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Functionality of protein-Based edible coating- review

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 Journal of Entomology and Zoology Studies 2020; 8(4): 1432-1440

E-ISSN: 2320-7078
P-ISSN: 2349-6800
www.entomoljournal.com
Functionality of protein-Based edible coating-
JEZS 2020; 8(4): 1432-1440
© 2020 JEZS
review
Received: 08-05-2020
Accepted: 10-06-2020
Hauzoukim, Sagarika Swain, Biswajit Mohanty
Hauzoukim
School of Fisheries, Centurion
University of Technology and
Abstract
Management, Odisha, India Consumer demand for convenience package and consumption, safe microbiologically, longer product
shelf-life and effect of packaging material on environment is forcing food processor and researcher to
Sagarika Swain develop new technique in food processing, cooking, handling, and packaging strategies. Most of ready-
School of Fisheries, Centurion to- eat foods are exposed to post-process contamination, leading to spoilage and reduced shelf-life.
University of Technology and Biopolymers extracted from biomass, synthesized from bio-derived monomers or produced directly by
Management, Odisha, India microorganisms with the advantages of biodegradability, process ability, no pollution to food, abundant
and renewable have become the leading food packaging materials. Furthermore, the raw materials to
Biswajit Mohanty produce biopolymers are low-cost, some coming even from by-product of agriculture and fish processing
School of Fisheries, Centurion waste. Proteins-based edible films can be incorporated into foods to impart nutritive value and functional
University of Technology and properties. The materials to develop protein-based coatings and packaging films can be divided into two
Management, Odisha, India
classes: plant proteins and animal proteins. Proteins referred in this review are broadly classified under
cereal, milk, oilseeds, collagen and gelatin based. Proteins-based edible coating has excellent gas barrier
properties and good mechanical properties. However, the hydrophilicity nature of proteins makes the
protein-based films poor water barrier properties. The application of plasticizers and treatments can
improve the protein-based films and coatings. The addition of physical and chemical active compounds
into protein-based films can increase the functional properties which can inhibit or delay the growth of
microorganisms and the oxidation of lipids thereby increase its shelf-life. The review summarized the
advances and research about the functional properties protein-based films and coatings in food packaging
with examples.

Keywords: Protein-based films and coatings; functionality; plasticizers; applications in food

Introduction
Consumers demand for high quality foods with enhanced keeping quality of raw and Ready-
to-Eat foods with minimal changes in nutritional and sensory properties. Food processor and
researcher are exploring an alternative or novel processing technologies to provide safe,
fresher-tasting, nutritive foods without undesirable changes in food due to processing [1, 2]. Use
of edible coatings to preserve food is not a new concept but have gain interest in recent times
due to their protective functions. It will minimize the concern over disposal of packaging
materials; reduce utilization of synthetic material [3, 4] and use of under-utilized agriculture
products for edible film forming [5, 6, 7, 8]. The choice of packaging material will varies
according to the specific food and major contributing factor for quality deterioration [9, 4]. The
edible coatings can simplify the total packaging structure [5, 3].

Background of Edible coating

An edible film can be defined as a thin layer used to coat food or act as a barrier between the
food and the environment [10]. The first free-standing edible film “Yuba” was developed during
the 15th century in Japan from soymilk and was used for food preservation [11, 12]. Edible films
can be prepared from proteins, polysaccharides, and lipids. Edible coatings derived from
proteins, lipids and polysaccharides have solute, gas, and vapor barriers functioning properties.
During the 12th century, the Chinese applied waxes on oranges and lemons to retard water loss
[13, 14, 15]
. Coating of foods with fat also known as ‘larding’ was used in England in 16th century
Corresponding Author:
to test their moisture barrier property [16]. Since the 1930s, hot melted paraffin waxes use to
Hauzoukim coat citrus fruits in the United States, and carnauba wax and oil-in-water emulsions to coat
School of Fisheries, Centurion fresh fruits and vegetables since the 1950s [17, 18, 19]. [20] Reported that edible films can extend
University of Technology and shelf life of fresh fruits by delaying moisture loss. Edible coatings have wide application as
Management, Odisha, India casing for sausages and chocolate coatings for nuts and fruits which
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do not require to be removed before consumption. Edible biological deterioration [34]. It can improve the physical
films mechanically protect foods by preventing the strength of the food products, reduce particle aggregation,
contamination from microorganism; prevent quality loss due and improve appearance [35, 36].
