International Journal of Biological Macromolecules 254 (2024) 128037

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International Journal of Biological Macromolecules

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

Review

Collagen and gelatin: Structure, properties, and applications in

food industry
Muhammad Ijaz Ahmad a, Yonghui Li b, Jinfeng Pan c, Fei Liu d, Hongjie Dai e, Yu Fu e,
Tao Huang f, Shahzad Farooq a, Hui Zhang a, *
a
College of Biosystems Engineering and Food Science, Zhejiang Key Laboratory for Agro-Food Processing, Zhejiang University, Hangzhou 310058, China
b
Department of Grain Science and Industry, Kansas State University, Manhattan, KS 66506, USA
c
National Engineering Research Centre for Seafood, Collaborative Innovation Centre of Provincial and Ministerial Co-construction for Seafood Deep Processing, Liaoning
Province Collaborative Innovation Centre for Marine Food Deep Processing, Dalian Polytechnic University, Dalian 116034, China
d
State Key Laboratory of Food Science and Technology, Science Center for Future Foods, Jiangnan University, School of Food Science and Technology, International Joint
Laboratory on Food Safety, Wuxi 214122, China
e
College of Food Science, Southwest University, Chongqing 400715, China
f
College of Food and Pharmaceutical Sciences, Ningbo University, Ningbo, Zhejiang 315800, China

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

Keywords: Food-producing animals have the highest concentration of collagen in their extracellular matrix. Collagen and
Collagen gelatin are widely used in food industry due to their specific structural, physicochemical, and biochemical
Gelatin properties, which enable them to improve health and nutritional value as well as to increase the stability,
Fibers
consistency, and elasticity of food products. This paper reviews the structural and functional properties including
Food packaging
Food additive
inherent self-assembly, gel forming, water-retaining, emulsifying, foaming, and thickening properties of collagen
Colloid structure and gelatin. Then the colloid structures formed by collagen such as emulsions, films or coatings, and fibers are
Functional properties summarized. Finally, the potential applications of collagen and gelatin in muscle foods, dairy products, con­
fectionary and dessert, and beverage products are also reviewed. The objective of this review is to provide the
current market value, progress as well as applications of collagen and its derivatives in food industry.

1. Introduction properties can be classified into two categories: first, the properties
linked with their gelling behavior, such as water binding capacity, gel
Collagen is one of the most ubiquitous and abundant protein found in formation, thickening, and texturizing of collagen; second, the proper­
all animal bones and skin, accounting for about 30 % of the total protein ties associated with surface behavior, such as film-forming, protective
content [1]. Blood vessels, tendons, cartilage, bone and animal skin are colloid function, adhesion and cohesion, stabilization, foam formation,
all composed of collagen [2]. The basement membranes and extracel­ and emulsion [6]. Recently, collagen has been widely used in agricul­
lular matrix are formed through their fibrillar and microfibrillar net­ tural, tissue engineering, biomedical, cosmetic, pharmaceutical, and
works. Connective tissues such as skin, tendon, cartilage, and bone food industries due to its excellent degradability and biological
contain fibrillar protein [3]. In addition, the structure and stability of compatibility [8,9]. Collagen can form stable and durable fibers due to
various organs and tissues are enhanced by high tensile and stable its ability to crosslink and self-aggregate, making it ideal for use in drug
insoluble fibrils of collagen [4]. The collagen and gelatin market value delivery systems [10,11]. Additionally, the natural properties of
exceeded ~4.7 billion USD in 2020, of which 80 % are used by the collagen make it suitable for use in pharmacology and medicine,
health and food industries, and it is estimated to grow over ~7 billion including biodegradability, hemostatic activity, and low allergenicity
USD by 2027 [5]. with high biocompatibility and antigenicity [12].
Collagen and gelatin can be used for the development of functional A considerable number of collagen molecules can be self-assembled
foods and to improve the quality of processed foods [6]. According to into highly diverse shapes with intact triple-helical structures under
Gómez-Guillén, Giménez, López-Caballero and Montero [7], collagen certain conditions [10]. The covalent and hydrogen bonds stabilizing

* Corresponding author.
E-mail address: hubert0513@zju.edu.cn (H. Zhang).

