Critical Reviews in Food Science and Nutrition

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Milk Proteins for Edible Films and Coatings

KHAOULA KHWALDIA , CRISTINA PEREZ , SYLVIE BANON , STÉPHANE

DESOBRY & JOËL HARDY

To cite this article: KHAOULA KHWALDIA , CRISTINA PEREZ , SYLVIE BANON , STÉPHANE
DESOBRY & JOËL HARDY (2004) Milk Proteins for Edible Films and Coatings, Critical Reviews in
Food Science and Nutrition, 44:4, 239-251, DOI: 10.1080/10408690490464906

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Critical Reviews in Food Science and Nutrition, 44:239–251 (2004)
Copyright C Taylor and Francis Inc.
ISSN: 1040-8398
DOI: 10.1080/10408690490464906

Milk Proteins for Edible Films

and Coatings

KHAOULA KHWALDIA, CRISTINA PEREZ, SYLVIE BANON,

STÉPHANE DESOBRY, and JOËL HARDY
Laboratoire de Physico-Chimie et Génie Alimentaires, Vandoeuvre-lès-Nancy Cedex, France

Due to the recent increase in ecological consciousness, research has turned toward finding edible materials. Viable edible
films and coatings have been produced using milk proteins. These films and coatings may retard moisture loss, are good
oxygen barriers, show good tensile strength and moderate elongation, are flexible, and generally have no flavor or taste.
Incorporation of lipids in protein films, either in an emulsion or as a coating, improve their properties as barriers to moisture
vapor. Interactions between chemical, structural properties, as well as film-forming conditions and functional properties of
edible milk films are elucidated. Some potential uses of milk protein packaging, which are hinged on film properties, are
described with examples.

Keywords edible films, bio-packaging, milk proteins, casein, whey protein, permeability, tensile properties