to mass transfer (e.g. gases, moisture, flavours, etc.). Edible 2. Prevention of moisture loss during storage of fresh or
films becomes a vehicle for incorporating natural or chemical frozen foods as edible coatings have a good moisture
antioxidants, antimicrobial agents, enzymes, other functional barrier properties which prevent weight loss due to
ingredients such as minerals, probiotics and vitamins [21, 8]. moisture evaporation. In other case application of edible
This review will discuss the rationale use of protein base coatings can prevent formation of juices on the package
edible coatings on fruits, vegetables, meats, poultry, and sea when fresh meat, poultry, fish cuts are packaged in retail
foods and summarizes research findings on the effectiveness plastic trays, which are unattractive to the consumers.
of and the problems associated with various types of coatings. While preserving the food, the production cost could also
be reduced as no extra moisture absorbent is required. [34,
37, 38, 3, 39]
Film-forming techniques .
Different techniques are used for film forming depends on the 3. Use of edible coatings of low oxygen permeability helps
different material or substances used. Some of which require to reduce the rate of rancidity and brown discoloration in
solvent extraction, thermal gelation, and solidification of melt meats but creating an anaerobic conditions should be
have been developed for forming edible films. avoided [34, 38].
A. Hydrocolloid edible films are produced solvent 4. Pre-heated edible coating solutions just before
extraction, a continuous structure is produced. The application could reduce the amount of spoilage and
physical and chemical interactions between molecules pathogenic microorganisms and partially inactivate
help to stabilize the product. Solvents used are water, deteriorative proteolytic enzymes at the surface of coated
ethanol, or acetic acid which contains additives such as foods [34].
plasticizers, cross-linking agents, solutes, etc. 5. Edible coatings could prevent loss of colour, volatile
B. In protein films the solution is heated denaturation, flavour and prevent pick-up of foreign odour in foods [37,
38, 3, 39]
gelification, or precipitation followed by rapid cooling .
produce gelation and coagulation [22]. 6. When edible coatings added with antioxidants or
C. Lipid based films are melted and solidified [23]. antimicrobials helps to delaying meat rancidity and
discoloration, and reducing microbial loads [37, 38, 3, 39].
Plasticizers added with biopolymers are used for protein 7. Edible coatings when applied on the surface of food
based edible films to modify and increase its functionality of before battering in a battered and breaded product reduce
the edible films. Plasticizers inclusion will decrease protein oil uptake during frying and loss of moisture thereby
interactions while increasing both the polymer chain mobility improving the products’ nutritional value [40].
and intermolecular spacing [24]. The biopolymers added help in 8. The greatest benefits of edible film and coating materials
film-forming mechanisms by intermolecular forces such as are their biodegradable and edibility nature [30, 5].
covalent bonds (disulfide bonds) cross linking, hydrophobic, 9. Carrier of bioactive compounds- Enrobing acts as a
electrostatic, or ionic interactions. One important factor in the carrier for various synthetic or natural antimicrobial and
film forming mechanism is to control the fabrication process antioxidant substances [41, 42, 43, 44, 45]. Reported that when
conditions, should be suitable for food process (pH added butylated hydroxytoluene and butylated
modification, salt addition, use food grade solvent, drying, hydroxyanisole in enrobed pork patties, it help to extend
enzyme modification, heating or reaction with other shelf life of enrobed pork patties.
chemicals). If not controlled, alteration of the kinetics and
reaction mechanisms may occur 25, 26]. The type and Classification of edible films:
concentration of plasticizer influences the properties of Edible films mainly classified under three major categories
protein films [27, 28]. Film additives are mostly small molecules viz. proteins, polysaccharides, and lipids.
having low molecular weight and high boiling point 1. Proteins based- wheat, gluten, collagen, corn zein, soy,
compatible with the polymers [29]. Plasticizers increase casein, and whey protein [34].
extensibility and decrease the brittleness of the film which is 2. Polysaccharide based - Alginate, dextrin, pectin, and
an important characteristic of the packaging applications. cellulose derivatives [34].
