Food Packaging and Shelf Life 34 (2022) 100945

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Food Packaging and Shelf Life

journal homepage: www.elsevier.com/locate/fpsl

A comprehensive review on gelatin: Understanding impact of the sources,

extraction methods, and modifications on potential packaging applications
Jahangir A. Rather a, Najmeenah Akhter a, Qazi Showkat Ashraf a, Shabir A. Mir b, Hilal
A. Makroo a, *, Darakshan Majid a, *, Francisco J. Barba c, *, Amin Mousavi Khaneghah d, *, B.
N. Dar a, *
a
Department of Food Technology, Islamic University of Science and Technology, Awantipora, Jammu and Kashmir, India
b
Department of Food Science & Technology, Government College for Women, M. A. Road, Srinagar, Jammu, and Kashmir, India
c
Nutrition and Food Science Area, Preventive Medicine and Public Health, Food Science, Toxicology and Forensic Medicine Department, Faculty of Pharmacy, Universitat
de València, Avda. Vicent Andrés Estellés, s/n, 46100 Burjassot, Spain
d
Department of Fruit and Vegetable Product Technology, Prof. Wacław Dąbrowski Institute of Agricultural and Food Biotechnology – State Research Institute, 36
Rakowiecka St., 02-532 Warsaw, Poland

A R T I C L E I N F O A B S T R A C T

Keywords: Gelatin is one of the most widely used hydrocolloids; mammalian, poultry, and fish wastes are an exciting source
Gelatin for gelatin production. The market size of gelatin will reach 5.0 billion USD by 2025 due to the consumption
Chemistry perspective of gelatin in today’s market. The gelatin market is predicted to reach 6.7 billion USD at the end of
Sources
2027 with a 9.29 CAGR rate, being a vital constituent of the food, pharmaceutical, cosmetic, and packaging
Modifications
industries owing to its foaming, emulsifying, gelling, and filmogenic properties. In the packaging sector, gelatin-
Packaging applications
Halal based films and coatings are gaining importance owing to their eco-friendly nature. The gelatin source, amino
acid composition, and extraction method play a prominent role in its packaging properties. In order to improve
the packaging properties of gelatin further, physical, chemical, enzymatic, and irradiation-based modifications
play an significant role. This paper reviews the impact of sources, extraction, and gelatin modifications on im­
provements of gelatin as packaging material, and provides detailed information on gelatin films/coatings in the
shelf-life extension of food products.

1. Introduction gelatin production (Alipal et al., 2021). Although pig skin is the most
frequently used raw material for producing gelatin on a commercial
Gelatin is a polymeric substance and a multi-functional ingredient scale, the alternative raw material from fish, animals, or birds slaugh­
obtained by the limited hydrolysis/heat denaturation of skin, bones, and tered by the halal method can be utilized, eliminating the religious
connective tissue collagen (Alipal et al., 2021). Gelatin contains 19 apprehension about the halal method the Muslim and Jewish populace.
amino acids, glycine (27–35%), proline, and hydroxyproline (20–24%) Not only religious objections, but there are also still other concerns
being the predominant amino acids (Nurilmala et al., 2021). The gelatin regarding the use of bovine, porcine skin, and bone gelatin due to BSE
composition plays an important role in film/coatings properties. The and mad cow disease (Kronenthal, 2015). The alternate sources of
mammalian gelatin has good packaging properties, followed by poultry gelatin that are gaining the attention of researchers are fish and poultry
and marine gelatin owing to their composition (Nurul Saadah Said & by-products. Poultry wastes such as blood, viscera, feet, and bone are
Sarbon, 2022). rich in collagenous protein and are now broadly used in food industries
The gelatin sources are pig and bovine skins, demineralized hooves, (Bichukale, Koli, Sonavane, Vishwasrao, Pujari & Shingare, 2018).
and bones. Among these, one of the primary sources of gelatin is pig skin Gelatin is a significant additive used as a gelling, emulsifier, and
(L. Lin, Regenstein, Lv, Lu & Jiang, 2017). Porcine contributes 46%, thickener for various products in the food industry, such as candy
bovine hides 29.4%, and pork and cattle skeletons 23.1% of the total preparation, bakery products, desserts, ice cream, and meat products

* Corresponding authors.
E-mail addresses: [email protected] (H.A. Makroo), [email protected] (D. Majid), [email protected] (F.J. Barba), [email protected]
(A.M. Khaneghah), [email protected] (B.N. Dar).

https://doi.org/10.1016/j.fpsl.2022.100945
Received 11 April 2022; Received in revised form 7 September 2022; Accepted 11 September 2022
Available online 24 September 2022
2214-2894/© 2022 The Authors. Published by Elsevier Ltd. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-
nc-nd/4.0/).
J.A. Rather et al. Food Packaging and Shelf Life 34 (2022) 100945

(Zhang, Liang, Li & Kang, 2020). It is vital in meat products to reduce kDa), respectively. The primary amino acids present in the gelatin are
purge and fat-binding properties and prevent color discoloration, glycine (27–35%), proline, and hydroxyproline (20–24%) (H. Jafari
rancidity, and microbial spoilage (Umaraw & Verma, 2017). Moreover, et al., 2020). Additionally, higher contents of β-components also con­
in confectionery products, gelatin improves foam stability, texture, and tributes towards better gel properties and promote strength in the
chewiness and provides creaminess and mouthfeel in low-fat spreads. In gelatin films as they inspire the better ability of renaturation to the full
dairy products, gelatin provides stabilization and texturization, and in native collagen form (Nurul Saadah Said & Sarbon, 2022).
baked goods provides emulsification, gelling, and stabilization proper­ As far as its bonding is concerned, it is stabilized by diverse forms of
ties (Mokrejš, Mrázek, Gál & Pavlačková, 2019). Gelatin being exploited covalent bonds, and various weak interactions govern its separation and
in numerous areas of food industries also has a substantial role in flexibility. At low temperatures, gelatin is present in a collagen fold
developing biodegradable packaging material. The biodegradable conformation capable of creating hydrogen bonds. Further, its double-
coatings/films can protect, maintain, extend the shelf-life of food stranded or triple helical structures are also hydrogen bond stabilized,
product, owing to the good filmogeniic ability of gelatin (Said & Sarbon, formed by glycine residues (occurring after every third amino acid
2022; Amiri, Moghanjougi, Bari & Khaneghah, 2021; Mahdavi et al., residue in the α-chain structure) inside the triple helix and form weak
2021; Liu, Yao, Yun, Zhang, Qian & Liu, 2021). For instance, gelatin bonds with the carbonyl group oxygen atom (Kessler et al., 2021). Water
films can be used for packaging to guard plant and animal origin food molecules also show their involvement in the hydrogen bonding of the
and products against microbial evolution, handling abuse, and pre­ gelatin network (Rahman & Jamalulail, 2012). Investigations also reveal
venting lipid/fat oxidation and moisture loss (Lee, Lee, Yang, & Song, that the three-dimensional structure of gelatin gels in deuterium oxide is
2016; Yadav, Kumar, Upadhyay, Singh, Anurag & Pandiselvam, 2022). stabilized by hydrogen bonds of –NH group of one chain with –CO
The physical and mechanical properties of gelatin protein films groups of other gelatin chain and hydrogen bonds made by water with
depend on the characteristics of the raw material source and the method chains of gelatin (Kessler et al., 2021). Similarly, hydroxyproline also
of extraction used (Nurul Saadah Said & Sarbon, 2022). Furthermore, forms hydrogen bonds with water by connecting hydroxyproline (–OH)
the properties of gelatin are also affected by physical parameters groups of one chain with the (-CO) backbone of similar or other strands,
involved in the processing of films and the inclusion of plasticizers, thereby stabilizing the triple-helical areas or junction zones (T. Luo &
polymers/fillers, and cross-linkers (Nazmi, Isa, & Sarbon, 2017). Gelatin Kiick, 2013). Hydrophobic interactions are known to perform an insig­
being highly hygroscopic needs the incorporation of other substances nificant role in triple helix development of collagen molecule assembly
like fillers and improvers to enhance its applicability for food packaging. but showed a chief effect on forming β-sheets. Experiments on skin
Adding phenolic substances, various polysaccharides, lipids, and other gelatin of pigs incorporated with glycidol showed improved aggregate
plant-based extracts can improve gelatin’s packaging properties (Said & formation with a concentration in this phenomenon; hydrogen bonds
Sarbon, 2022). This present review paper detailed the information on play an essential role (Xu, Li, Tang, Qiao & Jiang, 2012). They used UV
the source, extraction method, type of modification on the analysis to demonstrate hydrophobic interactions, which increased and
physico-mechanical film properties of gelatin protein films and coatings, competed with hydrogen bondings as a function of increasing gelatin
and their impact on the shelf life extension of the food products. concentrations. The protein foldings are also improved by hydrophobic
interactions, which perhaps cause chain aggregations, thus affecting the
physical and mechanical properties of the films. These hydrophobic
1.1. Chemistry and properties of gelatin
interactions also cause molecular chain extensions by forming a
beta-sheet structure due to increased repulsions in hydrophobic regions
Gelatin is derived from the Latin word gelatos, meaning ’stiff/frozen’
between charged residues (Duconseille, Astruc, Quintana, Meersman &
obtained from different animal sources by partial hydrolysis/thermal
Sante-Lhoutellier, 2015).
denaturation. The structure of gelatin is shown in Fig. 1. Gelatin
Salts and diverse pH also influence electrostatic interactions in the
approximately contains protein (88%), moisture (10%), and salts
gelatin polyelectrolytic gel as it is rich in protein content bearing
(1–2%), and on a dry-weight basis, the protein content is 98–99%
cationic wells and anionic groups. Studies on the swelling behavior of
(Valcarcel, Fraguas, Hermida-Merino, Hermida-Merino, Piñeiro &
gelatin using diverse NaCl concentrations have shown that the swelling
Vázquez, 2021). The protein gelatin is odorless, bland, dull, or slightly
degree is influenced by the ionization degree of solutions attributed to
yellow in color, fragile, and translucent. It is in tasteless sheet, flake, or
the ion pairs formation between charge networks and counter ions
powdered form and is unsolvable in organic solvents but solvable in
(Vigata, Meinert, Bock, Dargaville & Hutmacher, 2021). Moreover, salt
glycerol, hot water, and acetic acid. Gelatin is an amphoteric substance,
addition affects the stabilization of gel network by modifying the elec­
depending on the nature of the solution (Nik Aisyah, Nurul, Azhar &
trostatic interactions of gels. The studies can justify it by Haug, Draget, &
Fazilah, 2014). Gelatin has an isoelectric point at pH 4.8–9.4; gelatins
Smidsrød (2004) on the mechanical properties of fish gelatin by
processed by acidic treatments have a higher isoelectric point than
adjusting variable pH and incorporating salts. The salts and pH varia­
gelatin processed by alkaline treatments. It is a blend of diverse mo­
tions caused stabilization of the junction zones in gelatin due to the
lecular weight chains such as α- chains, β- chains, and ɣ- chains having a
formation of additional electrostatic interactions.
molecular weight of (80 ~ 125 kDa), (160 ~ 250 kDa), and (240 ~375
Despite the thermal and chemical treatments, covalent bonds remain
within the gelatin molecules and impart various mechanical properties.
It has been investigated that collagen covalent bonds are formed by the
allysine pathway in which aldolic condensation takes place by 2 allysine
residues (lysine with aldehyde group) to form a cross-link. Another
probable reaction includes forming a Schiff base by allysine and lysine
residues to form a lysinorleucine. Eyre, Weis, & Rai, (2019) also
described hydroxylysine (found in bone tissue) and allysine pathways,
which are both identified as precursors of cross-link formation. Pento­
sidine is a cross-link naturally found in skin proteins like collagen and
gelatin due to the reaction among pentoses and arginine or lysine side
chains (Vos et al., 2013). The hexoses also contribute to pentosidine
development by sugar fragmentation during prolonged protein glyco­
Fig. 1. Chemical structure of gelatin (Thakur, Govender, Mamo, Tamulevicius, sylation. Pyridinoline and deoxypyridinoline are 2 pyridinium ring-like
& Thakur, 2017). cross-links in collagen non-helical regions formed by the lysyl oxidase