1. INTRODUCTION be reduced and package recycling can be improved. Their pur-

Edible films and coatings are traditionally used to improve
food appearance and conservation. The most common exam-
ples are wax coatings for fruit,1,2 chocolate coatings for confec-
tionery, lipid films to protect meat products, and soy milk-based
lipoprotein films to improve the appearance and preservation of
certain foods in Asia.3–5
Considerable interest in edible films has been renewed due
to their environmentally friendly nature and their potential use
in the food industry.6–10 Edible films and coatings are natural
polymers obtained from agricultural productions such as animal
and vegetable proteins,11,12 gums, and lipids and are perfectly
biodegradable, and therefore perfectly safe for the environment.
Edible films formed as coatings or placed between food com-
ponents provide possibilities for improving the quality of het-
erogeneous foods by limiting the migration of moisture, lipids,
flavors/aromas, and colors between food components, carry-
ing food ingredients (e.g., antioxidants, antimicrobials, flavor),
and/or improving the mechanical integrity or handling characte-
ristics.13 Edible films and coatings also have the potential to re-
duce packaging waste through source reduction. To the degree
that an edible film coating acts as an efficient moisture, oxygen,
or aroma barrier, the amount and/or complexity of packaging can
Address correspondence to Khaoula Khwaldia, Laboratoire de Physico-
Chimie et Génie Alimentaires, INPL-ENSAIA, 2 avenue de la Forêt de Haye, BP
172, 54505, Vandoeuvre-lès-Nancy Cedex, France. E-mail: khaoula khwaldia@
yahoo.fr
239
pose is not solely to replace synthetic packaging films but they
provide opportunities for new product development as well.6
Edible films have the potential to control mass transfer be-
tween food and the environment and also between various food
product components, thus extending shelf life and improving
quality.12,14–19 They are generally made from proteins, polysac-
charides, and lipids used alone or together.
Proteins-based films have more interesting mechanical and
barrier properties than polysaccharides. Many protein materials
have been tested: collagen, corn zein, wheat gluten, soy protein
isolate, fish proteins, ovalbumin, whey protein isolate, casein,
etc.20–24 In addition to their nutritional value, milk proteins, such
as casein, have several key physical characteristics for effective
performance in edible films, such as their solubility in water
and ability to act as emulsifiers. Furthermore, considerable in-
terest exists in finding new uses for milk proteins due to their
industrial surplus. The objectives of this article are to (a) review
important milk-protein characteristics, (b) relate the composi-
tion and structure of milk-protein-based films and coatings to
their functional properties, and (c) summarize applications of
milk-protein films in food products.
2. FILM FORMATION: MILK CONSTITUENT
INTERACTIONS
Packaging films must include at least one synthetic or natu-
ral polymer able to form a cohesive and continuous matrix. Two
240 K. KHWALDIA ET AL.
general processes for bio-packaging formation can be distin-
guished: the dry and the wet process. The dry process is based on
the thermoplastic properties of biopolymers heated above their
glass transition temperature under low water content conditions.
Thermoplastic biopolymers are used either to form biodegrad-
able packaging materials or as a component of composite pack-
aging materials. The wet process is based on a film-forming
dispersion of biopolymers. This procedure is generally used for
preformed films and coatings.4 Food grade solvent systems for
edible films and coatings are limited to water, ethanol, or a com-
bination of the two.
Several reviews on edible film technology have been pub-
lished, presenting mechanisms and techniques for forming and
applying films and coatings.25,26 Kester and Fennema10 sug-
gested that edible films and coatings could be formed by an
associative phase separation or coacervation mechanism. De-
pending on the presence of one or two biopolymers in the solvent
system, the coacervation could be simple or complex.
2.1. Simple Coacervation
The formation of film by simple coacervation has been widely
studied. 10,27,28 Coacervation is based on the separation of the
solvent phase from biopolymer by precipitation or phase change
due to its incompatibility. The solvent system promotes biopoly-
mer/biopolymer interactions through water competition. The
simple coacervation is produced by the removal of the solvent,
by the addition of a non-electrolyte solute in which the polymer
is not soluble (e.g., zein and wheat gluten films), by the addition
of an electrolyte substance inducing “salting out” effect, or by
the modification of the pH of the solution. It could also result
from thermal treatment (e.g., soy protein films) or cross-linking
agent addition (e.g., whey protein films produced by enzymatic
crosslinking using transglutaminase).29
Solvent evaporation, heat denaturation (e.g., ovalbumin), or
even simple cooling of a warm biopolymer suspension followed
by gelation (e.g., gelatin or agar) or precipitation in the film pro-
duces an increase in the polymer concentration, causing a molec-
ular aggregation and a three-dimensional network formation.
The most cohesive films are obtained when the temperature
gradient between the film solution and the surface is low.25 Ex-
cessive temperature results in a rapid solvent evaporation and
prematurely immobilizes the biopolymer molecules before they
have the opportunity to coalesce into a coherent film, without
pinholes or non-uniform thickness (both of which increase film
permeability). Film forming protocol influenced the efficiency
of solvent evaporation being faster in atomized coating suspen-
sion than in casting or immersion.
In some circumstances, combined effects could favor film
formation. For instance, films produced by casting suffer a ther-
mal denaturation associated with solvent evaporation.11,30 Ther-
mal denaturation of the protein leads to exposition of hydropho-
bic groups, preferentially oriented towards the atmosphere and
molecular interaction in order to create a structured network.
Likewise, film solution containing acids or bases suffers a com-
bined effect due to the increase of polymer concentration asso-
ciated with solvent evaporation and also with pH modification
due to the removal of volatile acid or base. The simple coacer-
vation mechanism is dependent on parameters such as pH, ionic
strength, biopolymer–solvent ratio, temperature, and molecules
structure.
Long chain polymeric structures are required to yield film ma-
trices with appropriate cohesive strength when deposited from a
suitable solvent.25 Denaturing and cross-linking additives pro-
mote molecular order and, therefore, increase cohesion and rigid-
ity of films.3 The strength of protein films tends to increase upon
aging, reflecting rearrangements and increased interactions be-
tween component molecules in the film.
Molecular interaction degree depends upon the protein struc-
ture and degree of hydrophobic and hydrophilic amino acid in the
protein chain. A uniform distribution of polar groups along
the polymer chain increased cohesion and thus the possibil-
ity of interchanging hydrogen bonding and ionic interactions.25
The amount of hydrophilic amino acid residues is decisive in
film mass transport properties, especially when exposed to a
higher relative humidity.31 Films with high molecular interac-
tions present a rigid structure, non-flexible and with lower per-
meability value.
2.2. Complex Coacervation
Complex coacervation occurs when two or more oppositely
charged biopolymers are combined in a solvent system, caus-
ing electrostatic interactions and precipitation of the biopoly-
mer complex. For example, Shih32 studied the interaction of
soy isolate with sodium alginate and propylene glycol alginate.
The complex formation was controlled by electrostatic inter-
actions, and, to a lesser extent, by covalent bonding. Another
study related the formulation of edible films based on a blend of
sodium caseinate and wheat or corn starches in water.33 Among
the number of parameters affecting the coacervation, eg. pH,
ionic strength, biopolymer ratio, total biopolymer concentra-
tion, molecular structure of biopolymers, the charge density is
the most significant parameter.34 Complex coacervation is sup-
pressed at high macromolecular concentrations and low charge
densities.35 Low temperature enhances the extent of phase sep-
aration by increasing biopolymer/biopolymer interactions.36
A. Films from Total Milk Proteins
Cow’s milk contains about 33 g of protein/L. Milk proteins
are classified into two types: casein and whey protein.37 The film-
forming ability of caseins and whey proteins has been studied in
the last decade. It has been shown that edible films and coatings
can be formed from total milk proteins (TMP) or components
of milk protein.38–40 More fundamental studies have also been
performed to understand the film formation and to relate prop-
erties of protein based films to molecular and environmental
factors.12,31,41
 MILK PROTEINS FOR EDIBLE FILMS AND COATINGS
Krochta31 showed the effect of protein structure and compo-
sition on edible film barrier properties. For effective formation of
a cohesive film, biopolymer-biopolymer interactions are critical
in forming a continuous three-dimensional network. The nature,
type, and extension of interactions depend upon the proteins in-
volved and the environmental conditions. The relative contribu-
tion of each phase (air and solvent media) to stable film formation
has not been established. Banker25 suggested that maximum sol-
vatation and extension of the polymer molecules could lead to
cohesive structure.
Maynes and Krochta40 studied the TMP obtained from non-
fat dry milk (NFDM) for edible film formation. These films
were formed by drying the film solution on smooth casting sur-
faces at room temperature. The formation of TMP films was
complicated due to the presence of lactose, which crystallized
during film formation and leads to non-homogeneous film and
film adhesion to surfaces. Lactose can be extracted from NFDM
by ultra-filtration (UF) or suspension in ethanol followed by
a filtration. Addition of potassium sorbate inhibits crystal-
lization.40 UF-TMP films are more flexible and with better
water moisture barrier, but denaturation by ethanol may re-
duce film water solubility. Heating TMP solution up to 135◦ C
produces insoluble films, and films are stronger and less brit-
tle due to the dissociation of micelles and intermolecular
bonds.42
B. Films from Caseins and Caseinates
Casein, which comprises 80% of milk protein, consists of
three principal components: α, β, and κ-casein, that together
form colloidal micelles in milk containing large numbers of
casein molecules and are stabilized by calcium-phosphate
bridging.43–45 The amino acid composition of casein explains