Some of the food grade plasticizers are sucrose, sorbitol, 3. Lipids-waxes, acylglycerols, and fatty acids (Debeaufort
mannitol, glycerol, polyethylene glycol etc. Water also and Voilley, 1995; Park et al., 1995) [46, 47].
improves protein films [30] but film properties are affected by 4. Composite films – made by combining both lipid and
moisture. Common covalent cross-linking agents such as hydrocolloid components [29].
glutaraldehyde, calcium chloride, tannic acid, and lactic acid
are used to improve water resistance, cohesiveness, rigidity, Proteins based edible coating
mechanical strength, and barrier properties [31, 32, 33]. Edible films from animal and plant proteins, such as wheat,
gluten, collagen, corn zein, soy, casein, and whey protein and
The benefits of using Edible Coatings on foods their properties and formation was of recent interest due to
(Vegetables, Fruits, Meat, Poultry and Seafood) their numerous functional properties [48, 34]. Functional
Edible coatings are use for their functional properties in order properties can be defined as ‘‘those physical and chemical
to meet challenges related with nutritious, stable, and high properties that influence the behaviour of proteins in food
quality foods for a better economic and marketing safe. Some systems during processing, storage, cooking and
of the benefits are discussed below consumption’’ [49, 50]. stated that ‘‘the physico-chemical
1. Edible films and coatings enhance the quality of food properties that influence functional behaviour of proteins in
products, protecting them from physical, chemical, and food include their size, shape, amino acid composition and
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Journal of Entomology and Zoology Studies http://www.entomoljournal.com

sequence, net charge, charge distribution, hydrophobicity, chops reduce lipid oxidation (significantly lower
hydrophilicity, structures (secondary, tertiary and quaternary), thiobarbitouric acid values) but have poor moisture barrier
molecular flexibility/ rigidity in response to external properties after storage at 4°C for 6 and 9 days [71]. Precooked
environment (pH, temperature, salt concentration), or beef patties coated with wheat gluten reduce the moisture loss
interaction with other food constituents’’ [51]. Reported that during a refrigerated storage [72]. Corn-zein applied to apples
edible protein coatings provided a method of extending and pears, shows different in the respiration rate where the
postharvest storage of fruits and vegetables. Protein films are respiration rate of the former is decreased, but the opposite in
hydrophillic in nature possessing poor water vapor barrier pear. However, the weight losses of both the fruits are delayed
property [52], but exhibit better oxygen, carbon dioxide barrier [47]
. Zein coating incorporating with polymeric chelator
properties and mechanical properties than polysaccharide extends fish ball shelf life at refrigerated condition, 4 °C to
films [24]. The poor water vapour permeability can also be 19 days [73].
improved by the incorporation of hydrophobic materials such
as lipids [53] but the incorporation of lipid materials could 2. Milk protein
adversely affect the sensory characteristics of films. WPI and Whey is a by-product during cheese manufacturing, rich in
mesquite gum (MG) are showed compatible when cysteine, methionine and sulfur-containing amino acids.