2
J.A. Rather et al. Food Packaging and Shelf Life 34 (2022) 100945

pathway (Ricard-Blum, 2011). As the denaturation of collagen takes 2.1. Poultry gelatin
place and results in gelatin formation, other covalent bonds form due to
the chemical and environmental conditions during/after the The poultry processing industries are one of the best-rising agro-food
manufacturing process. The resulting cross-links are favored by higher segments in the world. The worldwide meat production from poultry
temperatures, humidity, UV-light & chemical substances like reducing sources grew from 92.68 MT IN 2008 to around 127.29 MT in 2018, as
sugars & formaldehyde (Solt et al., 2019). Other types of cross-links per FAOSTAT (2019). Among this production in 2008 share of chicken,
have also been observed and characterized in gelatin. The underlying Geneva fowl, duck, goose, and turkey were 80.84, 2.27, 3.83, 2.27, and
mechanism is that the free amine groups of lysine residue react with an 5.7 MT, respectively, while as shear of these birds in 2018 was 114.26,
aldehydic group, forming a hydroxymethyl amino, yielding a water 2.64, 4.46 and 5.9 MT, respectively. This tremendous increase in poultry
molecule to generate a secondary aldimine. The resulting imine group processing can generate huge quantities of byproducts and wastes uti­
further reacts with other lysine residues and forms dimethylene ether, lized for gelatin and pet meal production. Poultry processing results in
which undergoes rearrangements and links two lysine residues with the numerous by-products/wastes comprising liver, gizzard, feet, skin,
methylene bond (Vistoli, De Maddis, Cipak, Zarkovic, Carini & Aldini, feathers, and head, which contains 34.2% dry matter with 51% protein,
2013). Therefore, the cross-links in gelatin involve multiple interactions 41% fat and 6.3% ash content (Abedinia et al., 2020).
at both intra-molecular and inter-molecular regions of the helices. Management of these valuable sources possibly will offer economy to
However, a few more cross-links are still under observation and dis­ the countries and a solution to waste utilization. Chicken feet are
cussion, like disulfide linkages and pyridinoline (Duconseille et al., underutilized by-products in the planned poultry processing industry
2015). and often thrown away without treatment, and can be a reason for
environmental pollution. Chicken feet contain collagenous material that
2. Sources of gelatin can be utilized as a good source of gelatin (Chakka, Muhammed, Sakhare
& Bhaskar, 2016; Chakka, Muhammed, Sakhare & Bhaskar, 2017).
Mammalian sources such as pig skin and cowhides are the most Protein isolates are also obtained from low-value poultry processing
available sources of gelatin, accounting for 46% of the world’s gelatin wastes like bones and mechanically separated meat residues (Du, Khiari,
source, followed by bones (23%), hooves (29%), and the remaining 1% Pietrasik & Betti, 2013). Chicken wastes like a comb, bone, cartilage,
coming from marine sources such as fish (Rakhmanova, Khan, Sharif & and wattle contain higher gelatin content (Fig. 2). Chicken skin gelatin
Lv, 2018). In Europe, 95% of gelatin is obtained from bovine hides and contains more α-helix and β-sheet structures with hydrogen bonding;
porcine, and 5% from their bones (Alipal et al., 2021). Mammalian hence the gelatin has higher gel strength and elastic and viscous
gelatin has high boiling and gelling points and a thermoreversible modulus (Soo & Sarbon, 2018).
character. The bones, cattle hides, and pork skin are traditional In a study by Bichukale et al. (2018), gel strength of bone poultry
mammalian sources of gelatin (Alipal et al., 2021). The gelatin from cow
bone is of high quality and is preferred for industrial purposes. Due to
religious and aesthetic objections, pork gelatin and gelatin obtained
from other animals not slaughtered following Islamic laws are not used
(Rakhmanova et al., 2018). These reasons increased the halal foods and
additives market and gained researchers and industrialists (Ab Talib,
Sawari, Hamid & Chin, 2016). Therefore, researchers are searching for
an alternative, new, halal sources of gelatin. In recent years the market
potential of fish and poultry by-product gelatin gets increased. Poultry
wastes are probably the chief sources of gelatin soon but presently have
limited commercial production due to low yields (Abedinia et al., 2020).
Much research is being done to obtain gelatin from fish skin and poultry
wastes compared to gelatin obtained from mammals. From the pack­
aging point of view, the source of gelatin plays an important role in the
physical, chemical, and functional properties of the films that can be
developed from a particular source of gelatin which can be discussed by
Alfaro, Balbinot, Weber, Tonial, and Machado-Lunkes (2015). Table 1 Fig. 2. Gelatin content in different parts of poultry, turkey heads, chicken
summarises the physical and mechanical properties of different sources heads, chicken feet, chicken skin and chicken waste (Rahman & Jamalulail,
of gelatin films. 2012; Du et al., 2013; Sarbon et al., 2013).

