Purchased by U.S. Department of Agriculture for Official Use.

Reprinted from CEREAL FOODS WORLD, July 1979, Volume 24, No.7
Published by the American Association of Cereal Chemists, Inc.
3340 Pilot Knob Road, St. Paul, Minnesota 55121
Printed in the U.S.A.

Properties of Proteins Contributing

to Functionality of Cereal Foods 1

J. S. Wall, Northern Regional Research Center, Science and Educational Administration,

Agricultural Research, U.S. Department of Agriculture,z Peoria, IL 61604

The functional properties of proteins in foods, including emulsifier. This versatility reflects the fact that the 21 amino
those in cereal products, are determined by the molecular acids have different side chains tied together in varied sequences
composition and structure of the individual proteins and their and amounts. One protein may contain groups that form
interactions with one another and with other substances. associations with polar substances and groups that favor a
Improving or modifying food characteristics such as viscosity, nonpolar environment.
texture, water absorption, or fat emulsification may involve
altering the constituent proteins or adding other proteins.
Excellent reviews and symposia have related many aspects of TABLE I. Functional Properties of Proteins in Foods
the chemistry of proteins to their contributions to the stability and Their Applications
and organoleptic properties offoods (1-3). However, use of new Property Applications
techniques such as amino acid sequence analysis, x-ray Emulsification Meats, coffee whiteners. salad dressings
crystallography, and NM R in the study of protein structure and Hydration Doughs. meats
physical properties is advancing our concepts of the roles of Viscosity Beverages, doughs
proteins in food processing, structure, and acceptability. Gelation Sausages, gel desserts
Table I summarizes some important functional contributions Foaming Toppings, meringues, angel food cakes
of proteins to foods. The role of proteins, such as those in Cohesion binding Textured products, doughs
dough, may be critical, even though protein may be only a small Textural properties Textured foods
Solubility Beverages
fraction of the food product. Most of the examples in this review
are based on studies of proteins in cereal-<:lerived foods, but the
basic concepts generally apply to other food systems.
Most plant tissues used for food are storage organs, such as
seeds and tubers, where proteins and carbohydrates serve as
reserves. In developing endosperm of cereal grains such as FuilctiolIlI Groups Disrupting Solvents
wheat, most of the proteins are not dissolved in the cytoplasm Bond Type IlIvolved
but are deposited initially in storage organelles, membranes, PIlysical
and other subcellular structures (4). To facilitate their compact E1ettmtJ1ic Carboxyl Salt Solutions
deposition in storage bodies or their insertion into membranes, -CQO-····+NH 3- Amino Hiib or Low pH
seed proteins often have unique compositions. Usually such Imidazole
proteins are modified enzymatically after their synthesis and
Guanido
transport, thus accounting for some of their unusual solubility
and structural characteristics (5). lIydroi!ll IlolllI
One protein may serve both as hydrating agent and fat - C=0...HO- Hydroxyl Urea Solutions
I Amide GualIidille lIydrocbloride
. NH ~~~ ~~l!~~~~ _
1 Presented at the AACC 63rd Annual Meeting held in conjunction with Hydrophobic Bonds Long Alipllatic
the Sixth International Cereal and Bread Congress. Winnipeg,
Manitoba, Canada. September 1978. 0-vvvv Chains Detergents
l Mention of firm names or trade products does not imply their /V'V\./\.-O Aromatic Organic Solvents
endorsement or recommendation by the USDA over other firms or Covalent
similar products not mentioned.
Disulpltide Bonds Cystine Reducing Agents
-$-$- Sulfite
This material was written by Federal employees as part of their jobs and is Mercaptoethanol
considered to be in the "public domain" and not copyrightable. Fig. 1. Types of bonds between protein chains.