incorporated with antimicrobial agents [54]. The high water Whey-based films prepared from whey protein concentrates
vapour transmission rate can also be overcome by the addition (WPC) and isolates (WPI) have a protein content of 90% and
of plasticizers. Some protein are insoluble in water but are 50–80% respectively [74]. The film forming ability of whey
dissolve using a plasticizer or solvents whereas the proteins based film depends on the thermal denaturation of whey
soluble in water produce coatings of varying solubility protein in an aqueous solution. The three-dimensional
depending on the protein type and source and the conditions structure of whey protein is modified by heating which
of treatment and coating formation. The concentration, exposed the internal hydrophobic and SH groups having the
composition, size, and shape of plasticizers all affect the hydrophobic and intermolecular S–S bonding interactions
properties of protein films [55, 56, 57, 58, 59, 60]. Studied about the promoted upon drying [75, 76].When the pH of film-forming
good oxygen barrier properties in low relative humidity solution in WPC is adjusted to 6.6 and heating temperature to
environments of edible films from collagen, wheat gluten, 75oC, an uniform film was obtained [77]. Ultraviolet (UV)
corn zein, soy protein, and whey protein. While coating raw radiation and ultrasounds (US) can also improve the
meat, poultry or seafood, the protein-based edible coatings are properties of the whey-based films. The whey-based films
susceptibility to proteolytic enzymes present in the foods. made with plasticizers are flexible, Whey proteins have poor
Labelling of the food coated with protein based is important moisture barrier due to hydrophilic nature but produces films
due to some individuals allergic to protein fractions of milk, flexible, transparent, and flavourless when a plasticizer is
egg white, peanuts, soybeans etc. or other adverse effect to added [78, 79]. Lipid materials like fats and oils could increase
the individuals. Some individuals are gluten intolerance due the hydrophobicity of whey-based films and improve the poor
its gliadin fraction in particular, known as celiac disease or moisture barriers properties. The lipid materials can be from
gluten-sensitive enteropathy or non-tropical sprue [48]. Some plant oils [80, 81, 82, 83, 84, 85], fatty acids [86] and acetylated
individuals show lactose intolerance due to deficient in lactase monoglycerides [87]. Treatment with UV radiation and
[61]
. alkalization e.g., 7 or 9 to the WPC film-forming solutions,
the film become strong, puncture resistance of the films is
1. Cereal Protein improved. Studies of whey protein based coatings on common
Film formation from corn zein, the prolamin fraction of corn breakfast like raisins, cereals, cheese pieces and frozen peas,
proteins, and from wheat gluten, a mixture of the prolamin and on peanuts for its oxygen barriers properties. Whey
and glutelin fractions of wheat proteins, has been studied protein or whey protein with carbohydrate was used to
extensively [37]. Gluten films have good oxygen isolation microencapsulate food additives [71]. Edible coating prepared
performance with resistance to water vapor and mechanical from whey protein isolate with ascorbic acid and citric acid as
properties [3]. Addition of nonpolar hydrophobic substance an antioxidant were spray on King salmon, the edible coating
like mineral oil in the film can reduce 25% of water vapor does not have affect moisture loss rate but shows a delayed on
permeability when compared to the control group [62]. the onset of lipid oxidation and reduced peroxide values in
Thermal treatment can improve the mechanical properties of frozen [88, 89]. Reports frozen King salmon coated with whey
the gluten-based films for the casting films that were obtained protein powder shows 42–65% reduced in moisture loss and a
through covalent crosslinking of gliadin polypeptide [63, 64]. delayed in lipid oxidation. Whey protein with acetylated
Wheat gluten on eggshells improved shell strength, reduced monoglycerides on nuts show delayed in rancidity [90, 91, 92].
microbial contamination [65]. Recent studies have evaluated Whey protein, whey protein isolate (WPI), wheat gluten
properties of films from sorghum kafirin and rice bran protein (WG) on eggshells improved the shell strength, greater
[66]
. A composite of gluten and SPI (soy protein isolate) can puncture strength and reduced microbial contamination than
reduce fat deterioration in peanuts [67]. Zein is a by-product those of non-coated eggs [65]. Addition of sodium dodecyl
during corn processing constitute about 45–50% of corn sulfate (SDS) to soy protein isolate increase the extendibility
proteins [68, 69]. Mentioned that corn zein has been used in of the films substantially while simultaneously improved the
commercial coating formulations for shelled nuts, candy, and moisture barrier properties [93, 94]. The addition of cysteine