Table 1
Physical and mechanical properties of different sources gelatin films.
Gelatin Film WVTR (g/ms Pa) TS (MPa) EAB (%) Reference
− 10
Bovine hide/oregano essential oils 0.81–1.21 ₓ 10 8.90–14.00 8.30–10.10 Martucci, Gende, Neira, and Ruseckaite (2015)
Bovine hide/lavender essential oils 0.68–1.27 ₓ10− 10 8.80–15.40 4.30–7.60 Martucci et al. (2015)
Bovine/curcumin extract 0.90–1.20ₓ10− 10 1.90–3.40 144.30–198.60 Musso, Salgado, & Mauri, (2017)
Tilapia skin/ginger essential oils 1.88–2.61 ₓ10− 11 18.58–35.73 41.70–72.03 Tongnuanchan, Benjakul, & Prodpran, (2013)
Tilapia skin/turmeric root essential oils 1.89–2.48 ₓ 10-11 23.34–34.04 42.79–72.08 Tongnuanchan et al. (2013)
Fish skin/ haskap berries extract 5.96–7.14 ₓ 10-11 46.70–51.50 2.87–3.69 Liu et al. (2019)
Fish skin/Origanum essential oil 1.35–1.90 ₓ10-11 3.28–6.72 87.20–151.82 Hosseini, Rezaei, Zandi, and Farahmandghavi (2016)
Feet gelatin/25% glycerol 2.04 ₓ10-11 44.86 15.99 Tew et al. (2017)
Feet gelatin/35% glycerol 2.14 ₓ10-11 34.20 33.30 Tew et al. (2017)
Chicken skin/rice flour 6.83 ₓ 10-11 –1.39 ₓ 10-9 2.08–2.91 58.45–79.31 Soo & Sarbon, (2018)
Chicken skin/5–20% glycerol 4.86–6.67 ₓ10-12 1.75–3.64 106.43–148.33 Nor, Nazmi, & Sarbon, (2017)
Chicken skin/CMC/Centella 1.11–1.13 ₓ10-4 5.00 ₓ 10-2 271.17–281.00 Nazmi & Sarbon, (2020)
Chicken skin/CMC 1.03 ₓ10-4 3.00ₓ10-2 223.05 Nazmi & Sarbon, (2020)
Chicken skin 5.94 ₓ10-10 1.54 48.33 Soo & Sarbon, (2018)
Chicken skin 4.17 ₓ10-12 33.66 3.87 Nor, Nazmi, & Sarbon, (2017)

3
J.A. Rather et al. Food Packaging and Shelf Life 34 (2022) 100945

gelatin at 40 ◦ C, 45 ◦ C, 50 ◦ C, 55 ◦ C, and 60 ◦ C were 257.67, 274, mrigala, Labeo rohita, Aluterus monoceros, Channa striatus, Claris batra­
265.33, 263, and 260 g, while gel strength of poultry skin gelatin at chus, Pangasius sutchi was 367.7, 343.0, 258.0, 149.8, 311.2, 278.7, 325
similar temperatures were 258.33, 282.67, 273.67, 264.33 and 262 g and 487.6 g respectively (Nitsuwat, Zhang, Ng & Fang, 2021).
respectively. The viscosity of the gelatin extracted at similar tempera­ Fish gelatin exhibits good filmogenic properties, is transparent,
tures were 3.83, 5.53, 4.43, 4.07, and 4.03 cP for one gelatin, and the nearly colorless, aqua-soluble, and extremely extensible (Alfaro et al.,
viscosity values of skin were 5.77, 9.10, 8.33, 7.37, and 6.53 cP 2015). Abundant studies have been done on marine gelatin protein
respectively. This study indicates that the gel strength and viscosity were films, such as active fish gelatin/peppermint oil composite film and
higher at 45 ◦ C. Thus the gelatin extracted at this temperature showed intelligent fish gelatin/haskap berry extract film (Nurul Saadah Said &
improved packaging properties. Poultry wastes/byproduct gelatin ex­ Sarbon, 2022). Compared to animal gelatin films, the thickness of single
hibits good filmogenic properties owing to its higher bloom value and fish-based gelatin films has been reported in the range of 0.05–0.12 mm
imino acid groups (Nurul Saadah Said & Sarbon, 2022). Several in­ (J. Liu, Yong, Liu, Qin, Kan & Liu, 2019). While, the thickness of active
vestigations have been lead on poultry wastes/byproducts based gelatin fish gelatin composites with incorporated natural extracts of grape seed,
films, including the active chicken skin gelatin-Centella asiatica com­ basil, cinnamon, and lavender oils were stated in higher range of
posites (Suderman & Sarbon, 2019) and active duck paw 0.06–0.21 mm as compared to single fish gelatin films (Nurul Saadah
gelatin-cinnamon leaves essential oil biocomposite films (Yang, Lee, Said & Sarbon, 2022). The color (L*, a*, and b*) values for single gelatin
Beak, Kim, & Song, 2017). The single poultry-gelatin film derivative of films derived from tilapia, unicorn leatherjacket, and catfish were re­
chicken paw gelatin film showed a lower thickness (0.06 mm) almost ported in range of 90.32–94.25, − 2.51–(− 0.80) and − 1.68–15.81,
similar to those thickness values obtained from single films of bovine respectively (Arfat, Ahmed, Hiremath, Auras & Joseph, 2017).
gelatin (Tew, Soon, Benjakul, Prodran, Vittayanont & Tongnuanchan, Meanwhile, the UV light transmission (200–280 nm) for a single fish
2017). On topmost of that, single poultry gelatin films were seeming as gelatin films derived from numerous fish species exhibited higher values
lesser yellowish compared to animal and fish gelatin films. The color of 0.01–40.73 compared to the animal gelatin film (Jridi, Abdelhedi,
values (L*, a*, and b*) of single poultry-derived gelatin (chicken feet) Salem, Kechaou, Nasri & Menchari, 2020). The single gelatin films of
films showed L* value of 90.77–91.29 with a* value of − 1.40–(− 1.30), fish source have been described to reveal lower WVP than single animal
and b* as 3.18–3.01 (Tew et al., 2017). This might be accredited to gelatin films. The statement was also supported by the outcomes of
lower contents of amino acids cysteine (0.16%) and methionine (0.07%) Nurul Saadah Said & Sarbon (2022), who found that single marine
in poultry based gelatin films compared to fish and animal gelatin gelatin films showed WVP values of 6.00 × 10− 13–2.05 × 10− 10 g/m.
(Nurul Saadah Said & Sarbon, 2022). Addationally, single poultry s⋅Pa compared to the reported values from bovine gelatin films. The
gelatin-derived films of chicken skin have been stated to have lowest UV melting point of single fish gelatin film was reported to reveal a lower
light transmission of 0.03–4.48 compared to other sources of gelatin. endothermic melting shift of 53.14–124.45 ºC compared to single animal
The WVP of poultry gelatin films derived from chicken feet and skin gelatin films (Ali, Prodpran, & Benjakul, 2019). The marine-based
were 4.17 × 10− 12–5.94 × 10− 10 g/m.s. Pa compared to animal gelatin gelatin films exhibited lower TS value (6.23–43.62 MPa) compared to
films (Nor, Nazmi, & Sarbon, 2017). The melting points (Tm) of single marine animal gelatin films, the EAB value for a single fish gelatin films
chicken gelatin films were reported to be in higher range (49.51–134.22 was reported in range of 2.96–76.73% (Nurul Saadah Said & Sarbon,
ºC) compared to single mammalian and fish gelatin films. Besides, 2022).
poultry gelatin films derived from chicken feet and skin gelatin have
been stated to exhibit higher tensile strength of 34.20–44.86 MPa and 2.3. Mammalian gelatin
0.98–33.66 MPa respectively than reported from fish gelatin films
(Nurul Saadah Said & Sarbon, 2022). Various mammals used for gelatin production are cow, goat, buffalo,
and yak. The most crucial gelatin source in the 1930 s was pig hide
2.2. Fish gelatin which accounted for primary industrial gelatin production. The
mammalian collagen/gelatin sources are hides or skin, tendons, skele­
The fish and its byproducts were extensively studied as a potential tons, and cartilages. The gelatin from porcine and bovine sources is
source of gelatin protein. The fish processing industry generates a sub­ generally obtained from skin or hides and, to a lesser extent, from bones,
stantial amounts of by-products and wastes while manufacturing fish cartilages, and tendons. Buffalo processing wastes are well suited for the
fillets, as product yields are only ~30–50% (Coppola, Lauritano, Palma production of gelatin. Buffaloe’s hides are 6–8 mm thick and more
Esposito, Riccio, Rizzo & de Pascale, 2021). These wastes and potent than other mammals’ hides, corresponding to approximately
by-products are rich in gelatin protein, but to date, fish gelatin use is 11.5% of total body weight, and cowhide accounts for 9.0% only
limited in food industries compared to mammalian gelatin. The main (Crackers, 2011). Collagen is a significant constituent of buffalo hide,
reason for lower usage of fish gelatin has been reported owing to fishy and buffalo hide has more collagen than cowhide. Due to the higher
off orders, and other reasons are its poorer gelling ability (Tohmadlae, hydroxyproline content in buffalo hide collagen, collagen structure has
Worawattanamateekul, & Hinsui, 2019). higher complexity, heat stability, and gel strength (Mulyani, Setyabudi,
Fish processing wastes account for 75% of the catch weight (Coppola Pranoto & Santoso, 2017). A study of two diverse sources of mammalian
et al., 2021). Among these, fish skin and bone represent ~30% of the gelatins, i.e., bovine and porcine, showed that both contain diverse
weight, which contains higher collagen content that can be utilized to molecular weight components ranging between 10 and 400 kDa. The
produce fish gelatin. The gelatin from fish processing wastes such as skin extensively used mammalian gelatin has some constraints and skepti­
provides a substitute and serves alternative gelatin sources for markets cism amongst consumers due to sociocultural and health-related anxi­
worrying about the bovine spongiform disease. Fish gelatin has lower eties (Abdalbasit Adam Marion & Fadul, 2013). For extraction of gelatin
melting and gelling temperatures and lower gel strength than mamma­ from mammalian (bovine/porcine) sources, various extraction methods
lian gelatin. Gelatin obtained from warm waters fishes contains normal are used, but the majority of bovine gelatin was extracted by acidic
hydroxyproline content and gel strength, but gelatin obtained from process and porcine gelatin by alkaline methods (Mariod, Abdelwahab,
cold-water fishes has low hydroxyproline content and gel strength. Deep Ibrahim, Mohan, Abd Elgadir & Ain, 2011). The bovine gelatin is extra
cold-water fish processing waste gelatin contains a lesser quantity of popular than other gelatin sources for film making owing to its superior
proline and hydroxyproline, thus forming a gel at a lower temperature of gel forming capacity (gel strength and viscosity) and strong filmogenic
8–10 ◦ C (Shahiri Tabarestani, Maghsoudlou, Motamedzadegan & properties. Additionally, various studies have been presented on active
Sadeghi Mahoonak, 2014). and intelligent animal gelatin, like active bovine-gelatin/nano chi­
The gel strength of various fish species like Catla catla, Cirrhinus tin/corn oil composites and intelligent bovine/curcumin composite