https://doi.org/10.1016/j.ijbiomac.2023.128037
Received 23 September 2023; Received in revised form 1 November 2023; Accepted 9 November 2023
Available online 12 November 2023
0141-8130/© 2023 Elsevier B.V. All rights reserved.
M.I. Ahmad et al. International Journal of Biological Macromolecules 254 (2024) 128037

the collagen triple helix are broken during the extraction process, show greater bioavailability and digestibility compared with collagen or
resulting in a polypeptide mixture called gelatin, i.e., collagen partially gelatin [8].
degrades to form gelatin [13]. Film forming, foaming, emulsifying, and To fully exploit the application potential of collagen and gelatin in
gelling are all associated with the functional properties of collagen and food industry, it is essential to understand their basic structure, appli­
gelatin [7,14]. These properties make them suitable for use as a wide cation features, and key functional properties. In this review, the recent
range of food products, or edible packaging materials [12,15]. Edible research regarding the structure, functional properties, as well as cur­
packaging materials, including those based on collagen, have emerged rent applications in food industry of collagen and gelatin are summa­
as an essential component of the global food industry [16]. The unique rized, expecting to provide a detailed understanding of their
nature of their creation, often derived from hide or pig skins, offer characteristics and applications in food industry.
remarkable in their ability to act as systems of delivery, underpinned by
enhanced barrier and mechanical properties, augmenting the protection 2. Structure of collagen and gelatin
of food products. Their functionality is not just limited to preserving
freshness but also extends to manipulating sensory experiences. For 2.1. Structure of collagen
instance, the control-release of active ingredients can enhance flavors
while also offers nutritional benefits. Moreover, sausages are often In 1954, Ramachandran and Karta proposed the structure of
produced with collagen casings, which is an edible film. Compared to collagen, which led to a better understanding of collagen structural and
pork casings, collagen casings significantly reduced biogenic amines functional properties [25]. Even though different types of collagen differ
produced during fermentation, improving the quality characteristics of significantly in distribution, function, and size within tissues [26], the
sausages [17]. Added functionality, such as antimicrobial properties, general structure of collagen is characterized by a triple helix that ex­
can also be conferred with collagen casings [18]. The co-extrusion of tends from the middle and is usually composed of three parallel
sausage casing entails the involvement of collagen and alginate, two α-chains, each presenting a left-handed conformation similar to poly­
resources that serve to solidify the shape of sausage immediately after proline II (PPII) (Fig. 1) [27,28]. A non-fibrillar collagen molecule is
extrusion process [19]. Although both materials have their advantages known as tropocollagen [29]. Over 1000 amino acids are present in the
and disadvantages, collagen capability of imparting a superior snap is mature fibrillar collagen, including short telopeptides at each end that
noteworthy. Still, it does necessitate a higher investment for fiber play a critical role in binding to the matrix [10]. The triple helix of non-
alignment to emulate natural casing. Recently, Suurs, van den Brand, ten fibrillar collagens contains imperfections (one or three residues) or in­
Have, Daamen and Barbut [20] produced co-extrusion sausage casing terruptions (containing large numbers of residues) [28]. Moreover,
using cattle skin collagen with enhanced viscoelastic and mechanical many collagen molecules contain repeating amino acid motifs as part of
properties. A variety of benefits can also be derived from collagen their structure, where pro and 4-Hyp often occupy X and Y in Gly-X-Y,
consumption, including improved skin health [21], and alleviating the respectively. Triple helix of collagen is centered on every third amino
risk of cardiovascular diseases [22,23]. Additionally, collagen and acid residue, so the primary structure of the three positions is occupied
gelatin release bioactive peptides encoded in their sequences during the by the smallest amino acid, Gly [30]. Moreover, collagen folds more
digestion process of food products in the gastrointestinal tract [24]. efficiently when Hyp and Pro residues are abundant, since the hy­
Moreover, peptides prepared from a variety of animal by-products can droxyproline and proline sequences are pre-arranged into a PPII
be facilitated by low molecular weight collagen hydrolysates, which conformation, thereby reducing the entropic cost. For collagen triple

Fig. 1. The triple helix structure (A) of collagen with the three α-chains depicted in cartoon and partial stick representation (PDB code 1CAG). B shows a repeating
region of the Gly-X-Y motif in the black box in A, and the interchain hydrogen bonds are labeled with a dashed line in black. Reproduced with permission from
reference [27].