some of its properties. Low levels of cysteine result in few
disulfide cross-linkages and, thus, an open random structure.
In comparison with whey protein, the casein has a high content
of proline. As a result, caseins have better emulsifying properties
than whey proteins. They are soluble and able to form films ex-
hibiting resistance to thermal denaturation and/or coagulation,
which means that the protein film remains stable over a wide
range of pH, temperature, and salt concentrations.43
Little work has centered on individual casein fractions-based
films due to high manufacturing costs. The ß-casein films are
expected to have lower water vapor and gas permeabilities than
other milk protein films.46
Skim milk at pH 4.6 and 20◦ C produces commercially avail-
able caseinates.47 Precipitated caseins can be brought into so-
lution by neutralization through the addition of alkali. Sodium
(NaCas) and calcium caseinates (CaCas) are most common, but
magnesium (MgCas) and potassium caseinates (KCas) are also
available commercially.43 NaCas and PCas have better func-
tional properties, especially solubility, than calcium and mag-
nesium derivatives. NaCas is very heat stable, whereas CaCas
is heat stable at 120◦ C for 15 min at pH greater than 7 for a
concentration above 4% (w/w).
241
Caseinates easily form films from aqueous Caseinates solu-
tions due to their random coil nature and their ability to form ex-
tensive intermolecular hydrogen, electrostatic, and hydrophobic
bonds, resulting in an increase of the interchain cohesion.21,48–50
These films are easily water-soluble, however submitting these
films to a buffer solution at the isoelectric point of casein resulted
in water-insoluble films.51
The highly hydrophilic nature of caseinate films and coat-
ings limits their ability to provide a significant moisture barrier.
The increase of cohesion between protein polypeptide chains
is effective to improve the barrier properties of the films. Ca-
seinates were reported to be cross-linked with calcium ions21
and transglutaminase (Tgase ).52,53 Nevertheless, manufacturing
of milk protein films by the mechanism of Tgase -catalyzed poly-
merization is difficult because of high production cost and lim-
ited availability of the enzyme.
More recently, Brault et al.50 have used γ -irradiation to pro-
duce cross-linked CaCas films. Their work showed that the films
had improved mechanical properties and were water-resistant.
Krochta et al.51 took advantage of the emulsifying capabilities
of casein to create casein-lipid emulsion films with improved
moisture-barrier properties. In those emulsion films, the lipid
material provided resistance to water transfer, while the casein
provided structural cohesion, bound the film to wet surfaces, and
reduced the waxy appearance.
C. Films from Whey Proteins
Whey protein is the protein that remains soluble after casein
is precipitated at pH 4.6. Whey proteins, which are globular and
heat labile in nature, consist of several component proteins, in-
cluding α-Lactalbumin (α-La), β-Lactoglobulin (β-Lg), bovine
serum albumin (BSA), immunoglobulins (Ig), and proteose-
peptones (PP).54 β-Lg contains one free thiol group and two
disulfide groups per monomer; 4 hydrophobic groups are lo-
cated inside the globular structure.55,56
Whey protein fractions based edible films have not been ex-
tensively studied because of the purification and separation cost.
The most commonly used methods today for the production of
whey protein concentrates (WPC) are ultrafiltration and diafiltra-
tion because of their advantages of cost reduction, high process
speed, and the absence of protein denaturation.57 Industrially
produced WPC have a protein content of 25–80%. Whey pro-
tein isolates (WPI), which have a protein content of about 90%,
are prepared from WPC by adding an ion-exchange step.58
Heat denaturation above 65◦ C, opens the β-Lg globular struc-
ture, exposes sulfhydryl and hydrophobic groups, and induces
oxidation of free sulfhydryls, disulfide bond interchange, and
hydrophobic bonding.55,59–61 These reactions can be used to
form water-insoluble edible films.46,62,63 Heat denaturation also
promotes interactions between whey proteins and caseins and
causes dissociation of micellar protein.42 At higher temperature,
α-casein is intimately associated to the micelle, but upon cool-
ing below 40◦ C up to 50% of the complexes can dissociate.42
Presence of lactose increases the minimum temperature required
242 K. KHWALDIA ET AL.
for thermal denaturation.64 Free sulfhydril groups that are nor-
mally occluded within β-Lg and BSA can be exposed by heat-
ing, treatment with alkali65 or urea,66 and by adsorption at an
interface.67,68 Plasticizer addition in the denatured film solu-
tion could improve material flexibility, but increases the WVP.
Currently, edible film based on WPC have been developed and
compared with other protein products.62,69
Mahmoud and Savello70,71 examined the mechanical and wa-
ter vapor barrier properties of α-La, β-Lg, and a mixture of α-La:
β-Lg films. They used Tgase as a cross-linking agent to produce
films. 5% whey protein were covalently polymerized in a pH
7.5 buffer solution under reducing conditions (Dithiothreitol,
DTT) with calcium ions and glycerol (Gly). The dithiothreitol
changes the protein configuration and access of lysil and glu-
tamyl residues are accommodated to the active site of Tgase dur-
ing the cross-linking.72 Gly concentration directly affected film
resistance to breakage, moisture content, and resistance to water
vapor transfer. α-La: β-Lg mixed films were more permeable to
water vapor than either pure protein fraction.
McHugh et al.22 found that whey protein isolate films could
be produced without the use of enzymes by heating 8–12% whey
protein solutions between 75 and 100◦ C. Films were formed by
drying film solutions overnight on smooth, level casting surfaces
at room temperature. Without heat denaturation, films cracked
upon drying, while resultant films produced by thermal denat-
uration were extremely brittle, requiring the addition of food
grade plasticizers to impart film flexibility. In contrast to ca-
seinate films, whey protein films are water insoluble due to the
presence of covalent disulfide bonds. WPI films are excellent
barriers to the transport of CO2 and O2 .13
Individual caseins have random structures and are not notably
denatured by heat. Casein micelle size is not greatly changed
by heat, but heat can induce interactions between whey proteins
and caseins and can cause dissociation of micellar protein.42 The
α-casein unfolds less than α-casein at the air/water interface be-
cause it has a more ordered tertiary structure but may arrange
with time. Significant protein-protein interactions, repulsions,
and attractions occur between segments of polypeptide chains
that extended both above and below the plane of the air/water
interface in surface protein films. Whereas caseins form weak
films with low viscosity, globular β-Lg, α-La, and BSA form
stronger viscoelastic films73 reflecting greater interactions and
possible entanglements between the globular proteins which re-
tained tertiary structure in the film and presented greater resis-
tance to flow.74 Increasing pH indicates that the increased net-
work negative charge, by causing excessive repulsion, reduced
the formation of a continuous cohesive viscoelastic film.
3. FILM STRUCTURE INFLUENCES
ON FUNCTIONAL PROPERTIES
The properties of edible films have been reviewed
by.5,10,31,75,76 These properties, such as barrier, mechanical, and
sensory properties, depend on the nature of components and film
composition and structure. Edible films often require incorpora-
tion of additives (plasticizers, crosslinking, and texture agents)
to enhance some properties.
The addition of a plasticizing agent to edible films is required
to overcome film brittleness caused by extensive intermolecular
forces. Plasticizers reduce these forces and increase the mobility
of polymer chains, with a resulting increase in the mobility of
polymer chains and more flexible films.25 However, plasticizers
not only improve the mechanical properties of films but also
increase the film permeability.77
Plasticizers, which can interfere with protein chain-to-chain
hydrogen bonding, such as Gly, polyethylene glycol (PEG), sor-
bitol (Sor), and water, are generally used to form protein films.
The ability of a plasticizer to disrupt protein-chain hydrogen
bonding is influenced by the plasticizer’s composition, size, and
shape.78,79 These factors have been invoked in the literature to
explain the differences in film strength and permeability of many
plasticized protein systems, including NaCas (Gly and PEG),49
whey proteins (Gly vs Sor),80 γ -irradiated caseinate (propylene
glycol (PG) and triethylene glycol),81 and β-lactoglobulin (Gly,
PEG, Sor, PG, sucrose).79
Water is the most uncontrollable plasticizer for edible films
because it is able to affect the texture of many polymers. The
migration of sorbed water vapors swells the hydrophilic films,
which markedly increases the diffusion coefficient. Thus, film
moisture content as affected by content of other plasticizers and
the surrounding relative humidity can have a dramatic effect on
edible-film properties. The plasticizing effect of water may be
based on weakening hydrogen bonds and dipole-dipole intra-
and inter-macromolecular interactions due to the shielding of
these mainly attractive forces by water molecules, hence increas-
ing the free volume and reducing the glass transition temperature
of the biopolymer.82–84 Manheim and Passy85 defined the per-
meability as the state that permits the transmission of permeants
through materials. The water vapor permeability (WVP) is based
on Fick’s first law of diffusion and Henry’s law of solubility.
The temperature, size, shape, and polarity of the permeant
molecule, as well as polymer chain segmental motion within
the film matrix, affect the diffusion and solubility of permeants.
Besides, these two parameters depend on the type of forces be-
tween molecules of the film matrix, such as hydrogen bond-
ing and Van der Waals interactions, the degree of cross-linking
between molecules, the crystallinity, and the presence of
plasticizers or additives.49,86–88 Generally, polymer permeabil-
ity decreases with increasing cristallinity, density, orientation,
molecular weight, and cross-linking of the molecules during pre-
processing steps and film formation.3
In any polymeric packaging film or coating, two sets of forces
are involved: cohesion (interactions between film-forming poly-
mer) and adhesion (interactions between the polymer and the
food molecules for coatings only). The degree of cohesion,
which affects film properties such as flexibility and gas and
solute barrier properties, depends on biopolymer structure,
manufacturing process, physicochemical conditions (tempera-
ture, pressure, solvent composition and concentration, solvent
 MILK PROTEINS FOR EDIBLE FILMS AND COATINGS 243