4
J.A. Rather et al. Food Packaging and Shelf Life 34 (2022) 100945

films (Nurul Saadah Said & Sarbon, 2022). The material is placed in a solution of 0.2% acetic acid (v/v) for 40 min
The bloom strength of the mammalian gelatin was reported to be for additional extraction; the solution is drained and washed with water
higher than that of the fish and animal gelatin. Chandra & Shamasundar till neutral pH is attained. The final gelatin extraction is achieved at
(2015) reported the gel strength of porcine to be 466.4 g, while that of 70 ◦ C for 90 min with 1:9 (w/v) of sample and distilled water. The
the bovine gelatin was reported to be 350 g by Atma & Taufik, (2020). gelatin extract is filtered using multilayered cheese clothes and then
The single swinish gelatin films have been reported to have higher freeze-dried. Freeze-dried material is grounded to powder (Golpira,
thickness values compared to single bovine-gelatin films. This is owing Maftoonazad, & Ramaswamy, 2021). The type of acid and its concen­
to the higher protein contents in pig gelatin (91.30%) compared to tration greatly affects the gelatin’s gel strength and hence the gelatin’s
bovine gelatin films (88.45–91.20%) (Aykın-Dinçer, Koç, & Erbaş, packaging properties. Sántiz-Gómez et al. (2019) reported that the
2017). The color (L*, a* and b*) values reported for single bovine-based bloom strength of acetic acid (0.15 M) extracted gelatin was higher than
gelatin films were in the range of (89.07–97.30), (− 1.27 to 0.07), and that of HCl (0.15 M) extracted gelatin. The higher the gel strength, the
(2.00–5.40) respectively, whileas L* , a* and b* values of single porcine higher the tensile strength and better the sealing and barrier properties
gelatin films were reported in the range of (90.00–96.97), (− 0.39 to of developed films.
1.11) and (2.22–3.22) respectively (Nurul Saadah Said & Sarbon, 2022).
The WVP of single animal gelatin film was reported to be 3.2. Ultrasonic assisted extraction method
8.00 × 10 − 11–9.68 × 10 − 10 g/ms⋅Pa. The melting point (Tm) of
single animal gelatin film derived from bovine and swinish gelatin were This is one of the innovative and effective methods used in the food
reported in the range of 60.42–82.20 ºC and 66.80–87.70 ºC respectively and pharmaceutical industries (Lv, Gouda, Zhu, Ye & Chen, 2021). The
(Rawdkuen, Faseha, Benjakul & Kaewprachu, 2020). The higher Tm ultra-sonication treatment disrupts cells by causing acoustic cavitation,
observed in porcine gelatin films may be owing to higher imino acids which increases the mass transfer of cell contents and hence results in a
(23.70%) compared to bovine gelatin films (22.91–23.33%). It has also higher yield of gelatin extraction than other methods or techniques used.
been reported that gelatin with higher imino acid groups require higher Ming, (2013) reported that ultra-sonication aids in the cleavage of
temperature for conversion of coil structure to helix structure, thus collagen fibrils, facilitating acidic and enzymatic hydrolysis. This
gelatin with higher imino acid groups is thermally more stable (Nurul advanced method of extraction increases the yield percentage, and
Saadah Said & Sarbon, 2022). Numerous studies on TS of the animal extracted gelatin shows improved functional properties (Noor et al.,
gelatin films have been reported so for, single porcine gelatin films 2021).
showed TS of 2.40–63.25 MPa. These TS values were higher as This method of extraction, along with the use of food-grade acids can
compared to TS of single bovine gelatin films with TS of 0.70–51.68 MPa increase the yield per cent of gelatin due to a synergistic effect. The acid-
(Nurul Saadah Said & Sarbon, 2022). The EAB values described from treated gelatin source is extracted using a temperature of 70 ◦ C with an
single mammalian gelatin films of bovine and porcine were reported in ultrasonic power of 300 W for (100 min) time. The extract is then sieved
the range of 0.78–30.83% and 4.40–90.55% respectively (Rawdkuen using a two-layered cheesecloth and then freeze-dried. Freeze-dried
et al., 2020). material is ground to form a gelatin powder (Mad-Ali, Benjakul, Prod­
pran & Maqsood, 2017). The gelatin extraction procedure is based on
3. Methods of extraction of gelatin pretreatments with a mild acid to dissociate non-covalent, inter-and
intra-molecular bonds, followed by extraction at above 40 ◦ C in distilled
Gelatin is an essential protein obtained by partial hydrolysis of water to disrupt hydrogen bonds that stabilize helix to coil trans­
collagen. The hydrolysis is done by using acids, bases, enzymes, or by formation resulting in an alteration to soluble gelatin.
their combinations. The most common extraction method of gelatin in The oxhide gelatin hydrolysates treated with 300-W ultra-sonication
industries is the chemical method. However, in biological processes, the had the extreme antioxidant activities. Ultrasonication has been re­
enzymatic extraction method is a more promising hydrolysis process ported to inhibit formation of hydrogen bond, reduction in crosslinking
(Noor et al., 2021). The bonds of collagen polypeptide chains are broken between collagen molecules, transformation of folded structures into a
down. This leads breakdown of the fibrous structure of collagen to helical ones, and lowering of the heat stability of collagen molecules.
produce gelatin. Therefore, the gelatin’s quality and yield depend not Thus the gelatin films developed from gelatin of ultrasonically extracted
only on the gelatin source but also on the extraction methods of gelatin can have higher antioxidant activities and flexibility but lower water
and the conditions during the extraction process. vapour and oxygen permeabilities (He et al., 2021).

3.1. Acidic extraction method 3.3. Enzymatic extraction method

The acid solution is used to hydrolyze collagenous material in this This method creates less wastage and diminishes processing time,
extraction process. The produced gelatin has been called type A gelatin. but the method is extra costlier than other gelatin extraction methods. In
The Pig hides were commonly used materials for this extraction method, the enzymatic method of gelatin extraction, various protein hydrolyzing
which was treated for 10–45 h with acidic solutions (Abedinia et al., enzymes convert collagen to gelatin. For gelatin extraction by this
2020). Acidic treatments enhance collagen’s swelling, resulting in better method, the optimum parameters are treating with pepsin (547 U/g) at
hydrolysis and greater yield per cent (H. Jafari et al., 2020). The 46.98 ◦ C, pH 4 for 1.27 h. Tong & Ying, (2013) reported that gelatin
Swelling power and solubilisation of collagenous materials are highly obtained by the enzymatic method of extraction has better gel strength,
affected by concentration and acid type used, which can cause variation although gelatin yield is a little lower than other gelatin extraction
in molecular weight distribution of resultant gelatin. The significant methods. This higher gel strength is responsible for the higher tensile
acids utilized were phosphoric and other organic acids. However, they strength, storage modulus (G′ ) and barrier properties of the films, as
are gradually more costly and can adversely affect the smell and the reported by Nurul Saadah Said & Sarbon (2022), which is responsible for
flavor of gelatin produced. better sealing strength of the package. In this method, the gelatin source
The minute pieces of gelatin source are first soaked into NaOH so­ is washed and then chopped to a uniform minute size (0.5–1.0 cm).
lution with a 0.2% concentration (w/v) to remove non-collagenous Further, chopped material is stirred with NaCI solution (3.5%) for 24 h
material. Then the mixture is shaken and stirred continuously at to exclude non-collagenous materials. After this, a solution of 0.5%
22–28 ◦ C for 40 min. The material is then treated with an alkaline so­ Na2CO3 is used to remove lipid-soluble materials by stirring at 200 rpm
lution three times. Undesirable components get removed during this for two days. Defatted material is then neutralized with water. Next,
treatment, and the material turns soft and ready for gelatin extraction. pepsin enzyme solution is added for the extraction of gelatin. The