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helix stability, amino groups of Gly residues form hydrogen bonds with denatures, which results in the formation of triple helical structures
carboxyl groups of adjacent residues at the X position. Also, the ster­ [39]. By adjusting the temperature above its critical gel temperature,
eoelectronic effect stabilizes the collagen triple helix at 4-Hyp in the Y gelatin gels can change from gel to sol, which is a cold setting and
position [31]. Proteins encoded by collagen mRNA become protein thermo-reversible gel [40]. For gelatin, gel formation is a result of
chains at the ribosomes through translation. The lumen of the endo­ collagen-like triple helices from randomly coiling polypeptide chains
plasmic reticulum undergoes post-translational modifications (such as (Table 1). A triple helix region called a junction zone formed, when
glycosylation and hydroxylation) of the procollagen α-chains by different chains intertwine with each other upon cooling [41]. Then the
removal of the N-terminal signal peptide [32]. The catalysis of protein collagen-like triple helical structure of gelatin molecules partially re­
disulfide isomerase takes place at the C-terminal domains of α-chains of verts. In addition to hydrogen bonds, electrostatic and hydrophobic
disulfide bonds to modified procollagen α-chains align during the pro­ interactions have also been found to play an important role in stabilizing
cess of triple helix formation. Then a procollagen molecule is formed as a these triple helix [38].
result of α-chains triple helix extension from the C to the N-terminus
[10]. 3. Properties of collagen and gelatin
The cleavage of procollagen C-proteinase (PCP) and procollagen N-
proteinase (PNP), which are known as biological restrictive enzymes, 3.1. Self-assembly
leads to the formation of tropocollagen molecules (~1.5 nm in width
and ~ 295 nm in length) secreted in the extracellular matrix of pro­ Collagen has the inherent ability to self-assemble. A type I collagen
collagen molecules [33]. The N-propeptide of type I procollagen is fiber bundle can be formed in vivo by self-assembling into microfibrils
cleaved by PCP between Asp and Ala sites, whereas PNP cleaves between and subsequently into fibrils, which can be organized in different ways
Ala-Gln and Pro-Gln. PCP belongs to the Tolloid-like proteinases/bone according to organs and tissues [51]. In vitro, fibrils with the charac­
morphogenetic protein-1 (BMP-1) family, while PNP is classified as a teristic D-periodicity can also form spontaneously and orderly from
metalloproteinase and disintegrin with thrombospondin motifs collagen molecules that contain intact triple-helical domain [52]. There
(ADAMTS) [34]. In collagen microfibrils, tropocollagen molecules are is a great deal of similarity between the in vivo and in vitro structure of
longitudinally integrated after the N-/C- propeptides are enzymatically the fibrils. Collagen can self-assemble into sponges, gels, and fibrils
removed [13]. Upon interdigitating, collagen fibrils are formed by depending on the environmental conditions. Self-assembled aggregates
crosslinking the microfibrils. Ligaments and tendons are structurally are characterized by their distinct multi-hierarchical organization that
based on collagen fibers, which are made up of fibrils and proteoglycans contributes both to their biological and physical properties (Fig. 2)
[35]. [27,53].
Collagen self-assembles through nucleation growth, i.e., several
2.2. Structure of gelatin collagen molecules are gathered together to form cores, which are then
transformed into mature fibrils [54]. A two-phase kinetic process is
Gelatin with molecular weights ranging from 15 to 250 kDa is pro­ involved with the self-assembly, namely, the growth of nucleus center,
duced by partial hydrolysis of collagen [36]. It is possible to have two and the formation of nucleus center [55]. The typical process of collagen
types of gelatin, called type A and B, depending on the pre-treatment self-assembly includes a lag phase (cores are formed following the ag­
procedures, such as acid or alkaline pretreatment conditions. The pro­ gregation of monomer molecules), a growth phase (fibrils are formed
duction of gelatin also involves enzyme pre-treatment that targets spe­ when cores grow in length and diameter), and a linear plateau phase
cific labile peptide bonds [37]. In the final gelatin product, polypeptides (saturation of fibrils) [56]. Gisbert, Benaglia, Uhlig, Proksch and Garcia
of different conformations and sizes appear due to the combination of [2] used a high-speed biomodal atomic force microscope (AFM) to
different pre-treatment and extraction procedures. It may consist of recognize the four stages of collagen self-assembly: (1) a collagen pre­
higher molecular weights fractions, e.g., γ-chains (covalently linked cursor is nucleated, (2) grows into tropocollagen molecules, (3) then
α-chain trimmers), β-chains (covalently linked α-chains dimers), and assembles into microfibers, (4) and finally the formation of
microgels with very higher orders [38]. A gelatin molecule contains the microribbons.
same amino acids as collagen molecules, since gelatin is derived from Collagen self-assembly may be affected by a variety of factors [56].
collagen that has been denatured. The deamination of glutamine and The concentration [55], extraction method [57], and source [58] can
asparagine occurs when collagen is hydrolyzed into gelatin. During the have a significant impact on the self-assembly of collagen. Ultrasonic
manufacturing process of gelatin, collagen loses its native structure and treatment, phytic acid, sulfonated chitosan, molecular chirality, amino