PAGE 288/JULY 1979 VOL. 24, NO. 7

 Figure I illustrates the types of bonds that develop between In our laboratory we obtained two lines of evidence
sidechain functional groups of amino acids constituting demonstrating that hydrogen bonding of glutamine amide side
proteins (6). The strongest noncovalent electrostatic bond is chains contribute to wheat gluten insolubility. First. changing
between opposite charges of ionized amino acids. Hydrogen the amide groups to methoxyl groups by reaction in alcoholic
bonds between amide or hydroxyl groups also occur. and those
between backbone chain peptide amide groups are responsible
for a-helical and f3 conformations. Multiple hydrophobic
bonds. although individually weak. can cause associations of
considerable tenacity (7). Similar bonds can occur between 1 2 3 4 5 6 7 8 9 10 11 12 13
proteins and substances such as lipids. polysaccharides. and low NH2'Val·Arg·Val·Pro·Val·Pro·G In·Leu·G In·Pro·Gln·Asn·Pro·
molecular weight organic molecules. Covalent links due to
cystine residues are important intramolecularly in stabilizing
chain folding or intermolecularly in forming bonds between 14 15 16 17 18 19 20 21 22 23 24 25
chains (8).
Ser·G In·Gln·Gln·Pro·Gln·G lu· GIn·Val·Pro·Leu·Val·
PROTEIN STRUCTURE Fig. 2. Amino acid sequence of N-termlnal portion of ao and )',
glladlns (9,10).
The complete amino acid sequence of some important food
proteins has been determined and others are being investigated.
Covalent structures explain some aspects of protein
functionality. For example. the amino acid sequence in Fig. 2
shows that the first 25 N-terminal amino acids of Ponca wheat 0'
or II gliadins are mainly hydrophyllic (9.10). Eight glutamine
residues. including a sequence of three. can engage in hydrogen
bonding. The six proline residues twist the chain at fairly regular
intervals. In another portion of this polypeptide chain. near its
center, the amino acids are primarily nonpolar; three of the six
half-cystine residues are also located in that region (II). The r-;;::-..~/ HHj ICI
sequences of the various residues probably regulate the folding COi"IC
of the chain through their interactions with one another and
with the aqueous environment.
The role of noncovalent bonds in determining protein
secondary and tertiary structure has been confirmed by x-ray
analysis of protein crystals. Figure 3 shows a model of the chains
of the protein a-chymotrypsin in which backbone regions with
a-helicaL folded f3-structure. and random arrangements are
further convoluted into globular structures (12). At 2 A
resolution the sites of the individual amino acids can be located.
and the proximities of functional groups that contribute to
protein tertiary structure can be established. Intramolecular
disulfide bonds due to cystine residues connect different regions
of the chains (indicated by connecting links in Fig. 3). The
conformation of the outer part of the molecule changes with
variations of pH or solvent that alters functional group
interactions (13).
The various functional groups on the outer region of the
protein molecule can interact with appropriate groups in other
protein molecules to cause aggregation. X-ray crystallographic
analysis of the trypsin-trypsin inhibitor complex indicates that
only a small region on the protein surfaces is involved in the
association (14). Hydrogen. electrostatic. and hydrophobic
bonds all participate to hold the proteins together at the active Fig. 3. Conformallon of polypeptide chains in a chymotrypsin A
based on x-ray analysis at 2 A resolution. From Sigler et al (12).
site.

POLAR GROUP INTERACTIONS

The effect of electrostatic forces on the solubility of globular =

:=
-...... 1.0

.--
proteins is clearly illustrated by the difference in solubilities of
the genetic variants of the milk protein f3-lactoglobulin. These E...;;-. . ._----r..;.;,,;;..;.;..:--.-
100% B
proteins have the same shape and size. As shown in Fig. 4. f3-
lactoglobulins A and B vary by only one charged group. but "'"
~ 0.5 / "". ,
75% B - 25% A
their solubilities in aqueous salt solutions at neutrality differ
considerably (IS). The two proteins associate with each other by
~
=> £:_0
.P':........ o - o - - - - o · o
50% B - 50% A
0-------
electrostatic forces. as shown by the solubility curves of A and B c ,&::::~- ..__..__-.;,I,;.;OO;.;"I..;..o..;,A;.... .._
mixtures with solubilities intermediate between those of the : 4')r;."-
pure proteins. Wall and Beckwith (16) demonstrated that the "- aa
solubilities of mixtures of A and B are a function of the amounts 0.5 1.0 1.5 2.0 2.5 3.0
of each protein in the solid. the solubility of each pure protein. Total Protein, grams/lOa ml
and the amount of salt in the solutions. Of course. if the pH of Fig. 4. Solubilities of {3 lactoglobullns A and a and mixtures of A
protein solutions is made more acidic or basic so that negative or and a in 0.00625 M NaCI. {3-lactoglobulin A differs from a by two
positive charges predominate. the proteins will be highly soluble amino acid residues.a. contains alanine and glycine. A contains
due to charge repulsion. valine and aspartic acid. From Treece et al (15).