evaporation method), presence of plasticizers and cross-linking
additives, and final thickness of the film.25,3 High chain order
in polymers favors film cohesion. Excessive solvent evapora-
tion or cooling may sometimes produce non-cohesive films due
to immobilization of polymer molecules before they coalesce
into a continuous, coherent film and inadequate associations of
polymer chains.25
3.1. Barrier Properties (H2 O, Gas, Aroma)
A. Water Vapor Permeability
To avoid the moisture transfer that can affect food quality,
WVP control is important to get stability and safety during dis-
tribution and storage. The most common method used for the de-
termination of WVP through films and thin sheets of packaging
is the standardized gravimetric method.89,90 Under well-defined
environmental conditions (% relative humidity (RH) and tem-
perature (T)), permeability of bio packaging is related to the film-
permeant system. Table 1 shows WVP values of milk proteins-
based edible and synthetic films.
Adjustment of NaCas film to the isoelectric point of casein
insolubilizes the film and also produces significant reduction in
WVP, most likely due to increased protein-protein interaction.
It was reported that ionic cross-linking reduced protein polymer
segmental mobility, as well as protein solubility in water, thus
reducing water vapor and gas permeability through the protein
matrix.51
Avena-Bustillos and Krochta21 reported that the adjustment
to pH 4.6, calcium ion cross-linking, and combined effects with
calcium ascorbate buffer reduced WVP of NaCas films by 36%,
42%, and 43%, respectively (table 1). The use of physical treat-
ments, such as irradiation, can also increase the cohesive strength
of the protein by the formation of cross-links. γ -irradiation treat-
ment reduced by about 40% the WVP of films cast from solutions
containing different WPI-CaCas ratio.91
1. Effect of Adding Lipids. One of the principal functions of
an edible film or coating is to impede moisture transfer; lipids can
be incorporated in the film because of their hyrorepellency.92 Ac-
cording to Blank,93,94 lipids with the best H2 O barrier properties
are those formed from saturated, straight-chain, fatty acids, fatty
alcohols, and esters containing 16 carbons or more. Increased