Table 1
Differences between collagen and gelatin properties.
Property Collagen Gelatin References

Origin Animals/ humans Collagen from bones/ skin [42,43]

Precursor Fibroblast Collagen type 1 [44]
Peptide structure Triple helix of polypeptide chain Small peptides [44]
Number of amino Approximately 1050 <20 [7]
acids
Types Fibril-forming and non-fibril forming A and B [44]
Aromatic radicals Present Absent [45]
Physical Elastic, tough and versatile structural protein Smooth and gel-like substances [7]
characteristics
Solubility NaCl solution/ dilute acid H2O [7]
Mechanical strength Poor Poor [46]
Gelling properties No Yes [7]
In vitro degradation Serine protease, pepsin cleaving enzyme, gelatinease and collagenase Collagenase [47,48]
In vivo degradation Endopeptidase MMP-2 and MMP-9 [47]
Digestion Difficult Easy [49]
Protease Resistant Susceptible [50]
Usage Burns, hemostasis, tissue defects, regeneration of nerves, wound dressings, artificial dermis Adhesive of soft tissues, artificial skin, wound [47]
skin replacement dressings

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M.I. Ahmad et al. International Journal of Biological Macromolecules 254 (2024) 128037

Fig. 2. Schematic diagram of the biosynthesis process of collagen and collagen fiber in vivo. P4H: prolyl 4-hydroxylase; P3H: prolyl 3-hydroxylase; ADAMTES: a-
disintegrin-and-metalloproteinase-with-thrombospondin-like-motifs family; BMP1: bone morphogenetic protein. Reproduced with permission from reference [27].

acid composition, ionic conditions, pH, and temperature are the external linked through polypeptide chains [39]. Above setting temperature, the
factors that affects the self-assembly of collagen molecules [59,60]. gelatin solution appears as sol and these polypeptide chains are random
Electrostatic interactions, hydrophobic interactions, and hydrogen coils. However, upon cooling, some of the chains intertwine to form
bonding may modify the kinetics of self-assembly, as well as the struc­ partially ordered collagen-like triple helical structures, resulting in a gel
ture and properties of the self-assembled aggregates [61]. For example, network [41]. Particularly, gelatin can form a thermal-reversible gel
as the temperature increases (20–37 ◦ C), collagen transforms from a with a gel-melting temperature < 37 ◦ C. This feature provides a melt-in-
hydration-rich PPII structure to an ordered sheet structure, which pro­ the-mouth property, which can provide a fat-like sense to food, offering
motes the self-assembly of collagen molecules and enhances hydro­ innovative product development opportunities [8]. This enables the
phobic effects [53]. A pH closer to the isoelectric point will allow application of gelatin in gel foods, e.g., surimi products, sausages, aspic
collagen molecules to self-assemble more readily, which reduces the products, confectionaries, etc. [63,64]. Besides, soluble collagen and
electrostatic repulsion leading to faster collagen intermolecular in­ gelatin usually show good water binding capacity, which makes them
teractions as the net charge of the protein decreases [62]. suitable for keeping juiciness and reducing drip loss in frozen muscle
products [65,66]. Viscosity is another important property of gelatin.
3.2. Gel forming, water retaining, and thickening ability Combined with other hydrocolloids, gelatin can be applied as a thick­
ener in dressing, yogurt and beverage for satisfactory sensory properties
The complete native structure of collagen is destroyed during the [67]. Recently, it has been used for developing 3D printing foods. The
processing of gelatin, but the resulting fragments still keep partially gelatin solution above its gelling temperature is easy to push into the

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M.I. Ahmad et al. International Journal of Biological Macromolecules 254 (2024) 128037