CEREAL FOODS WORLD/PAGE 289

HCl alters the protein solubility (17). and second. spectroscopic
and solubilitv data indicate that svnthetic polvpeptides
containing high contents of glutamine are asso~iated by
hvdrogen bonds (18). Jankiewicz and Pomeranz' stud v (19)
showed that addition of urea markedly decreased the vis~osity
and cohesiveness of wheat flour dough. as indicated by
decreased mixing time and stability as measured in the
farinograph. This action of urea is attributed to its disruption of
protein-protein hydrogen bonds contributing to gluten
cohesion, because urea forms hydrogen bonds with protein
polar functional groups according to Kuntz and Brassfield (20).
Proteins are important in maintaining moisture in semimoist
foods and baked cereal goods. Kuntz (21) used nuclear magnetic
resonance to examine the extent and sites of water-binding on
synthetic polypeptides formed from single amino acids.
Charged groups on polypeptides or proteins were found to bind
five or six water molecules. since the charges enhance the dipole
moment of the adjacent water molecules. In contrast. uncharged
polar groups attract only one or two water molecules. Nonpolar
groups bind very little water but tend to encourage formation of
neighboring water crystal lattices due to their hydrophobicity.
HYDROPHOBIC BONDS
Many proteins. especially membrane proteins, remain
associated even in the presence of strong hydrogen bond-
breaking solvents such as 8M urea. Various surfactants such as
sodium dodecyl sulfate (SDS) or salts of fatty acids can disrupt
the hydrophobic bonds that unite these proteins. Kobrehel and
Bushuk (22) reported that wheat glutenin disperses well in
sodium stearate solution. During gel filtration chromatography
on agarose columns. glutenin behaves as if it consists exclusively
PAGE 290/JUL Y 1979 VOL. 24. NO. 7
of high molecular weight proteins in 8M urea. When glutenin is
chromatographed on the same column in SDS solution. 10\\
molecular-weight protein is resolved from the higher molecular
weight materials (23.24). The low molecular weight glutenins.
possibly membrane proteins. are associated with the higher
molecular components by hydrophobic bonds.
When hydrophobic bonds link lipid to protein. the protein
properties may be changed. Charbonnier (25) found differences
between the compositions of 70(;i ethanol extracts of defatted
and nondefatted wheat !lours. Based on gel filtration analysis.
the 7OC:i ethanol extracts of the nondefatted !lour contain more
high molecular weight protein. The additional extracted protein
exists as a lipid complex with certain glutenin proteins that.
when free of lipid. are not soluble in 70ci ethanol.
The presence of polar lipids in !lour improves the functional
properties of dough. including the mixing characteristics and
dough strength. Addition of polar lipids or surfactants improves
the tolerance of doughs to mixing and to the addition of soy
proteins for production of breads with acceptable textures (26).
The polar lipid seems to enhance aggregation and cohesion of
gluten proteins.
DISULFIDE BONDS
The role of intermolecular disulfide bonds in functionality of
food proteins. especially wheat !lour doughs. is being critically
reevaluated. Rheological properties of dough are generally
explained in terms of either rather extensive intermolecular
disulfide crosslinks (27) or fairly linear concatenations of
limited disulfide-linked glutenin polypeptide chains (28). Based
on the increasing importance attributed to hydrophobic bonds.
some workers now minimize the need for extensive
intermolecular disulfide bonds. Kasarda et al (29) explain the
action of reducing agents on protein properties as the result of
conformational changes in the proteins after disulfide cleavage.
During gel filtration chromatography. careful fractionation
of proteins dissolved in dissociating solvent provides evidence
that a range of protein species. differing in type and extent of
disulfide bonds. exists in plant seeds. especially endosperms of
cereal grains. Most globulins and gliadins and possibly some
wheat glutenin proteins have only intramolecular disulfide
bonds (Fig. 5). Most acetic acid soluble glutenin molecules have
Class Solubility Features
+ SH
Albumins and
Globulins
Gliadin
Salt Solutions
70% Alcohol
6
+ S's
SH
. \
..
_
-
Solution
Glutenin 1% Acetic Acid
Residue Reducing Agents
or Alkali
Fig. 5. Variation in structure of different wheat gluten proteins
depending on their differences in intramolecular and inter-
molecular disulfide bonds.
limited intermolecular disulfide bonds that result in large
asymmetric molecules having ample surface for associative
interactions. A remaining protein fraction in wheat flour is
insoluble in most protein solvents including acetic acid (30) and
SDS (31) solutions. This residue protein must have extensive
intermolecular disulfide crosslinks. because it can be solubilized
only after reductive cleavage of the disulfide bonds (32).
Huebner and \Vall (33) compared the relative amounts of
proteins differing in number and extent of disulfide crosslinks
for several hard red winter wheats (Fig. 6). The flour varieties
with the strongest mixing properties have the largest amount of
insoluble protein and glutenin with the highest molecular weight
(Glut-I). Apparently the insoluble proteins and the high
molecular weight glutenins are the major factors required to
produce doughs that can tolerate rigorous mixing for bread
production. A suitable mixture of all protein fractions is
necessary to achieve good loaf texture and volume. however.
MODIFICATION OF PROTEIN PROPERTIES
Protein properties can be modified. within limits. toaltertheir
performance in foods and the changes can be made that retain
organoleptic characteristics and nutrition acceptability.
Physical methods of treating proteins can alter protein
products. Mixing changes the rheological properties of wheat
flour gluten. Heating may result in chemical and physical
changes. When corn grain is heated. the albumins. globulins.
and zein proteins become less soluble in aqueous or alcohol
solutions. as shown in Fig. 7 (34). These insoluble denatured
proteins were partially unfolded by heating so that newly
exposed groups formed new bonds (physical and disulfide)
between neighboring protein molecules. When the residue meals
are further extracted with surfactant solutions and solutions
containing reducing agents. the insolubilized proteins can be
solubilized. Denaturation can be a desirable process in food