Table 1 Water vapor permeability of milk protein-based edible and synthetic films (adapted from
Refs. 19, 31, and 46)

Thickness Test conditionsa Permeability

Film (µm) (T, ◦ C; RH, %) (g.mm/m2 .d.kPa) References

UF-TMPb :Glyc (4:1) 71 25; 0/65 70.3 40

NaCasd 83 25; 0/81 36.7 21
CaCase 82 25; 0/85 28.1 21
Buffer-treated NaCas 70 25; 0/84 24.9 21
(pH4.6)
Buffer-treated NaCas 72 25; 0/86 22.3 21
(pH4.6)
Buffer-treated NaCas 72 25; 0/86 20.9 21
(pH4.6)
CaCl2 -treated NaCas 58 25; 0/83 21.1 21
(pH9.6)
NaCas:AM f (2:2) 88 25; 0/88 22.1 21
NaCas:AM (1:4) 40 25; 0/84 15.8 21
NaCas:lauric acid (4:1) 74 25; 0/92 9.6 49
NaCas:Gly (0.89:1) 104 20; 45/0 11.5 19
NaCas:Gly (1.67:1) 72 20; 45/0 5.4 19
NaCas:PEGg (0.81:1) 99 20; 45/0 22.3 19
NaCas:PEG (1.32:1) 71 20; 45/0 14.8 19
WPIh :Gly (1.6:1) 106 25; 0/11 6.64 22
WPI:Gly (1.6:1) 121 25; 0/65 119.8 22
WPI:Gly (4:1) 129 25; 0/77 70.2 22
WPI:Sori (1.6:1) 129 25; 0/79 62 22
WPI:BW j :Sor (3.5:1.8:1) 19 25; 0/93 28.1 38
WPI:BW:Sor (3.5:1.8:1) 14 25; 0/98 5.3 38
LDPEk 25 38; 90/0 0.08 144
HDPEl 25 38; 90/0 0.02 144
Cellophane 25 38; 90/0 7.27 145
EVOHm (68% VOHn ) —∗ 38; 90/0 0.25 145
a Relativehumidities (RH) were those on outside and inside of the test cup (outside/inside); b Total milk
protein obtained by ultrafiltration; c Glycerol; d Sodium caseinate; e Calcium caseinate; f Acetylated mono-
glyceride; g Polyethylene glycol; h Whey protein isolate; i Sorbitol; j Beeswax; k Low density polyethylene;
l High density polyethylene; m Ethylene vinyl alcohol; n Vinyl alcohol.
∗ Not specified.
244 K. KHWALDIA ET AL.
unsaturation or branching and reduction in carbon chain length
result in increased moisture permeability. Kester and Fennema95
observed the following barrier efficiency order stearic alcohol
> tristearine > beeswax > acetylated monoglycerides > stearic
acid > alkanes. These differences can be explained by the pres-
ence of relatively large pores in some lipid surface layer, and
by the homogeneity of the composition of the network, related
to polymorphic shape and orientation of the chains in the lipid
layers.
Addition of lipids to hydrophilic protein-based films by form-
ing a stable emulsion39,96 or by laminating the film with a lipid
layer,97,98 greatly improves water vapor barrier properties. The
barrier efficiency of such composite films strongly depends on
the polarity of the film components and the uniform or dis-
persed distribution of hydrophobic substances in the component
films.99,100 Martin-Polo et al.97 showed the importance of the
affinity (difference in polarity) between the continuous and the
dispersed phase on water transfer: the lower the affinity, the
lower the homogeneity of the film. Some studies indicated that
bilayer films have 10-1,000 times better barrier efficiency against
water transfer than emulsified films.95–100
For emulsion-based edible packaging, the water vapor effi-
ciency depends on the lipid type, amount, and structure (solid fat
content, crystal type). Lipids with long fatty acid chains decrease
the WVP because of lowered water solubility.38 Solubility arises
when the relative weight fraction of apolar molecule increases
because the attractive solute-solvent forces become stronger than
the solute-solute forces. Perez-Gago and Krochta101 reported
that the different chemical composition of lipids could be respon-
sible for the difference in particle sizes. Particle size increased
with increased chain length of fatty acid in whey protein-fatty
acid emulsion films.102 The most hydrophobic lipids have the
best barrier efficiency.27
Shellhammer and Krochta103 studied the effect of the lipid
type in whey protein emulsion films on WVP. They found that
beeswax emulsion films are consistently the lowest in WVP at
each concentration. Crystalline lipids provide a better barrier
to moisture transport than do liquid lipids. Consequently, high-
melting fatty acids and monoglycerides, hydrogenated fats, and
waxes are useful edible lipid barriers in a composite film.10,104,105
Several authors90,95,97,106 have shown that orthorhombic lipid
crystals, found in beeswax and paraffin wax, have better barrier
efficiency than hexagonal crystal types such as those found in
tristearin or acetylated monoglycerides. This is explained by a
more dense and compact structure of orthorhombic lipid crys-
tals, which contain less free volume for water molecule migra-
tions. Lipids can form good barriers to moisture transmission,
but these compounds have certain disadvantages with respect to
application, mechanical and chemical stability, and organoleptic
quality.
2. Plasticizing Effect on WVP. Siew et al.19 studied the ef-
fect of Gly and PEG on the WVP of NaCas films. At similar
plasticizer concentrations, the films containing PEG have higher
WVP (Table 1). This could be explained in terms of differences
in film molecular structure. A larger percentage of random coil
segments was found in the NaCas/PEG films, indicating that this
structure forms an open molecular network conductive for water
transport. The higher WVP of the PEG films compared to the
Gly system can also be partly associated with the hydratation of
the plasticizers. The PEG system is more effective in attracting
water molecules to the film surface and, hence initiating water
transmission.
B. Gas Permeability
Most of edible films are water sensible, but their hydrophilic
property makes them excellent barriers against the non-polar
substances, as aromas and oxygen. Dry hydrocolloid films have
good oxygen barrier properties. In the presence of moisture,
the macromolecule chains becomes more mobile which leads
to a substantial increase in O2 permeability.86 The prediction of
O2 and aroma transport depends on the compilation of barrier
properties and their correlation with edible polymer structure
and composition. It will be possible to apply generalized the-
ories explaining O2 and aroma mass transfer behavior to solve
food and economic packaging problems. Generally, polymer
permeability decreases with increasing cristallinity, density, ori-
entation, molecular weight, and cross-linking of the molecules
during pre-processing steps and film formation.3
Gas permeability could be determined by several techniques
as gas chromatographic, manometric, volumetric, isostatic con-
centration, coulometric, infrared detection, and bioluminescence
methods.48 In general, protein films appear to have lower O2
permeabilities than non-ionic polysaccharide films. This may
be related to their more polar nature and more linear struc-
ture, leading to higher cohesive energy density and lower free
volume.107
O2 permeability of milk protein-based edible films is not
sufficiently explored. O2 permeabilities of protein-based edible
and synthetic films are listed in Table 2. Films that are based
on globular proteins appear to have greater O2 permeabilities
than of collagen-based films at (0%RH).80 This is probably due
to the fact that globular proteins possess a greater percentage
of large amino acid and a lower linear structure, resulting in
a smaller cohesive energy density and larger free volume. Low
O2 permeability value of milk protein-based films could be thor-
oughly employed in postharvest control of fresh fruits and veg-
etables and could benefit directly the commodity quality. Whey
proteins-based films appear to have greater O2 permeability than
collagen, wheat gluten and soy protein isolate based films.80
However, modification of polymer structure combined with op-
timized plasticizer selection may affect the polymer free volume
and result in further reductions in O2 permeability.
C. Aroma Permeability
The food’s characteristic flavor and aroma are the result of
a complex construct of many individual constituent compounds
interacting to produce a recognizable taste and aroma. Thus, it is
important to preserve these aroma components from oxidation
 MILK PROTEINS FOR EDIBLE FILMS AND COATINGS 245