nozzle, and form a stable gel in a circumstance with a temperature lower to enhance the emulsion stability for food applications [15,83]. Dey,
than a gelling point after printing out from the nozzle, showing an Kadharbasha, Bajaj, Das, Chakraborty, Bhat and Banerjee [83] obtained
excellent printing capacity [68]. two collagen hydrolysates (CH) with higher surface activity from Pacu
skin and Tilapia bones by screening seven fish processing by-products.
3.3. Emulsifying and foaming ability Santana, Perrechil, Sato and Cunha [15] evaluated the emulsifying
properties of collagen fibers under different conditions of pH, protein
As a polymer with charged and amphiphilic groups, gelatin shows content and type of emulsification device. At a low pH value (3.5), the
active surface behaviors, especially emulsifying and foaming properties. electrostatic interactions were responsible for the emulsion stability,
Intact collagen is an ineffective emulsifier, but acid-/pepsin-soluble while steric hindrance and interface film dominated the emulsion sta­
collagen containing sufficient hydrophilic and hydrophobic amino acid bility at higher pH values (4.5–7.5).
residues, which can absorb oil-water interfaces and promote emulsion Despite the impressive emulsifying ability of gelatin, it is still
formation by lowering interfacial tension [69]. The electrostatic repul­ considered to be a relatively weak emulsifier compared to other surface-
sion could prevent the aggregation of emulsion droplets. Meanwhile, active biopolymers such as globular proteins and gum Arabic [84,85].
emulsion stability is also improved by gel formation and viscosity of Thus, some strategies have been used to improve the stability of gelatin
gelatin. Thus, the treated collagen or gelatin has been commonly applied emulsions. Feng, Dai, Ma, Fu, Yu, Zhu, Wang, Sun, Tan and Zhang [84]
in emulsified muscle foods, such as patty, sausage, and surimi products investigated the effect of three drying methods (hot air, freeze and spray
[66,70,71]. Gelatin and soluble collagen can exhibit fairly good foaming drying) on the solubility and amphiphilicity of gelatin, and found that
properties, which are mainly attributed to their capacity of reducing the the spray dried gelatin had a better amphiphilicity (92.48◦ ) which is
surface tension at liquid-air interface. Moreover, gelatin can form a beneficial for stabilizing emulsions. Zhang, Sun, Ding, Li, Tao, Wang and
three-dimensional network to increase the continuous phase, which Zhong [85] found that the emulsion stabilized by bovine bone gelatin
could stabilize foams. Therefore, gelatin has been used for the manu­ was more stable than commercial cold-water fish skin gelatin, due to the
facture of aerated confectionaries, like marshmallows or soft gel candies differences in secondary structures and thickness of gelatin film-like
[72] [73], and for improving the texture and structure of ice cream [74] nanostructures. Additionally, the gelatin emulsion stabilization has
and bakery products [75]. been proven to be affected by different extraction methods, which lead
to different protein secondary structure, molecular interaction, and thus
3.4. Stabilizing ability affecting the formed emulsion droplet structure, and emulsion stability
[86].
It is known that the three-dimensional network formed by gelatin
can increase the continuous phase, which can stabilize emulsions and 4.2. Films or coatings
foams [65]. Namely, gelatin is an emulsifier and foamer, but it is an
emulsion- and foam-stabilizer as well. Due to the frequent occurrence of Collagen is a degradable material with suitable film-forming prop­
NH2- and OH-, gelatin can form hydrogen bonds with compounds in erty, and the recent development of film materials for packaging based
food mixtures, which often increases food stability. It has been reported on collagen has been extensively investigated [87]. Collagen can rely on
that gelatin could reduce the formation of sugar crystals and inhibit the a large number of hydrophilic carboxyl and hydroxyl groups on its
relative separation of oil and water in syrup [76]. Syneresis led by surface to form a dense hydrogen bond network, which offers an
temperature fluctuations or pasteurization in yogurt may be inhibited by appropriate template for biologically active cargo. For example, the
gelatin due to its strong water-binding capacity and gel structure [77]. collagen solution mixed with lysozyme can be applied to prepare the
For frozen food, gelatin and its hydrolysates can inhibit the formation of coatings for preserving salmon fillets, in which the formed collagen film
large size ice crystals, which could be helpful for maintaining the quality encapsulates lysozyme to prevent the growth of microorganisms [88]. At
of ice cream and surimi products [78,79]. Additionally, gelatin as a the same time, the dense hydrogen bond network in the coatings can
binder can reduce brittleness, and facilitate molding and cutting during prevent the exchange of gases on both sides to improve the shelf life of
the manufacture of confectionery [76]. fish products [88]. In order to strengthen the physical and chemical
properties of the collagen-based films, bioactive substances have often
3.5. Fining ability been added into the films with specific functions by compounding with
collagen. Song et al. [87] reported that the strong hydrogen bonding
Clarity is an important structural criterion for many liquid foods, between collagen, zein, and gallic acid could lock gallic acid in the
such as beer, wine, and fruit juices. At a pH lower than the isoelectric collagen-zein fibers by electrostatic spinning, thus making the antioxi­
point, gelatin is positively charged. It would react with the negatively dant property of gallic acid effective in the fiber film and significantly
charged polyphenols and anthocyanins in the food matrix by electro­ improving the shelf life of film-packed fish fillets. Besides, collagen can
static interactions to form precipitated complexes that can absorb be utilized as a structural enhancer to improve the film attributes of
turbidity-forming substances, causing them to co-precipitate [80]. other film-forming food-grade macromolecules. Liu et al. [89] reported
Therefore, gelatin has been widely applied as a fining agent to clarify the that the digestible collagen extracted from blue shark skin could
cloud in beer, wine, or fruit juices. significantly boost the fresh-keeping effect of chitosan-based protective
films on fresh red porgy during storage, and the hydrogen bonding be­
4. Colloids structures tween collagen and polysaccharides played an essential role in the film-
forming process.
4.1. Emulsions The applications of many active ingredients in collagen or gelatin-
based composite films have been studied (Table 2), such as 3-phenylace­
The structure formation properties of collagen and gelatin depend on tic acid, pomegranate peel extract, cellulose nanoparticles, and grape
the charged groups in the protein side chains and the partial collagen seed extract, which have been proven to effectively inhibit the oxidation
sequence containing either hydrophilic or hydrophobic amino acids and growth of food-borne pathogens to maintain the quality of foods as
[81]. The amphiphilic nature of this protein results in effective migra­ active packaging materials [90–92]. For example, the pH-sensitive
tion from the water phase to the oil-water interface, and subsequently anthocyanin substance has been reported to be incorporated into the
form an interfacial layer, showing a great potential application in collagen-based films to detect the freshness of meat in real-time through
emulsion systems [82]. the color changes of the films. With the decline in meat quality, the
The emulsifying properties of collagen have attracted much attention surficial pH of meat products changes significantly, as anthocyanin is a