pharmaceutical tablets. The use of corn zein as an edible increases the film tensile strength. Irradiation and heat curing
coating or packaging film for cooked meat and poultry has after the film formation improve the soy protein films
recently been suggested. Tomatoes coated with corn‐zein performance due to the bityrosine formed between two
(CZ) protein film delayed in ripening without adverse effects. protein chains through irradiation which increase its
Tomatoes delayed color development, loss of firmness, and mechanical properties. Heat curing increase the tensile
weight loss [70]. Corn zein when coated on precooked pork strength from 8.2 to 14.7 MPa but the film elongation
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Journal of Entomology and Zoology Studies http://www.entomoljournal.com

decreased from 30% to 6% [95]. Thermal treatment with 60% on dry weight basis. The antinutritional factors (phytic
irradiation improves the mechanical properties of soy protein acid, trypsin inhibitors and tannins) and low protein solubility
films [96]. Precooked beef patties coated with soy protein present in meals could limit its application. The application of
reduced moisture loss compared to unpackaged patties after 3 aqueous processing, with or without enzymes hydrolysing the
days of refrigerated storage. ‘‘Fuji’’ and ‘‘Golden 95 structural polysaccharides of the cell wall to enhance the
delicious’’ variety of apples coated with soy protein improves extraction of oil will also improve the nutritional and
the quality by delayed the changes in firmness, colour, and functional properties of the protein [130, 131, 132, 133]. Egg
acidity [97]. Lactoperoxidase system (LPOS)-Whey protein albumen and soy protein isolate mixture was use to stabilized
treated on rainbow trout fillet shows antimicrobial activities dehydrated meat as describe by (Khan et al., 1993). Meat
by reducing total specific spoilage organisms (Shewanella flavour was retained when soy protein as microencapsulating
putrefaciens and Pseudomonas fluorescens) and extended the medium was use as coating while the product had good
shelf-life from 12 days to 16 days on refrigerated storage [98]. texture and rehydration characteristics (Torres, 1994).
[99]
Reported that the use of ultrasound-treated whey protein
coatings on frozen Atlantic salmon delayed lipid oxidation. 4. Collagen
Casein contains four main subunits: kappa-casein, beta- Unilever developed a more advanced technology where the
casein, alpha s1-casein and alpha s2-casein that make up 13%, collagen casing is co-extruded around the sausage meat batter
[12]
36%, 38% and 10% of the casein composition respectively . It is continuous and better controlled compared to
[100, 101]
. Without further processing, casein can form films conventional batch process where meat batter is stuffed into
easily from aqueous solutions because of the strong inter- pre-formed casings. Furthermore, use of proteins other than
chain cohesion caused by their random-coil nature and a great collagen, such as wheat gluten, corn zein, soy protein, peanut
number of formed intermolecular hydrogen, hydrophobic and protein, and feather keratin, in manufacturing of sausage
electrostatic bonds [102]. Caseins are easily water soluble, good casings has been suggested [134]. Jones and Whitmore mixed
emulsification properties, high nutritional value and easily ground collagen with aqueous mixture of lactic acid and
availability makes caseins desirable biomaterials for the glyceraldehydes setting pH 7, heated at about 75°C and coat
preparation of edible films [103, 104, 105, 106, 107]. Caseins are more on hamburgers which can withstand a cooking temperature.
insoluble as compare to other protein which makes caseinate Collagen casings for sausage prepared from the regenerated
(mainly sodium caseinate) an alternative to traditional corium layer of food-grade beef hides [48]. An edible collagen
packaging materials. Although casein has many advantages film “Coffi” can reduce cook shrink, increase product
there are defects that need to be improved. The interactive juiciness, when coated on boneless hams, fish fillets, roast
forces between non-polar and polar amino acid in the beef, and meat pastes [135]. Beef steaks wrapped in Coffi
structure of casein causes shrinkage during the drying process collagen film both refrigerated and frozen/thawed exhibited
and then become brittle which can be overcome by the significantly less fluid exudate than unwrapped controls. The
addition of plasticizers like sorbitol or glycerol [108]. The thiobarbituric acid, color analysis and sensory results shows
mechanical properties and elasticity can be improved by the the collagen films had no significant effect on meat oxidation
modification of the polymer network through physical and and color [59], Collagen used as casings for sausages, as
chemical treatments can make the films functionality be studied by [12].