Table 2 Oxygen permeability of protein-based edible and synthetic films that variations in aroma permeability were due to a moisture
(adapted from Refs. 31, 46, and 80) plasticization effect and the considerable action of water vapor.
Test conditions O2 Permeability DeLassus112 pointed that the O2 barrier properties of poly-
Film (T, ◦ C; RH, %) (cm3 .µm/m2 .d.kPa) References mers are not directly correlated with their aroma barrier prop-
Collagen RTa ; 0 <0.04–0.5∗ 82
erties. Recent studies showed that the barrier properties of WPI
Gluten:Glyb (2.5:1) 23; 0 3.9 11 films, containing 25% Gly (dry basis), to d-limonene were com-
SPIc :Gly (2.4:1) 25; 0 6.1 146 parable to ethylene vinyl alcohol copolymer (EVOH) films, un-
β-Lgd : Gly (5.7:1) 23; - 20 142 der similar environmental conditions.113 In addition, permeabil-
β-Lg:Gly (2.3:1) 23; - 28 142 ity of WPI films to d-limonene was significantly dependent on
β-Lg:Gly (1.5:1) 23; - 75 142
NaCase :Sor f (2.3:1) 23; 50 3.2 80
temperature and relative humidity conditions but not on perme-
WPIg :Gly (5.7:1) 23; 50 18.5 80 ant concentrations.114
WPI:Gly (2.3:1) 23; 50 76.1 80
WPI:Gly (2.3:1) 23; 50 25 142
WPI:Gly (1.5:1) 23; 50 68 142
3.2. Mechanical Properties
WPI:Sor (1:1) 23; 50 8.3 80
WPI:Sor (2.3:1) 23; 50 4.3 80 The milk protein-based edible films have generally good ten-
WPI:Sor (3.5:1) 23; 40 0.7 80 sile strength (TS) and moderate elongation (E). The mechanical
WPI:Sor (3.5:1) 23; 50 2.6 80
properties of edible films are linked with the film-forming con-
WPI:Sor (3.5:1) 23; 70 43.3 80
WPI:BWh :Sor (3.5:1.8:1) 23; 50 11.6 80 ditions (type of process and process parameters), as well as ex-
LDPEi 23; 50 1870 147 perimental conditions. Plasticizers, lipids, cross-linking agents,
HDPE j 23; 50 427 147 anti-oxygen, antimicrobial, texture agents, etc. affect strongly
Cellophane 23; 50 16 145 mechanical properties. Plasticizers function by weakening in-
Cellophane 23; 95 252 145
termolecular forces between adjacent polymer chains, reducing
EVOHk (70%VOHl ) 23; 0 0.1 147
EVOH (70%VOH) 23; 95 12 147 tensile strength and increasing film flexibility.25 TS and E values
PVDCm —based films 23; 50 0.4–5.1 147 for a selection of milk-based edible and synthetic films are listed
Polyester 23; 50 15.6 148 in Table 3.
a Room temperature; b Glycerol; c Soy protein isolate; d β-lactoglobulin; e Sodium
Table 3 Mechanical properties of milk protein-based edible and synthetic
caseinate; f Sorbitol; g Whey protein isolate; h Beeswax; i Low density polyethy- films (adapted from Refs. 19 and 31)
lene; j High density polyethylene; k Ethylene vinyl alcohol; l Vinyl alcohol;
m Poly(vinylidene chloride). Tensile strength Elongation
∗ Based on values for PVDC-based films. Film (MPa) (%) References