5
J.A. Rather et al. Food Packaging and Shelf Life 34 (2022) 100945

gelatinous solution is centrifuged for 20 min at 500 rpm to remove Table 2

insoluble materials. Gelatin precipitation is done using ammonium Applications of gelatin based films and coatings on shelf life of food and food
sulfate (2.6 M). In second centrifugation, precipitated material is products.
collected and then freeze-dried. Feng et al. (2013) reported that enzyme Product Coating/film Improved features References
solutions of concentration 2.42% with liquid to solid ratio of 11.8:1 for findings
6.45 h are the most yielding parameters. Fruits & Gelatin and shellac Ripening & Soradech,
vegetables softening gets Nunthanid,
3.4. High-pressure extraction delayed, Limmatvapirat, and
diminished weight Luangtana-anan
loss with extended (2017)
High-pressure extraction is another innovative non-thermal tech­ shelf-life greater
nique in gelatin extraction (Pinheiro, Martí-Quijal, Barba, Tappi & than 30 days
Rocculi, 2021). The high pressure causes the protein’s denaturation and Banana Gelatin and shellac Ripening & Soradech et al.
distresses non-covalent interactions, making gelatin protein extract softening gets (2017)
delayed,
easily (C. C. Lin, Chiou, & Sung, 2015). High pressure and acid treatment diminished weight
have also been reported to enhance extraction yield by causing acid to loss with extended
penetrate more into the pretentious material, thereby increasing the shelf-life greater
extraction percentage (H.-W. Huang, Cheng, Chen & Wang, 2019). It has than 30 days
Strawberries Gelatin & mentha Depressed Aitboulahsen et al.
also been reported by Zhang et al. (2020) that extraction time is reduced
essential oil (MEO) microflora growth, (2018)
by more than 50% using this extraction method. Noor et al. (2021), with retention of
extracted gelatin from fish skin using this extraction method by placing pH, firmness,
alkali/acid pretreated skins in polyethylene bags containing distilled weight, TSS and
water. The sample bags were placed in the high-pressure chamber for visual appearance
greater than 13
10 min at 250 MPa and showed a higher yield than conventional
days.
methods, as already told by (H.-W. Huang et al., 2019). Chen, Ma, Zhou, Grapes Gelatin & iron Enhanced Mehmood, Sadiq, &
Liu, and Zhang (2014) reported that the gel strength and viscosity get oxide mechanical, Khan, (2020)
improved by the application of 300 MPa pressure. Higher the gel nanoparticles barrier & physical
properties of films,
strength of high pressure extracted gelatin can improve the film-forming
20% of
properties of gelatin, as gelatin with higher gel strength showed incorporated
improved tensile strength properties. Yusof, Jaswir, Jamal, Jami, and nanoparticles
Octavianti (2017) also reported improvements in the red tilapia gelatin, exhibited
which could be responsible for better packaging properties. antibacterial
activity against
E. coli and
4. Applications of gelatin Staphylococcus
aureus, increased
Gelatin is known for its multifunctional properties, including its shelf life of grapes.
Grapes (red Gelatin-corn starch Increased Fakhouri, Martelli,
rheological (Santana et al., 2020), emulsifying and foaming capacities
crimson) mechanical and Caon, Velasco, and
(Chakka et al., 2017), bioactive properties (N S Said, Howell, & Sarbon, barrier properties, Mei (2015)
2021), fat replacing properties (Almeida & Lannes, 2017), and retained visual
film-forming properties (Lu et al., 2022). appearance and
Gelatin is a vulnerable material with wide applicability in numerous weight loss
reduction during
industrial sectors. It has numerous applications in fruit and vegetable,
storage.
dairy, meat, confectionery, bakery, and packaging industries. It is used Grapes & Gelatin, Exhibited Kamari & Phillip,
as a coating, thickening, and refining agent in the fruit and vegetable cherry methylcellulose, antibacterial (2018)
industries. In the confectionery industry, it acts as gelling, stabilizing, tomatoes Chitosan and activity against
tannic acid E. coli & S. aureus,
and whipping agent. It is also a stabilizing agent in foods like ice creams,
reduced weight
cheese, foams, and fruit salads. It has been used in desserts and gummy loss and browning
bears (7–9%), meat products, sausages, broths and canned meats of fruits and
(1–5%), dairy products (0.2–1.0%), frozen foods (0.1–0.5%) and bev­ prolonged the shelf
erages (0.002–0.015%) (Abedinia et al., 2020). of fruits at least 14
days.
Gelatin plays a prominent role in the medical industry as it is used in
Cherry Gelatin-Lotus stem Reduced weight Rather, Makroo,
coating pastilles, tablets, and capsules and encapsulates nutritional tomatoes starch loss, retained color, Showkat, Majid, and
supplements. Gelatin has been reported to have higher health- TSS and pH, Dar (2022)
promoting properties. The gelatin possesses biodegradability, biocom­ retained firmnesss,
patibility and lower antigenicity. Hence can be used as a potential enhanced shelf life
upto 15 days.
constituent in healing wounds and regeneration of tissues (Lv et al., Potatoes Gelatin-alginate Diminished disease Pour, Saberi-Riseh,
2021). Fish gelatin has showed higher potential of treating diverse dis­ with Pseudomonas incidence, Mohammadinejad,
eases owing to its composition. Osteoporosis is a major problem nowa­ fluorescens bacteria sheltered and Hosseini (2019)
days in older people due to calcium loss which results in porosity of probiotics from
damaging
bones by causing a lowering of bone marrow density. In another study,
condition of soil
Noma et al. (2017) showed that gelatin is utilized to reduce bone brit­ and increased
tleness. The gelatin can be exploited in diets of hypertensive people as an shelf- potato stored
anti-hypertensive representative (C. C. Lin et al., 2015). Table 2 sum­ life.
marizes gelatin-based films and coatings applications on food and food Cucumber Gelatin-clove oil Strong Cui, Bai, Rashed, and
with chitosan antibacterial Lin (2018)
products. nanoparticles properties against
(continued on next page)

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J.A. Rather et al. Food Packaging and Shelf Life 34 (2022) 100945

Table 2 (continued ) Table 2 (continued )

Product Coating/film Improved features References Product Coating/film Improved features References
findings findings

E. coli O157:H7 Gelatin-chitosan oxidation of lipids Xiong, Chen,

biofilms, retention with nisin and and proteins and Warner, and Fang
of original color grape seed extract stunted microbial (2020)
and flavor of growth during cold
cucumber during storage for 20 days.
storage. Pork slices Gelatin-chitosan The Coatings Zhang et al. (2020)
Olive oil Gelatin with Reduced oxidation Wang et al. (2019) coating with inhibited
anthocyanins during storage and encapsulated deterioration of
prolonged shelf-life tarragon essential pork slices,
of olive oil. oil tarragon essential
Extra-virgin Gelatin, Corn Enhanced water Malherbi et al. oil prevented
olive oil starch with vapor barrier, (2019) oxidation and
Fish & activated prevented microbial growth.
meat guabiroba pulp oxidation with Enhanced shelf life
maintained acidity of pork slices
index and peroxide during 16 days of
index values of cold storage.
olive oil during Chicken fillet Gelatin, chitosan Showed activity Amjadi, Emaminia,
storage. nanofiber & Zinc against S. aureus, E. Nazari, Davudian,
Fish fillets Gelatin & Prevented fish filet Sun et al. (2019) oxide coli, and Roufegarinejad, and
(grass carp) curcumin/β oxidation and nanoparticles P. aeruginosa, Hamishehkar (2019)
cyclodextrin proteolysis, abridged weight
(CUR/βCD) reduced spoilage loss, reserved
emulsion and enhanced the product quality
storage life of filets. and improved
Fish Gelatin/polyvinyl Enhanced Zeng et al. (2019) shelf-life
freshness alcohol with elongation at break significantly.
evaluation anthocyanin from 589.22% to Active food Gelatin, sodium Inhibited lipid Roy & Rhim, (2020)
905.86%, packaging dodecyl sulfate oxidation of
anthocyanins (Industrial products and
delivered sensitive scale) exhibited strong
response to diverse activity against
pH & seemly in E. coli and
monitoring volatile L. monocytogenes.
compounds Hygienic Gelatin/sericin/ Improved tensile Purwar, Verma, &
produced during product clay, strength at Batra, (2019)
the spoiling of fish packaging glutaraldehyde & 8.1 MPa, presented
and helped in glycerol activity against
evaluating bacteria Staphylococcus
easily & aureus, Escherichia
maintained the coli etc.
organoleptic Cheese Gelatin, moringa Presented Lin et al. (2017)
features of shrimp. oil with chitosan antimicrobial
Shrimp Gelatin & chitosan Suppressed growth Mohebi & Shahbazi, nanoparticles activity against
of P. fluorescens, (2017) L. monocytogenes
Shewanella and S. aureus and
putrefaciens, reserved the
Pseudomonas spp., sensory quality of
L. monocytogenes cheese for 10 days.
and lactic acid &
flavor for
minimum 10 days 4.1. Gelatin as packaging material
storage during
refrigeration.
Beef meat Gelatin-chitosan Films hindered Cardoso et al. (2019)
Packaging is an essential unit operation in the food chain, and its
(monolayer and weight loss & lipid importance is in every type of food product. Edible packaging material
bilayer oxidation of meat such as coatings and films has great packaging demand because of their
composites) even after 6–10 biodegradable nature, maintaining quality, and improving food and
days and
food products (Soo & Sarbon, 2018). The coatings and films act as al­
suppressed
psychrotrophic ternatives in packaging, having excellent barrier properties and thus
bacteria, molds enhancing of shelf life of foods. These protein-based films are gaining
and yeast growth. importance nowadays over traditional petroleum-based packaging ma­
Pork meat Gelatin nisin/ Nisin & catechin Kaewprachu et al. terials. Among the protein-based packaging materials, gelatin films and
catechin with prevented the (2018)
microbial growth of spoilage
coatings have better properties due to their uniqueness. Gelatin coatings
transglutaminase microorganism, and films retain the quality of foods throughout storage, acting as bar­
crosslinker diminished fat riers to oxygen gas, light, and moisture, preventing deterioration, re­
oxidation, tards oxidation, and protecting food from other quality losses.
maintained the
Made barrier properties of gelatin coatings and film can be improved
quality of pork
meat during by combining gelatin with various polysaccharide substances like xan­
storage. than, chitosan, and rice flour (Ahmad, Hani, Nirmal, Fazial, Mohtar &
Pork Retained normal Romli, 2015). Including antioxidant and antimicrobial substances in
pH, inhibited gelatin films and coatings improves barrier properties and preservation