Gliadin cD
6.0 P~
...= 58~ Mixing
Q
L4: 5.0 Strength
60 ffiII]
bll

~ 4.0 K·51m
K·l.

Insolubles
Albumins

1.0

Fig. 6. Yields of protein fractions from flours of hard red winter wheat varieties differing in baking quality. C, Comanche; P, Ponca; 58,66-
2558; 60, 66-2560; K-5, K501099; and K-1, K-14042. Mixing strength decreases from left to right. From Huebner and Wall (33).

Drying Air
Temperatura

0::
Nitrogen Extracted
by 0.5% SDS in II 15°C

"' 40
cD
Nitrogen Extracted
by 10% EtOH
pH 10 Borate Buffer
+ II 60°C
0.6% Mercaptoethanol
0::
:a 30
I§) 143°C
...e
z
Nitrogen Extracted
... 20
C;;
c:>
I-
by 0.5% SDS in
pH 10 Borate Buffer
'Q 10

o
Fig. 7. Yields of protein nitrogen extracted by different solvents In sequence from meals of corn dried al different temperatures. From Wall
et al (34).

CEREAL FOODS WORLD/PAGE 291

applications if it improves protein hydration and results in
better textured products and gel and foam production.
Additives also can influence protein performance. Earlier we
alluded to the effect of surfactants and lipids on dough protein
performance. The effect of reducing or oxidizing agents on
disulfide groups of proteins in dough is also well established.
The interaction of gluten or other food proteins with gums and
pentosans gives interesting effects (35). Addition of gums to
dough changes the mixing performance, as shown in Fig. 8. The
low protein and weak gluten of the soft wheat Brevor results in
poor mixing characteristics of dough prepared from it. Addition
of 0.6% alginate to the flour increases the mixing time and
dough stability. By forming salt and hydrogen bonds with the
protein, the gums improve the protein functionality.
SUMMARY
Adaptation of computer and electronic technology to protein
research recently is helping to decipher the structures of
complex protein molecules in foods. The sequences in which
amino acids are arranged, the way in which the molecules are
folded, and how they are tied together by disulfide bonds are
being determined. This information provides ideas about how
the functional groups on the molecules are exposed to the
solvent in which they are dispersed and how the proteins interact
with other molecules. Solubility of food proteins depends on
their net positive or negative charges due to ionizable amino
acids. Protein aggregation through hydrogen and hydrophobic
bonds contributes viscosity, cohesion, and bonding properties
to food ingredients. Lipids bind to proteins mainly through
. r
I \. ,'"
\.\5~ ~\~revor'\
~- ." \ ~\ te, \ . \ . \
\ 0.3 g Alginate
-t--+-'rl-.......,.~b-+-~ nnn- ~ ~ -----\----',----'I---'--\---'c---',----'H-'
\ 33 ml Water \
Fig. 8. Effect of addition of alginate gum on mixing characteristics
of a soft wheat flour. From Huebner and Wall (35).
PAGE 292/JUL Y 1979 VOL. 24. NO. 7
association with hydrophobic groups; the lipid may contribute
to cohesion of the protein. Despite current controversy.
intermolecular disulfide bonds in gluten best explain many
aspects of dough rheology. Additives such as lipids or gums
modify protein functionality by combining with the protein
molecules.
As more is learned about the basis of cereal and food protein
function, we may be able to better develop and select improved
plant varieties or chemically and physically modify their
proteins to optimize their performance in specific foods.
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(cOfl!'d on page 3/3)
Technical Section
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New Members