UF-TMPa :Glyb (4:1) 10.0 5.2 40

and loss during storage and distribution. Effective control of the β-casein:Gly (2:1) 6–9 250 115
αs1-casein:Gly (49:1) 4.1 38 53
oxygen and aroma mass transfer across the packaging material
αs1-casein:Gly (49:1), Tgasec 10.6 77 53
can prevent undesirable off-flavor and sensory alteration during β-Lgd :Gly (2.6:1), Tgase 141.2 — 71
storage. NaCase :Gly (4:1) 17.4–26.7 10.5 19
The aroma barrier properties of a film are influenced by the NaCas:Gly (2:1) 2.98 29.9 62
external factors, such as temperature, humidity, light and phys- NaCas:PEG f (4:1) 10.9–16.35 5.3 19
NaCas:PEG f (4:1) 10.9-16.35 5.3 62
ical properties of the food. All these factors must be taken into
CaCasg :Gly (2:1) 4.25 1.4 62
account when determining the barrier property of a film. KCash :Gly (2:1) 2.97 42.8 62
The effectiveness of a polymer film as an aroma barrier can WPIi :Gly (2:1) 5.76 22.7 62
be described by its diffusion, permeability and solubility coeffi- WPI:Gly (2.3:1) 13.9 30.8 80
cients. Several polymer films as aroma barriers have been studied WPI:Gly (5.7:1) 29.1 4.1 80
WPI:Sor j (1:1) 14.7 8.7 80
to estimate the vapor aroma concentration and temperature effect
WPI:Sor (2.3:1) 14.0 1.6 80
over the diffusion, permeation and solubility coefficients.108 WPCk :Gly (2:1) 3.49 20.8 62
Published reports are scarce concerning the aroma transport NaCas:AMl :Gly (2:2:1) 1.32 27.4 62
properties of edible films. However, reviews of synthetic poly- CaCas:AM:Gly (2:2:1) 2.14 13.4 62
mer are relevant resources to the researcher studying the aroma KCas:AM:Gly (2:2:1) 1.66 17.7 62
WPI:AM:Gly (2:2:1) 3.14 10.8 62
barrier properties of edible films.109,110 Debeaufort and Voilley96
WPC:AM:Gly (2:2:1) 1.08 13.6 62
were the first to study the aroma permeability in edible films. LDPEm 13 500 147
They found that gluten (wheat protein) film was a better barrier HDPEn 26 300 147
to 1-octen-3-ol (mushroom aroma) than either the low density a Milk protein obtained by ultrafiltration; b Glycerol; c Transglutaminase;
polyethylene (LDPE) or methyl cellulose (MC) film at 35◦ C with d β-lactoglobulin; e Sodium caseinate; f Polyethylene glycol; g Calcium ca-
a saturated atmosphere of pure aroma compound corresponding seinate; h Potassium caseinate; i Whey protein isolate; j Sorbitol; k Whey protein
to a 0–5.68 µg/mL helium concentration differential, but not concentrate; l Acetylated monoglyceride; m Low density polyethylene; n High
as good as the cellophane film. Debeaufort et al.111 suggested density polyethylene.
246 K. KHWALDIA ET AL.
The β-casein films had higher TS and E than other casein
and caseinate films. The high TS and E of β-casein films may
indicate they are more resistant to damage during handling than
other casein- and caseinate-based films.115
Brault et al.50 have used γ -irradiation to produce cross-linked
caseinate films. Their work showed that the films had improved
mechanical properties. Irradiation of a solution based on Ca-
Cas produced more cross-links than a solution based on NaCas.
As a consequence, films based on CaCas showed a better me-
chanical strength. Addition of Gly has significantly increased
the formation of cross-links within caseinate chains, accounting
for the increase of the puncture strength. In addition, Gly acts
as a plasticizer, being responsible for the improved film exten-
sibility and viscoelasticity. Depending on the Gly/Cas ratio, the
irradiation treatment was beneficial for the toughness and the
flexibility of the films. Among the formulations investigated,
films obtained from the irradiation process exhibited the best
mechanical strength and flexibility at Gly/protein ratios of 0.5
and 0.67.
More recently, Lacroix et al.91 have used -irradiation and
thermal treatments to produce sterilized cross-linked films from
whey, casein and soya proteins. They pointed out that the me-
chanical properties of all the films were significantly increased
by inducing cross-links between protein chains. Films contain-
ing an equal WPI-Cas ratio (50-50) showed higher puncture
strength than pure CaCas-based films. This could be a result
of other favorable interactions than intermolecular bonding be-
tween WPI and CaCas.
A. Effect of Lipids
Shellhammer and Krochta103 studied the effect of lipid type
(anhydrous milkfat fractions, beeswax, carnauba wax and can-
delilla wax) and concentration on the mechanical properties of
whey protein emulsion films. They observed that film strength
and elastic modulus decreased with increasing lipid concentra-
tion. The carnauba wax emulsion films were the strongest at each
lipid level, while the candelilla wax emulsions were weakest.
In bilayer films, the lipid layer possesses really poor mechani-
cal resistance, whereas a lipid-hydrocolloid emulsion-based film
exhibits good mechanical resistance.116 McHugh and Krochta39
and Debeaufort and Voilley117 observed that the stability of the
emulsion significantly influence the mechanical properties of
emulsified films.
B. Effect of pH
Frinault et al.118 developed an alternative procedure for con-
tinuous casein film production based on a modified wet spinning
process.119 They determined the influence of film-forming pH
solutions on functional characteristics and ultrastructure of the
films. The optimal film was obtained at pH 9.0 and showed
highest TS (4.5 MPa), highest percentage elongation at break
(68.6%), low solubility in water and lowest WVP values (3.9
10−10 g.m−1 .s−1 .Pa−1 ).
Anker et al.120,121 have studied the mechanical properties and
glass transition temperature of WPI films at various pH values
using Sor as a plasticizer. The films were cast from heated aque-
ous solutions and dried in a climate chamber at 23◦ C and 50%
RH for 16 hours. The films’ mechanical properties (elongation,
young’s modulus, stress at break) showed different behavior at
pH 7 and 8 compared to that at pH 9. This could be due to alkali-
induced chemical changes in the polymer matrix at higher pH
values.
C. Effect of Additives
Blocking the free sulhydryls in WPI films with N-
ethylmaleimide had an effect on Young modulus, yield stress
and breaking stress.122 N-ethylmaleimide addition makes the
WPI films less extensible, due to change in protein conforma-
tion and increased hydrogen bonding.
Arvanitoyannis et al.123 prepared blends of NaCas and
starches (corn and wheat) plasticized with water, Gly or sugars,
in order to study mechanical, thermal, and barrier properties.
An increase in plasticizer content resulted in a considerable de-
crease in the elasticity modulus and in the TS of films. NaCas
was preferred over casein because of its higher water uptake.
The plasticizing effect of several molecules on NaCas could be
ordered as follows: glycerol < sorbitol < xylose < sucrose.
Somanathan124 used acrylonitrile (AN) and n-butyl methacry-
late (n-BMA) grafted onto casein to modify the mechanical be-
havior. The physical properties of polymers are governed by
several variables such as temperature, rate of plasticization, and
molecular weight. The stress-strain properties of polymer sen-
sitive to temperature and TS decrease with the increase of tem-
perature. When the strain rate increases, the TS and modulus
increase, whereas the breaking strain shows an inverse relation-
ship. Stress-strain behavior of casein grafted with AN, is strongly
influenced by temperature and strain rate. Due to the incorpora-
tion of n-BMA, the material becomes flexible. The mechanical
properties of casein grafted with a binary mixture of monomers
clearly show the inverse ratio between temperature and strain
rate effect in the experimental range.
3.3. Sensory Properties
Since an edible film becomes a part of the food product and
is consumed with its contents, sensory attributes of edible films
are very important in determining the acceptability of a food
product and wether these films interfere with the food products
taste, aroma, and texture.
Films primarily composed of milk proteins have suitable
overall optical properties.107,125 They vary from transparent to
translucent, which enlarge the potential attractive benefits and
applications in food and non food commodities.11 Transparency
is the property of a material that allows one to see through it.
According to Hernandez,126 the transparency of a polymer de-
pends on its morphology rather than the chemical structure or
molecular mass of the material.
 MILK PROTEINS FOR EDIBLE FILMS AND COATINGS 247