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Table 2 Table 2 (continued )

Application of gelatin/collagen-based films or coatings. Versatile Film/coating materials Findings References
Versatile Film/coating materials Findings References application
application
quality deterioration
Chilled chicken Gelatin-chitosan-3- Effectively inactivated [92] and prolonged the shelf
phenyllactic acid film foodborne pathogens life of fish muscle for at
Staphylococcus aureus least two days.
and Escherichia coli and Mangoes & Collagen- A 28 % less O2 [125]
prolonged the apples galactomannans consumption and 11 %
preservation of chilled coating less CO2 production
chicken to 4 days. were observed in
Shrimp Gelatin-chitosan film Suppressed growth of [90] coated mangoes; the
food borne pathogens CO2 production and the
including P. fluorescens, O2 consumption was
Shewanella putrefaciens, approximately 50 %
Pseudomonas spp., lower in the coated
L. monocytogenes and apples.
lactic acid and flavor Salmon fillets Collagen-lysozyme Significantly improve [88]
for minimum 10 days of coating the preservation quality
refrigerated storage of fresh-salmon fillets,
Pork Chitosan-gelatin Retained normal pH, [91] decreased the TVB-N,
composite film inhibited lipid and reduced the weight loss
incorporated with protein oxidation and and inhibited the
nisin and grape seed retarded microbial growth of bacterial.
extract growth during 20 days Butter and Emulsion-based food Enhance the shelf life of [126]
of cold storage at 4 ◦ C. chocolate stabilization by fish- stored butter and
Bread Pigskin-originated Retardation of the [119] sauce derived collagen chocolate sauce,
gelatin film staling process, hydrolysate increased abundance of
polymer hydroxylated proline
reorganization, and residues to trap water,
altered starch retro- and rapid diffusion to
gradation oil water interface
Citrus wine Delayed-bitterness in Decreased the limonoid [120] Frankfurters Pork back-fat Greater water holding [127]
citrus wine by fining concentration, replacement by capacity, product
agent specially gelatin increased the retention hydrolyzed collagen stability, increased
rate of ascorbic acid, protein content, and
and retained reduced lipid content
antioxidant activity Ice cream Ice crystal growth Short collagen/gelatin [78]
Chocolate Chocolate spread- Satisfactory [121] inhibition in an ice polypeptides in the
spread based fat formulation spreadability, very soft cream mix matrix by molecular mass range
replaced with gelatin and very low hydrolyzed fish gelatin of 1000e2500 Da
consistency inhibited ice crystal
Jelly Honey jelly candies Increased the hardness, [63] growth in frozen
prepared by various adhesiveness, systems, stabilization of
gelatin doses chewiness and the electrostatic and
gumminess values of hydrogen bonding
candies interaction in the
Beef patty Gelatin film Two kinds of films [122] peptide ice crystal
incorporated with the effectively delayed complex
extracts of the plants lipid oxidation and Frozen dough Pigskin collagen Inhibit the ice [128]
Caesalpinia decapetala deterioration of beef hydrolysates recrystallization,
(CD) and Caesalpinia patty quality during protect the gluten
spinosa ‘Tara’ (CS) storage; the CS film was networks
the most effective Surimi Gelatin hydrolysate Enhance surface [116]
antioxidant for the beef from blacktip shark hydrophobicity and
patties (Carcharhinus limbatus) disulfide bond content,
Strawberries Gelatin-mentha Rapidly depressed the [123] and prevent the
pulegium essential oil growth of microflora, denaturation of surimi
(MEO) coating various molds and protein
yeasts, retained pH,
firmness, weight, total
soluble solid and pH-sensitive and easily color-changed antioxidant [93]. In addition,
natural appearance Amaranthus leaf extract can also be incorporated into the films for
>13 days of storages.
detection of fish and chicken quality [94], as it shows a color change
Beef Gelatin-chitosan Significantly reduced [124]
coating weight loss and lipid from red to yellow when pH increases caused by spoilage.
oxidation of the steaks
after 5 days of storage, 4.3. Fibers
and films with higher
gelatin concentrations
were more effective Natively, the formation of collagen and gelatin fibers mainly includes
Tilapia Collagen/zein/gallic The Col/ZN/GA [87] the extraction, acid swelling, molding and drying of collagen. Cowhides
(Oreochromis acid (Col/ZN/GA) electrospun films and tendons, and pork hides are the most common source materials.
niloticus) electrospun film containing 8 % (w/w) First, the non-collagen components and mineral substances in the raw
muscle gallic acid (GA8)
significantly (p < 0.05)
collagen tissue materials are removed by pretreatment, and then the size
halted tilapia muscle of the raw materials is reduced by crushing. In the process of fragmen­
tation, the ordered, dense and high-strength skin collagen fibers are
broken and partially denatured. The disordered arrangement of collagen