7
J.A. Rather et al. Food Packaging and Shelf Life 34 (2022) 100945

of food products (Martins, Cerqueira, & Vicente, 2012). Numerous ef­ Gunathilake, Pathirana & Fernando, 2021). Nowadays, coating by
forts have been made for natural antioxidants to prevent oxidative various edible substances such as lipids, proteins, polysaccharides, or
deterioration of food products. Plants such as phenols, tannins, flavo­ their combinations is applied to these horticultural products. The
noids, and plant extracts have been included in gelatin films with anti­ application of coatings on horticultural commodities provides a substi­
microbial and antioxidant properties, thus increasing shelf life and tute for modified atmosphere storage for quality retention through
improving food quality. The added antimicrobials of essential oils alteration and regulation of the internal atmosphere of the different fruit
remain in films, prevents microbial spoilage for a longer duration, and and vegetable. Biodegradable coatings reduce moisture loss, oxidative
extends shelf life (Khorshidian, Yousefi, Khanniri & Mortazavian, 2018). reactions, solute migration, and gaseous exchange, and decrease or
Tea’s polyphenols can be incorporated in free and encapsulated form reduce physiological disorder problems (Dhall, 2013). Gelatin-based
into gelatin films to improve packaging properties. Polyphenols in the coating solutions prevent weight loss, prevent degradation of Vit C,
free form are distributed homogeneously in gelatin films and released and darken the color of fruits. These gelatin coatings may be introduced
fast, while encapsulated ones would be released slowly and uniformly with other natural substances such as plant extracts containing antiox­
from nanoparticles to the gelatin film matrix. Initial oxidation of food idant and antimicrobial components to enhance the shelf-life of these
products is prevented by the free tea polyphenols packaged in these horticultural commodities. The gelatin coatings incorporated with ex­
gelatin films, whereas encapsulated ones are released slowly from the tracts of tea and Aloe vera maintain and prolong the fresh-cut orange
nanoparticles and extend overall shelf life. Encapsulated and free anti­ quality. Coating apple slices with gelatin containing plant extracts of tea
oxidants guarantee the long-term storage life of foods (F. Liu et al., and Aloe vera increases their storage life (Radi, Firouzi, Akhavan &
2015). Adding nisin antimicrobial in gelatin films in free and encapsu­ Amiri, 2017). Yousef, El-Moniem, & Mahmoud (2020) reported
lated forms shows promising results in preserving and retaining the enhanced storage life of date fruits coated with soy protein-gelatin
quality of foods (Imran et al., 2012). These edible coatings and films coating and showed lower weight loss, retained pH and firmness than
with incorporated essential oils help in the preservation of fish and meat control ones. Additionally, Pellá et al. (2020), reported extended storage
(Sánchez-González, Vargas, González-Martínez, Chiralt & Chafer, life of guava fruit packaged in gelatin-casein-statch films, and showed
2011). Alparslan, Baygar, Baygar, Hasanhocaoglu & Metin, 2014, lower senescence and overall quality of the guava fruit packaged in these
concluded that laurel essential oil as an agent of antimicrobial and films. R. Jafari, Zandi, & Ganjloo, (2022), reported reduced weight loss,
antioxidant extends the storage period of refrigerated rainbow trout firmness, volume changes and lower increment of TSS and pH of
fresh fillets. Applying modified gelatin films to different food products zucchini fruit coated with gelatin-alginate with incorporated anise oil.
protects food from various deteriorations. The application of gelatin Instead, Makroo, Showkat, Majid, & Dar (2022), also reported increased
coating and films as packaging in different foods is as follows: shelf life up to 15 days of cherry tomatoes coated with gelatin-lotus stem
starch coating.
4.2. Meat and meat products coating
4.4. Fish packaging
Various preservative methods protect meat and meat products, such
as smoking, refrigeration, and freezing. Besides, the coating of meat The fish industry is also vital for enhancing the economy of several
products is also a technique of preservation. Collagen and gelatin have coastal regions and countries. Due to its biological and chemical
been extensively used as a surface coating on these products to reserve composition, fresh fish is a highly perishable product (Kazemi and
color, reduce aroma deterioration, improve the sensory properties, and Rezaei, 2015). In order to inhibit pathogenic spoilage, various strategies
slow microbial and chemical spoilage. The beef steaks coated with have been developed, including incorporating natural antimicrobial
gelatin and stored for weak showed lower purge than the uncoated beef substances in edible coatings and films to prevent spoilage and
steaks (Gedarawatte et al., 2021). Beef cubes packaged in collagen films contamination of fish and fish products (Gyawali & Ibrahim, 2014;
for 20 weeks showed a slight variance in lipid oxidation to control ones Kazemi & Rezaei, 2015). The edible films for shelf-life extension of fish
because the collagen wrapping showed less oxygen permeability than are prepared from lipids, proteins, and polysaccharides (Kocira, Kozło­
plastic wrapping (Sánchez-Ortega, García-Almendárez, Santos-López, wicz, Panasiewicz, Staniak, Szpunar-Krok & Hortyńska, 2021). Gelatin
Amaro-Reyes, Barboza-Corona & Regalado, 2014). In another study, the is a coating material for fish owing to its high film-forming ability,
sausages were free of mold growth when dipped in gelatin solution abundance, and low manufacturing cost of gelatin films (Peña, Mon­
(23%), sodium hexametaphosphate (6%), hydrochloric acid (2%), and dragon, Algar, Mondragon, Martucci & Ruseckaite, 2013). Gelatin with
water (69%) at the end of three-week storage. In another study, Jridi, other edible ingredients enhances the properties of packaging material
Mora, Souissi, Aristoy, Nasri, and Toldrá (2018) coated the beef meat for fish and fish products. The coatings of 8% gelatin/chitosan in a ratio
with gelatin-henna extract and reported a decreased level of protein and of 3:1 incorporated with clove oil (7.5%) (Socaciu, Semeniuc, & Vodnar,
lipid oxidation, and lower weight loss in the coated samples. Addition­ 2018) and coatings of 1%, 1.5%, and 2% chitosan increases the shelf life
ally, Rasul, Asdagh, Pirsa, Ghazanfarirad, and Sani (2022) reported of fish fillets by 6 days. Song, Lee, Al Mijan, and Song (2014) reported a
enhanced storage life of minced meat coated in gelatin-chickpea protein reduction in TABRS (28%), peroxide value (36%) and reduction in E.coli
coating with incorporated nanoparticles. Gallego, Arnal, Talens, Toldrá, and Salmonella count of smoked salmon packaged in chicken gelatin film
and Mora (2020) reported enhanced storage life of pork meat coated with incorporated clove oil. Nessianpour, Khodanazary, & Hosseini
with gelatin-tomato byproduct coating. Wulandari, Erwanto, Pranoto, (2019) also reported that gelatin coatings with propolis extract extended
Rusman, and Sugiyanto (2020), reported lower weight loss, retention of the shelf life of Saurida tumbil fillet by approximately 4 days by reduction
pH, color, and enhanced shelf life of chicken sausages packaged in of TABRS and enhancing sensory quality.
gelatin-soy protein film with transglutaminase as crosslinker.
4.5. Probiotic encapsulation
4.3. Fruits coating/packaging
In food industries, microencapsulation has numerous applications
Fruits and vegetables are highly perishable commodities, as 80–90% such as core material stabilization, oxidative reaction control, the tem­
of water needs proper attention during storage. Most quality and poral and time-controlled release of substances, flavor, color or odor
quantity losses of fresh vegetables and fruits occur between the har­ masking, shelf-life extension, and protection of the components against
vesting and consumption. To prevent quality and quantity changes in nutrient loss. Various food-grade polymers are used in microbial
fruits and vegetables, two main techniques, modified atmosphere stor­ encapsulation, such as gelatin, pectin, carrageenan, chitosan, alginate,
age and controlled atmosphere storage, have been used (Rajapaksha, and CMC (carboxymethyl cellulose) (Riaz and Masud, 2013). Probiotic