Generally, milk protein-based edible films are flavorless, ing increases their perishability by causing cellular disruption,
tasteless and flexible.13,127 However, in the case of WPC (whey increased respiration, increased ethylene production, and syn-
protein products), certain off-flavors, mainly stemming from thesis of secondary metabolites.130,131
lipid oxidation, Maillard reaction products and degradation of Use of edible coating to minimize the deleterious effects
vitamins, could be developed during storage, affecting the prod- of minimal processing has been reported for several comm-
uct quality and acceptability.128 odities.132 They can provide partial barriers to moisture and gas
Kim and Ustunol129 have studied the sensory attributes of exchange (CO2 and O2 )16,130,132,133 and could lead to a reduction
whey protein isolateWPI/candelilla wax emulsion films (trans- in the spoilage of the fruits and vegetables which is estimated
parency, milk odor, sweetness, and adhesiveness), using a trained from 25 to 80%.134
sensory panel. The films had no distinctive milk odor; however, Research by Krochta et al.51 indicated that edible coatings
they were perceived to be slightly sweet and adhesive by the made from milk protein and vegetable oil derivates substantially
trained sensory panel. Whey protein isolate films WPI films reduced moisture loss and oxidative browning in apple slices.
without candelilla wax were clear and transparent, whereas can- Avena-Bustillos et al.135 found that NaCas and stearic acid
delilla wax containing films were opaque. emulsion coatings improved the storage stability and reduced
water loss of peeled carrots. The use of sucrose esters of fatty
acids, mono-and diglycerides allowed the increase of water va-
4. POTENTIAL FOOD APPLICATIONS por resistance (up to 75%) in zucchini fruit.136
OF MILK PROTEIN PACKAGING Brault et al.50 reported that cross-linked caseinate films, pro-
duced by γ -irradiation, have reduced considerably the water
The main concepts of using the edible films and coatings are loss for strawberries during the storage and have delayed the
extending food shelf life, improvement food quality, addition the browning of potatoes and apples.
value of natural polymer material and also reduce the synthetic
packaging materials. Many processing procedures had been used B. Frozen Foods
to form edible coating and films, such as dipping, spraying,
Many types of coating materials have been tested in attempts
foaming, fluidization, enrobing, casting and extrusion. All of
to maintain quality of frozen foods, such as ice glazing, car-
them could be employed for the milk protein films.
rageenans, alginates and acetylated monoglycerides. Such coat-
Milk proteins have received attention in edible films and coat-
ings had limited success and acceptance.137,138
ings area because they provide the potential to control transfer
Addition of lipid substances to proteins to form emulsion
of moisture, oxygen, aroma, oil, and flavor compounds in food
films provides effective protection against moisture loss. Casein
system depending on the nature of edible film-forming materi-
and acetylated monoglycerides emulsion coatings were used on
als. Table 4 summarizes some food applications of milk protein
frozen salmon pieces which were stored at −10◦ C, and reduced
films and coatings.
moisture loss when compared to uncoated salmon.138 Stuchell
and Krochta139 displayed an efficient protection of salmon
4.1. Moisture Barrier Applications against lipid oxidation and water loss by a coating of a mix-
ture of WPI and acetylated monoglycerides.
A. Fresh Fruits and Vegetables
4.2. Gas Barrier Applications
Recently, there has been a surge of interest in conveniently
packaged fresh produce. Sales of “fresh cuts” include, for the
A. Fresh Fruits and Vegetables
most part, minimally processed fruits and vegetables. Since
these products are still metabolically active, minimal process- McHugh and Krochta48 showed that milk proteins are good
gas barriers at low to moderate RH. RH also has an exponential
Table 4 Food applications of milk protein films and coatings effect on the O2 permeability of WPI film.80 Thus, WPI-based
Foods Functions Milk protein References film coatings have potential for use in food system to provide pro-
tection against O2 when the storage RH is intermediate or low.
Zucchini Moisture barrier Casein-AMa 136
Edible coating on fruits could serve either as gas or moisture bar-
Apples and celery sticks Moisture barrier Casein-AM 136
Banana fruit Reduce ripening rate WPIb 149 riers. They could help to lessen moisture loss, and or reduce fruit
Frozen salmon Reduce moisture loss Caseinate-AM 139 O2 uptake from the environment and then slow respiration.140
Reduce rancidity WPI-AM 138
Dried chicken dice Reduce mechanical loss WPI 150
B. Appetizers
Breakfast cereal Moisture barrier WPI 69
Peanut Reduce rancidity WPI 141, 142 Peanuts are susceptible to lipid oxidation, which depends on
Walnut Reduce rancidity WPI 151
O2 concentration during storage, causing rancidity. Mate and
Flavor (d-limonene) Aroma barrier WPI 107, 114
Krochta141 coated peanuts by dipping them into an increased-
a Acetylated monoglyceride; b Whey protein isolate. viscosity WPI solution followed by air-drying. They showed
248 K. KHWALDIA ET AL.
that WPI-based edible coatings are good O2 barriers on the nut
surface and could delay considerably O2 uptake of dry-roasted
peanuts at intermediate (53%) and low (21%) storage RH. To
evaluate how WPI-based edible coatings affect the development
of rancidity, Mate et al.142 used different standard methods, such
as peroxide values and static headspace gas chromatography.
C. Frozen Foods
A spray of WPI solution followed by an antioxidant spray
delayed lipid oxidation and reduced peroxide values in stored
frozen king salmon.139 No effect on peroxide values or moisture
loss was found for the WPI solution spray alone or with WPI-
acetylated monoglycerides emulsion spray.
4.3. Aroma Barrier Applications
Edible films can be employed as flavor carriers in addition
to provide a protection to aroma loss.3 The sorption ability of
edible coating may allow the flavor and aroma incorporation
into a coating for delayed release in order to improve the flavor
profile of the food. Flavor and aroma could be released in the
mouth by mastication or during the intermediate steps of food
preparation (heating, rehydration).
Milk protein edible films could integrate flavor and aroma
enhancers and also nutritional substances. Films obtained from
irradiated CaCas-solutions might be used as microencapsulating
agents of flavors in coating of fruits, vegetables, and cheese, as
well as in food packaging.50
Metzger143 developed a method for producing a casein bio-
degradable film, as planar or tubular films. Since they were es-
pecially advantageous because of their great strength and biode-
gradability, showing a good ability for packaging aromatic dry
powder, such as tea, coffee and spices.
5. CONCLUSIONS
This study has demonstrated a number of characteristics of
milk proteins that make them suitable for the formation of differ-
ent films and coatings. Milk proteins-based films and coatings
are very promising systems for the future improvement of food
quality and preservation during processes and storage. They of-
fer numerous advantages over other conventional synthetic pack-
aging materials. Their inherent edibility and biodegradability
are strong advantages of these edible films and coatings. In ad-
dition to their environmentally friendly nature, increased food
safety can be achieved by incorporating active agents into the
films/coatings. Resarch is still necessary to increase understand-
ing of film composition-structure-function relations and thus
enable food applications. In addition, new legislations and stan-
dards in favor of edible materials seem to be very helpful to spur
the market growth.
The thrust for future work is to develop milk protein coating
on paper/paperboard or plastic. Milk-protein-coated paper will
be fully compostible. Milk protein coating on plastic has the
advantage of being easily removed for recycling of the plastic.
Milk protein coating can provide not only better physical perfor-
mance of packaging materials and prolonged shelf-life of foods,
but also reduce solid waste and improve plastic recycling.
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