(cont'dfrom page 307)
Co, Ltd., 27-5, Sendagaya 5-chome, Shibuya-ku, Tokyo, Japan.
Lee, Chao-Chou (Graduate Research Assistant), Kansas
State Univ., Dept. of Grain Science & Industry, Manhattan, KS
66506.
Lin, Chifa F. (Research Associate, Research & Develop-
ment), Stauffer Chemical Co., Eastern Research Center, Dobbs
Ferry. NY 10522.
Martin, August J. (Baking Technology, Keebler Co.), 1655 S.
Oakland Ct., Aurora, CO 80012.
Matsuda, Kenichiro (Student, Kyushu Univ.), 6295
Hoshikuru, Nichinan, Miyazaki 889-25, Japan.
Mauger, Robert E., Sr. (Quality Assurance Manager,
International Division), Gerber Products Co., 445 State St..
Fremont, MI 49412.
McKay, Jane (New Product Development), Pillsbury Co.,
311 S.E. Second St., Minneapolis, MN 55414.
McLaughlin, Elizabeth E. (Yeast Research, Fermentation,
and Bake Tests), Universal Foods Corp., Technical Ctr., 6143
N. 60th St., Milwaukee, WI 53218.
McQuilkin, Catherine (Nutrition Analyst, USDA, Hyatts-
ville, MD), 3218 Wisconsin Ave" N.W., Apt. 101, Washington,
DC 20016.
Meiske, Donna P. (Instructor for Basic Food Science), Univ.
of Minnesota, Dept. of Food Science & Nutrition, 1334 Eckles,
St. PauL M N 5510 1.
Morad, M. M., SEA-AR-USDA, Wheat Quality Lab., II
Wilson Hall, Washington State Univ.. Pullman, \VA 99164.
Ophuis, Bernard O. (Supervisor, Agro-Industrial Projects),
The World Bank, 1818 H St., N.W., \Vashington, DC 20433.
Pancoe, Edward M. (Technical Sales Representative), Atlas
Chemical Industries, Canada, P.O. Box 1085, Brantford, Ont.,
Canada N3T 5T2.
Poock, Steven J. (Quality Control Manager), Grain
Processing Corp., 1600 Oregon St., Muscatine, IA 52761.
Rounds, Stephen P. (Coordinate Effons of Labs with Baking
Industry, Eastman Chemical Products). Kingsport,
TN. 36 Quaker Rd., Princeton Jct., NJ 08550.
Sauer, Charles, (Supervisor and Bench Work, Amstar
Corporation), 1005 W. Stinson, Dimmit, TX 79027.
Schilling, Otto P. (Technical Sales Service), Ogilvie Mills
Ltd., 1620 Sun Life Bldg., MontreaL Que., Canada H3C 3H 1.
Sciberras, Joe (Quality Control Inspector, Maple Leaf Mills
Ltd.), 23 Rayside Dr., Etobicoke, Ont., Canada.
Setser, Carole S. (Assistant Professor), Kansas State Univ.,
Dept. of Foods and Nutrition, Manhattan, KS 66506.
Shirao, Yoshihiro (Product Development), Nippon Flour
Mills Co. Ltd., No. 27-5, Sendagaya 5-chome, Shibuya-ku,
Tokyo, Japan.
Smith, Randall L. (Analytical Chemist), Raltech Scientific
Services, Kindsmen Blvd., Madison, WI 53707.
Summers, Arthur W. (Quality Assurance Section Manager),
Safeway Stores, Inc., Bakery Division, Oakland, CA 94660.
Szalai, Lajos, Research Institute for Baking Industry,
Dombovari ut 5-7, 1117 Budapest, Hungary.
Teicher, Harry (Senior Research Group Leader), Monsanto
Co., 800 N. Lindbergh Blvd., St. Louis, MO 63166.
Toney, John W. (Director, Technical Service), Henningsen
Foods, Inc.. 14334 Industrial Rd .. Omaha, NE 68144.
Trentesaux, Etienne (Director of Research), Semoulerie de
Bellevue S.A., 131 Ave, Corot, 13013 Marseille, France.
Trood, Ian S. V. (Service Feed Additive Equipment),
Pennwalt Flour Service Division, 700 3rd Line, Oakville. Ont..
Canada.
Veach, Susan K. (Student), 1122 Bluemont, Apt. 3,
Manhattan. KS 66502.
Wasik, Ronald J. (President), R.J.W. Consulting, 1293
Limberlost Rd .. London, Ont.. Canada N6G 3Ml
Wise, Charles E. (Development and Quality Assurance,
Bakery Mix Fried Products, Pillsbury Co.), 6036 11th Ave.. S..
Minneapolis. MN 55417.
CEREAL FOODS WORLD/PAGE 313