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J.A. Rather et al. Food Packaging and Shelf Life 34 (2022) 100945

bacterial cells are most commonly encapsulated by spray drying, gelling properties of mammalian gelatin are 28–31 ◦ C, 100–300 bloom,
emulsion, and extrusion methods. These bacteria get entrapped in a gel and 20–25 ◦ C, respectively, while that of fish gelatin is 11–28 ◦ C,
matrix (Riaz & Masud, 2013; Solanki et al., 2013). Due to its thermor­ 70–270 bloom, and 8–25 ◦ C, respectively. The gelatin in food products is
eversible and amphoteric nature, gelatin is an excellent encapsulating usually chosen for gelling, rheological, chemical, surface-active prop­
agent mixed with polysaccharides such as gellan gum. These poly­ erties, and packaging properties, so modification of gelatin is of greater
saccharides have a net negative charge, repel each other, and are importance to improving these properties. Table 3 summarizes some
miscible at pH above 6, while gelatin has a positive at pH below the methods of gelatin modification for improving the properties of
isoelectric point, and hence it has a strong attraction with negatively films/coatings. Various methods of gelatin modification are as under:
charged hydrocolloids. Gelatin at a higher concentration (24% w/v)
encapsulates lactic acid bacteria when cross-linking with toluene-2, 5.1. Enzymatic modification
4-diisocyanate is used to produce biomass (Huq, Khan, Khan, Riedl &
Lacroix, 2013). de Almeida Paula, Martins, de Almeida Costa, de Oli­ Enzymes such as transglutaminase, tyrosinases, and laccase improve
veira, de Oliveira, and Ramos (2019) encapsulated Lactobacillus Plan­ the techno-functional properties. Compared to tyrosinases and laccase,
tarum with gelatin-alginate coating solution and showed that 1% gelatin, transglutaminase is used to improve gelling and rheological properties
and 0.1% alginate showed a higher amount of viable cells (4.2 ×109 of the gelatin (Bode, Da Silva, Drake, Ross-Murphy & Dreiss, 2011; T.
CFU/g). Albadran, Monteagudo-Mera, Khutoryanskiy, and Char­ Huang et al., 2017). Transglutaminase modification of gelatin results in
alampopoulos (2020), also reported encapsulation of Lactobacillus the development of ε-(γ-glutamyl)-lysine (G-L) cross-links by three steps,
Plantarum in chitosan-gelatin and gel protected the Lactobacillus Plan­ namely acyl transfer, cross-linking and deamidation reactions (Savoca,
tarum for 2 hrs in simulated gastric fluid (pH 2). Sengsaengthong & Tonoli, Atobatele & Verderio, 2018). Transglutaminase from microbes
Oonsivilai, (2019), reported microencapsulation of Lactobacillus sp. results in acyl transmission between ɤ-carboxamide group of the peptide
21C2–10 using gelatin-maltodextrin as wall material and incorporated with glutamine residue and various other primary amines. Covalent
in ice cream showed no significant effect on ice cream sensorial prop­ bond formation occurs between a ε-amino group of lysine (acyl
erties. The exposure of encapsulated probiotics in ice cream was simu­ acceptor) and gelatin (G-L bond). This covalent bond G-L is formed
lated to gastro-intestinal juices (pH 2) for 5 h. The ice cream with between intra and intermolecular cross-links. By forming these isopep­
encapsulated cells showed higher probiotic survival than ice cream with tide bonds, protein structure changes and results in stable and robust
free probiotic cells. network formation, improving viscosity, solubility, gelation, and
emulsification properties of gelatin. Water acts as an acyl receptor in the
4.6. Other applications deamination process, and deamination of glutamine results in charge
changing and solubility of gelatin (Gaspar & de Góes-Favoni, 2015). The
Gelatin has wide applications in various types of food products. appropriate enzyme concentration is used to modify gelatin, as
Gelatin gels melt at a lower temperature than body temperature, making increased concentrations result in hardening of gel and lower strength
gelatin a more favorable food component than other gelling agents due to inhibition of uniform network. Non-thermal reversibility also
(Abedinia et al., 2020). In a few parts of the world, water dessert gels are results from using higher concentrations of transglutaminase in gelatin
made of carrageenan gum and do not liquefy in the mouth, so they are to modification (Wu, Liao, Zhang & Chen, 2019). Microbial trans­
be chewed. Although both gelatin and carrageenan-made gels are called glutaminase modification of gelatin improves textural properties like
water dessert gels, they vary in sensory attributes. In the dairy industry, elasticity, cohesiveness, and adhesiveness. This dense and ordered
gelatin acts as a stabilizer and modifies the texture of dairy products. structure also depends on gelatin’s incubation time and temperature
Gelatin has applications in ice cream, yogurt, and other dairy products. during the modification process. The effect of transglutaminase (TG) and
In yogurt, gelatin is used to diminish syneresis and raise firmness. The pectin on the microstructure of fish gelatin gels are shown in Fig. 3.
gelatin is companionable with milk proteins, not masking the product’s (Huang et al., 2017) concluded that fish gelatin films exhibit a loose
flavor compared to other gums, improving the sensory quality of foods. network in microstructures, with modification, show enhanced network
Food processors obtain broad ranges of textures in foods by using diverse structures due to covalent bond formation and substantial aggregations.
concentrations of gelatin. In confectionery products like marshmallows Increased TG enhances these networks and hence results in good barrier
and soft gummy-type candies, gelatin is an essential ingredient. The properties of the films. Compared to control gelatin, incorporating fish
gelatin is the main ingredient in these confectionery products and is used gelatin with pectin enhances networks and fish gelatin properties. TG
in 3% concentration and acts as a stabilizer and whipping agent (Boran increases linkage, improves mechanical strength, reduces moisture and
& Regenstein, 2010). A significant proportion of gelatin in the medical UV light sensitivity, and reduces film solubility (Q. Luo et al., 2022).
industry is used in pastilles, tablets, and capsules (Chakka et al., 2017).
The main use of gelatin in the beverage industry is for clarification 5.2. Chemical modification
and sedimentation. Gelatin induces clearness of suspended beverage
particles and stabilizes this clearness by partial or complete flocculation The functional properties of protein and polysaccharides-based films
and sedimentation of particles in suspension. The gelatin for this pur­ can be enhanced by applying various treatments such as chemical cross-
pose is used in beverages containing tannin substances, as gelatin reacts linking, phosphorylation, and various natural phenolic substances. For
with tannins and forms complexes. In bakery industries, gelatin acts as a enhancement in the technological properties of proteins, phosphoryla­
setting and stabilizing agent or foam-producing material in bread and tion has played an important role (Z. Xiong, Zhang, & Ma, 2016).
cakes, and in icings, gelatin is used as a stabilizer (Widyasari & Raw­ Polysaccharides and hydrocolloids are also modified to enhance func­
dkuen, 2014). tional roles (Shukri & Shi, 2017). Various chemical agents are used to
phosphorylating proteins to enhance functional properties (Lili, Huan,
5. Modification of gelatin for enhancing packaging properties Guangyue, Xu, Dan & Guangjun, 2015). Through the phosphorylation
reaction, hydroxyl groups of proteins get attached to the phosphate
The main technological properties of gelatin are viscosity, bloom group, resulting in improved functional properties of films. The addition
strength, and melting temperature. These properties depend on gelatin of phosphates to the gelatin improves the emulsion stability by pro­
composition, molecular weight, the ratio of α- and β-chains of gelatin, moting hydrophobic interaction at the interface and surface of oil
bloom or gel strength, and viscosity, affecting the fibrogenic properties droplets (Z. Xiong et al., 2016). Hence the introduction of phosphate
of films (da Trindade Alfaro, Balbinot, Weber, Tonial & groups to gelatin improves its emulsification properties.
Machado-Lunkes, 2015). The melting temperature, bloom strength, and At this stage of development, the information regarding the impact of

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J.A. Rather et al. Food Packaging and Shelf Life 34 (2022) 100945