improved [104, 109]. Some of the agents applied to improve the
quality are transglutaminase [110, 111], glutaraldehyde [112], 5. Gelatin
genipin [113, 114, 111], tannic acid [115] and wax [106] are used as Gelatin is protein based polymer obtained from animal skin,
crosslinkers or by combination with polysaccharides [116, 117] bones, connective tissue and fish skin after partial hydrolysis
or lipid [108, 118, 110], pH alteration [120], photo-induced of collagen. In the hydrolysis process, the raw animal material
polymerization [121], pulsed light [122]. Lactic acid–treated is treated with dilute acid or alkali and results in partial
casein with sorbic acid is tested on papaya cubes inoculated cleavage of the cross-links where the structure is broken down
with Staphylococcus rouxii, Aspergillus. niger. After 30days to ‘‘warm-water-soluble collagen’’, i.e. gelatin [136].
of storage 30% of the sorbic acid was retained and there is no Preservations of meat and other food using coating of gelatin
growth of both the test organisms. A complete diffusion of films were proposed by [137, 138].
sorbic acid is sorbic acid is observed within 24 hrs if not Gelatin is mainly use for microencapsulation of ingredients
treated with casein. This shows that the edible film matrix and coatings for tablet and capsule [48]. Gelatin is readily
helps to entrap the antimicrobial properties and reduced the soluble in water at temperatures above 40ºC, which destroys
diffusion during storage studies [123]. Casein when applied to the triple helical structure of collagen forming a viscous
peeled carrots helps reduced dehydration and white blush solution of random-coiled linear polypeptide chains. At about
formation [124, 125] and when casein with acetylated 20ºC, gelatin formed a collagen like helices but short
monoglycerides used to coat celery sticks reduced including only part of the material which forms a gel. Higher
dehydration [126]. Sodium caseinate film reduced oxygen and amino acid content in mammalian gelatin gives the advantage
carbon dioxide permeation when treating green bell peppers of better physical properties and thermostability than fish
[97]
. gelatin. Its film forming ability directly relates to its
molecular weight. Molecular weight distribution and amino
3. Oilseed proteins acid composition of gelatin defines its physical properties i.e.,
Importance of protein structure in relation to the functional the higher the average molecular weight, the better the quality
properties was reported by [127, 128]) study the functionality of of the film. The quality of the gelatin film depends mainly on
proteinic products by modification of protein. The amount of the degree of collagen cross-linking and the extraction
water and proteins interaction is related with its amino acids procedure [139]. [70], reported that when sprayed turkey steaks
profile and increases with the number of charged residues [129] with an aqueous gelatin suspension with various antioxidants
Protein content from dehulled oilseeds ranges from 35% and results in less lipid oxidation (lower peroxide values by 60–
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Journal of Entomology and Zoology Studies http://www.entomoljournal.com

90%) in the skin and meat fat compared with uncoated and biodegrade. Study on the relations between the function,
controls during frozen storage at –12°C for 6 months. This structure and composition of protein-based films will give
shows gelatin have shown potential as carriers of information on the methods and film modification required so
antioxidants. [140, 141], reported that gelatin from marine sources that the protein-based films is suitable for food packaging to
(warm- and cold-water fish skins, bones, and fins) can be increase its functional properties. Active packaging is
alternative to bovine gelatin as it is free of the risk of promising for the rapid development of the functional food
outbreaks of Bovine Spongiform Encephalopathy and also market. The active properties i.e. antioxidant and
religious sentiments [142]. Fish gelatin gives a better utilization antimicrobial properties of protein-based films selected based
as by-product of the fish-processing industry waste and on the food characteristics and storage requirements, can
providing a valuable source of gelatin [143]. The collagen electively inhibit or delay the growth of microorganisms and
content in the fish skin waste of Japanese sea-bass, chub the oxidation of lipids thereby ensuring food safety and
mackerel, bullhead shark were found to be 51.4%, 49.8% and prolonging the shelf life of food.
50.1% (dry basis) respectively as reported by [144, 145].
Reported that Alaska pollock gelatin can be used up to 10 Acknowledgement
g/kg without a negative effect on the mechanical properties of I would like to acknowledge the co-authors for their support
surimi. It was found that with increase in the level of fish and contribution in writing this review paper.
gelatin, the breaking force and deformation of surimi gel
decreased (p˂0.05). However, there was an increase in References
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