 254, 273, 279, 283, 292, 294, 296, 316, 326, 328,
rehydration, 168 329, 348
reproduction, 74 saponin, 313, 314, 316
repulsion, 16, 52, 53, 77, 82, 120, 145, 154, 160, 168 saturated fat, 108, 111, 112, 113, 114, 116, 129
requirements, 1, 3, 37, 196, 272, 284, 289, 331, 348 saturated fatty acids, 108, 111, 112, 113, 114, 116,
researchers, 58, 66, 181, 188 129
residues, 5, 17, 39, 40, 41, 42, 43, 44, 46, 55, 58, 74, saturation, 19
76, 84, 87, 95, 96, 98, 145, 146, 148, 153, 165, scanning calorimetry, 30, 156
166, 177, 181, 183, 231, 233, 234, 239, 273, 303, scavengers, 71, 128, 281
320, 323, 326, 330, 338, 339 scent, 258
resins, 348 school, 178
resistance, 51, 84, 85, 92, 96, 166, 169, 182, 213, science, xi, xii, 1, 3, 4
287, 305, 323 sclerosis, 194
resorcinol, 315 seafood, xii, 185, 196
resources, 2, 4, 173, 174, 185, 272 secretion, 94, 201, 233, 252, 260, 331
respiration, 93, 205, 316 security, 245
response, 75, 246 sedimentation, 91, 172
restrictions, 289 seed, 114, 176, 177, 184, 188, 198, 203, 289, 293,
retail, 10, 290 295, 304, 314, 315, 331, 332
retardation, 71, 304, 319 selectivity, 132, 133, 318, 324
reticulum, 170 selenium, 222, 309
retina, 193, 194 sensation, 45, 54, 246, 247, 248, 249, 251, 252, 254,
retinol, 191, 192, 193, 194 265, 275
RH, 50, 121, 269 sensations, 252
rheology, 53, 85, 290 senses, 245
riboflavin, 150, 203, 205, 206, 217, 219 sensitivity, 151, 153, 178, 246, 306
ribose, 69, 144, 300 sequencing, 139
ribosome, 150, 310, 311, 312, 313 serine, 99, 111, 140, 170, 231, 320, 336
rickets, 192, 196 serum, 101, 153, 162, 163, 164, 171, 233
rings, 53, 58, 62, 203, 229, 230, 292, 317, 339, 341 serum albumin, 153, 162, 163, 164, 171
risk, 278, 291, 305, 319, 324, 339 sex, 107, 330
risks, 319, 326, 330, 347 sex hormones, 330
RNA, 320 SFI, 119
rodents, 326 shade, 298
ROOH, 121, 281 shape, 1, 2, 21, 22, 23, 46, 51, 52, 53, 79, 80, 91,
room temperature, 49, 115, 118, 203, 212, 276, 279, 118, 145, 152, 153, 158, 159
326, 340, 346, 347 shear, 51, 52, 98, 162, 165, 166, 169, 292, 294
root, 37, 74, 255, 298, 305, 331 shelf life, 30, 33, 82, 86, 95, 96, 120, 157, 277, 278,
roots, 36 281, 284, 289, 339
rubber, 23 shellfish, 269, 317, 318
rubbers, 347 shortage, 319
rubbery state, 33 showing, 249, 276
rules, 109, 140, 141 shrimp, 185, 316
368 Index