Table 3
Methods of gelatin modification and improvement in properties of films/coatings.
Modification Functional ingredient Applications References

Chemical/physical Chitosan and ZnO Antimicrobial (Z.Liu, Lv, Li & Zeng, 2016)
Aloe vera extract Antimicrobial (Radi et al. 2017)
Black and green tea extract Antioxidant (Radi et al., 2017)
Beeswax and Aloe vera Enhance barrier properties/antioxidant (Mudannayaka, Rajapaksha, & Kodithuwakku, 2016)
Borage extract Enhance barrier properties/antioxidant (Gómez-Estaca, López de Lacey, Gómez-Guillén, López-Caballero
& Montero, 2009)
Sweet basil and lemongrass extract Thermal strength/higher gel strength (Yasin, Babji, & Norrakiah, 2017)
Aloe vera and green tea extract Antioxidant (Amiri, Akhavan, Radi & Branch, 2017)
Seaweed extract Improves mechanical properties (Rattaya, Benjakul, & Prodpran, 2009)
Glutaraldehyde Improves mechanical/thermal properties (Bigi, Cojazzi, Panzavolta, Rubini & Roveri, 2001)
Tea polyphenols Antioxidant (Liu et al., 2015)
Epigallocatchin gallate Antioxidant/enhance mechanical and barrier (Nilsuwan, Benjakul, Prodpran & de la Caba, 2019)
properties
Laurel oil Antimicrobial (Alparslan et al. 2014)
Oregano oil Antimicrobial (Kazemi & Rezaei, 2015)
Physical Rice flour Enhance barrier properties (Soo & Sarbon, 2018)

Ammonium sulphate Increase/decrease strength(concentration (Sha et al., 2014)

Dependent)
Enzymatic Transglutaminase Improve barrier/mechanical properties (Lim, Mine, & Tung, 1999)
modification Transglutaminase Improve barrier/mechanical properties
Enzymatic/ Transglutaminase/gly oxal/ Improve barrier and mechanical properties (De Carvalho & Grosso, 2004)
chemical formaldehyde

Fig. 3. Microstructures of unmodified/modified gelatin gels with different concentrations of trans gultaminase and pectin (Huang et al., 2017).

different phosphorylation methods on the gel properties of gelatin is gelatin chains, enhancing its film-forming properties (Benbettaïeb, Gay,
scarce. So further research is needed to know the actual size and extent Karbowiak, & Debeaufort, 2016; Azeredo and Waldron, 2016). Adjacent
of phosphorylation at every site on gelatin. Various factors govern the residues of amino acids such as ε-NH2 of hydroxylysine and lysine
phosphate linkage nature, such as the concentration of phosphates, pH, groups react with glutaraldehyde, forming similar bonds like Schiff base,
and reaction time. The introduction of excess phosphates increases hence increasing water resistance and strength of the structure formed
repulsive forces with protein molecules and hence lowers gel strength, (Farris, Song, & Huang, 2010).
hence poor packaging properties. Gelatin chains aggregate to form large Nowadays, phenolic substances like ferulic acid, caffeic acid, tannic
bundles that disturb the configuration of uniform fine gel networks due acid, and rutin have been exploited to alter the properties of gelatin and
to long-time phosphorylation. There is acceleration in accessible OH and increase antibacterial properties (Bouarab Chibane, Degraeve, Ferhout,
NH2 groups on gelatin chains during alkaline conditions to react with Bouajila & Oulahal, 2019). The OH group of phenolics interacts with
phosphate groups. Various chemical cross-linking agents are utilized to COO groups of gelatin molecules by hydrogen bonding. Hydrophobic
modify gelatin and other proteins, but aldehydic agents show greater interactions result in hydrophobic gelatin side chains and phenolic ar­
efficiency by improving various properties such as mechanical, thermal, omatic rings, resulting in reduced barrier properties of films (Kaewdang
and moisture resistance by introducing covalent bonds among gelatin & Benjakul, 2015). Rutin and gallic acid enhance thermal stability and
chains (Skopinska-Wisniewska, Tuszynska, & Olewnik-Kruszkowska, gel strength but diminish swelling properties (Yan, Li, Zhao & Yi, 2011).
2021). Formaldehyde easily migrates between gelatin chains and Gelatin modified with rutin shows thermal stability and viscoelastic
forms new covalent bonds with lysine, cysteine, and histidine groups on modulus but lower swelling with higher cross-link networks. This is

10
J.A. Rather et al. Food Packaging and Shelf Life 34 (2022) 100945

because of higher binding sites in xerogels. However, increased phenolic enhance the antioxidant properties of the developed films.
concentration decreases gelation property because of more likely
interaction with gelatin as aggregates leading to disordered structure
5.3. Physical modifications
(Kaewdang & Benjakul, 2015). One more important property of phe­
nolics is that they increase gelatin protein’s antioxidant and emulsifying
The simplest and most commonly used method of gelatin modifica­
capacity (Haddar, Sellimi, Ghannouchi, Alvarez, Nasri & Bougatef,
tion is the physical method in which electrolytic and non-electrolytic
2012). Thus phenolic substances incorporated in gelatin films can
solutes are used. Salts are common electrolytic solutes that have been

Fig. 4. Schematic diagram depicting the modification of fish gelatin (FG). FGG (FG + 0.040% GE), FGG+ (FG + 0.025% GE + 3 mM CaCl2), FGK (FG + 0.20%KC)
and FGK+ (FG + 0.18% KC + 5 mM KCl). PG: Pork gelatin; FG: Fish gelatin; GE: Low acyl-gellan; KC: κ-carrageenan (Sow et al., 2018).

11
J.A. Rather et al. Food Packaging and Shelf Life 34 (2022) 100945

used for modification for a long time. According to Sow & Yang (2015), CRediT authorship contribution statement
salts affect gelatin protein by modifying electrostatic forces and salt
bridge formation. Karayannakidis and Zotos, (2015) observed that salts Jahangir A. Rather: Conceptualization, Methodology, Writing –
like calcium chloride, magnesium chloride, and NaH2PO4 improve the original draft. Najmeenah Akhter: Writing – original draft. Qazi
melting point and strength of gel fish gelatin, and a higher concentration Showkat Ashraf: Methodology. Shabir A. Mir: Methodology, Writing –
(0.5 mol/L) of NaH2PO4 shows higher efficiency. The positive and original draft, Writing – review & editing. Hilal A. Makroo: Concep­
negative ion salts affect gel properties depending on the composition of tualization, Methodology, Supervision, Writing – review & editing.
gelatin, salt type, and conditions of experimentation (Masuelli & San­ Darakshan Majid: Conceptualization, Supervision, Writing – review &
sone, 2012). Amino acid hydroxyl groups form coordinate links with editing. Francisco J. Barba: Supervision, Writing – review & editing.
Mg2+, so they promotes ordered triple helical structure and hence effi­ Amin Mousavi Khaneghah: Supervision, Writing – review & editing. B.
cient mechanical and physical properties of films. Due to higher hy­ N. Dar: Conceptualization, Methodology, Writing – original draft, Su­
droxyproline content in tilapia skin gelatin than megrim skin gelatin, pervision, Writing – review & editing
tilapia fish gelatin with MgSO4 has higher temperatures of melting and
gelation. Sow and Yang (2015) reported that larger monovalent aniocs Submission declaration
such as chloride anions hinder hydrogen bond formation and interfere
with hydrophobic interactions. There is a melting and gelation tem­ This paper has not been submitted to any other journal for
perature decrease when gelatin is treated with (NH4)2SO4 at higher pH publication.
(10).
Sugars, polysaccharides, and glycerol as non-electrolytes also
Conflict of interest
improve the functional characteristics of gelatin (Sow, Kong, & Yang,
2018) by enhancing cross-linking, as shown in Fig. 4. There are
There is no conflict among authors or any other agency and authors
hydrogen and electrostatic interactions between
agreed to publish in Food Packaging and Shelf life.
protein-polysaccharide, which contribute to improvement in gelation
and rheology properties. Higher the crosslinking, efficiency will be the
Data Availability
barrier and mechanical properties of the films. Other factors affecting
gelatin-polysaccharide systems’ properties are molecular characteristics
The authors do not have permission to share data.
and mixing conditions of complex systems. Sow, Peh, Pekerti, Fu, Ban­
sal, and Yang (2017) observed that calcium chloride and gellan gum
break the balance among attraction and repulsion forces in the Acknowledgement
gellan-gelatin system, and its nanostructure changes, resulting in the
development of hydrogen bonds among –NH gelatin groups and –COO All the authors extended their gratitude to the Department of Food
and –OH groups of gellan gum. The introduction of gelatin with pectin Technology, IUST Kashmir, for providing the necessary facilities to
and xylitol increases gelation properties by forming hydrogen bonds (T. conduct the present work.
Huang et al., 2017). Thus, incorporating other crosslinking agents like
polysaccharides, salts, and sugars improves gelatin packaging Ethical guidelines
properties.
Ethics approval was not required for this paper.
6. Conclusions
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