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fibers interacts with the collagen molecules or supramolecular structures “branches” in collagen fibrils.
filled therein to form a film structure (Fig. 3a) [95]. Gelatin gels are formed at a low temperature as a result of confor­
In food field, researchers believe that the formation of collagen mational transformation from coil to helix and the structure of collagen
fibrous film is related to the self-assembly of collagen [52]. Yang, Shi, Li, triple helix is similar to that of gelatin helices. Depending on the
Wang, Wang and Luo [96] employed counter-rotating extrusion tech­ annealing temperature and the concentration of gelatin, the final helix
nology to fabricate collagen fibers from insoluble collagens, which had a configuration will be either non-looped or single-looped helix [107].
tensile strength comparable to natural rat Achilles tendons. Xu, Liu, Goff The gelatin formed gel at lower temperature than the sol-gel transition
and Zhong [52] successfully prepared collagen fiber films by casting, temperature when the concentration of gelatin is >1 % [40]. Fish gelatin
and studied the effect of pH on the film-forming properties of collagen of cold water has a lower gel formation temperature (~4–12 ◦ C) than
fiber dispersions (Fig. 3b, c). Wu, Liu, Yu, Ma, Goff, Ma and Zhong [97] fish gelatin of warm water (~18–19 ◦ C), both of which are lower than
immersed the neutralized collagen fiber paste in a carboxymethyl cel­ those of poultry gelatin and mammalian gelatin (~30 ◦ C). Differences in
lulose composite film, and found that the addition of glycerol increased amino acid composition may account for the different gel formation
the distance between collagen molecules and decreased the relative temperatures among the various types of gelatin [36]. In situ measure­
triple helix content. Ma, Teng, Zhao, Zhang, Zhao, Duan, Li, Guo and ment of optical rotation of gel is the best method for monitoring the gel
Wang [98] prepared micro/nanocollagen fibers using a high-pressure formation mechanism of gelatin, which is related to the helix to coil
homogenization technique to study the effect of fiber size on the final conformation transition from collagen [108]. The amount of helices in
film properties. With the decrease in fiber size, the mechanical proper­ the gelatin chains can be directly determined by normalizing the optical
ties and water vapor barrier properties of collagen film were improved, rotation value [109]. In a study conducted by Qiao, Wang, Zhang and
which may be due to the physical entanglement and non-covalent bond Yao [41], kosmotropic ions promoted gel formation of gelatin solution
enhancement caused by fiber size reduction (Fig. 3d). in the presence of different Hofmeister salts using a polarimeter, but
Recently, the gelatin films have been also extensively studied for chaotropoic ions hindered this process.
food applications (Fig. 4a) [99]. Herrera-Vázquez, Dublán-García,
Arizmendi-Cotero, Gómez-Oliván, Islas-Flores, Hernández-Navarro and 5. Food applications
Ramírez-Durán [100] evaluated the effects of gelatin fiber, whey protein
and chitosan concentrations on the properties of the prepared composite 5.1. Muscle foods
films by response surface methodology, and found that the maximum
gelatin films resulted in better mechanical property, lower water content Sausage, patty, and burger are emulsified muscle protein matrices
and solubility of the composite films. In addition, gelatin films can with a unique gel structure and texture [110]. Collagen or gelatin is
exhibit excellent barrier behavior to gas, oxygen and aromatic pene­ commonly applied to improve its emulsifying stability, hardness, resil­
tration under a relatively low or moderate humidity. Abedinia, Ariffin, ience, and water binding capacity. Lee and Chin [111] reported that
Huda and Mohammadi Nafchi [99] successfully prepared a duck feet low-fat sausages (<2 g/100 g) with the addition of pork gelatin had a
gelatin film to replace bovine gelatin film, and found that the duck feet good water holding capacity, leading to the reduced cooking loss, but
gelatin film had a lower water vapor permeability, which was attributed the addition of cuttlefish skin gelatin increased meat emulsion stability,
to the difference in Hyp content that could form hydrogen bonds with and chewiness of the formulated sausage [110]. This can be attributed to
water. Liu, Majeed, Antoniou, Li, Ma, Yokoyama, Ma and Zhong [101] the ability of pork gelatin to form protein-water bridges in the emulsion,
proposed that the mechanical properties of the TGase-modified gelatin resulting in the better texture and improved overall yield. However, the
films could be tuned by changing the relative number of triple helices inclusion of 1 % gelatin or gelatin hydrolysate might not be sufficient to
and covalent bonds, which in turn was controlled by changing the fully exploit these properties. This suggests that higher levels of gelatin
drying temperature around the gelation temperature of gelatin (Fig. 4b). may be needed to form a gel matrix that effectively traps moisture in
meat sausage, resulting in better water retention. Gao, Qiu, Nan, Wang,
4.4. Gel formation Yang, Zhang and Yu [112] substituted fat with ultra-high pressure-
assisted-prepared cowhide gelatin in beef patty (42 %–56 %), and found
Changes in temperature, pH, or ionic conditions can initiate collagen the addition of gelatin lowered the cooking loss and increased the
gel formation, which includes fibril intertwining in vitro, self-assembly, moisture. This aligns with previous findings that suggest gelatin can
and fibril formation [102]. Collagen gels are composed of elastic serve as an effective fat replacer, improving the water-holding capacity
collagen fibril network that are responsible for three-dimensional of meat products [113]. Moreover, Essa and Elsebaie [64] reported that
structure [103]. An average collagen gel network has a diameter of low-fat burgers containing complex gels comprised of gelatin and solu­
~100 nm, and possess D-periodicity structures to natural collagen fi­ ble dietary fibers as a fat replacer achieved a softened texture close to the
brils. Collagen gel formation is controlled by the conditions that initiate fat group. This finding suggest that the use of such gels can effectively
the sol-gel transition of collagen. Tian, Ren, Shi, Hao, Chen and Weng mimic the texture of traditional burgers while significantly reducing the
[60] observed that an increase in NaCl concentration in a simulated fat content. Furthermore, the incorporation gelatin and soluble dietary
body fluid led to a denser fibril network structure in collagen gels. fibers not only provides a healthier alternative but also enhances the
During collagen fibril formation, collagen fibrils are heterogeneous and overall eating experience by maintaining the desired softness in the
tightly packed due to the neutralizing effects of the chloride ion since it burgers (Fig. 5). Surimi products are gel foods containing a high content
neutralizes the surface charge of collagen molecules. Moreover, collagen of myofibrillar protein [66], and have been often mixed with bovine or
fibrils with D-periodic structures may be formed by chloride anions fish gelatin at an appropriate level to improve the textural properties
[54]. In a study by Shi, Tian, Wang, Hao, Chen and Weng [104], pH was [114]. Fish gelatin has been found to increase the moisture content but
studied as a factor in determining the diameter and number of fibrils in a decrease the nutrient loss in fish balls, and improve the texture by
collagen gel. The researchers observed increased collagen gel fibrils decreasing hardness and chewiness [66]. Huang Yuping, Weng Wuyin
numbers and diameters with increasing pH ranging from 5.0 to 8.0. and Xichun [115] reported that the breaking force and water holding
Moreover, increasing ambient temperature from 4 to 37 ◦ C resulted in a capacity of silver carp surimi gels were increased by 20 % and 35 % by
decreased fibril diameter and pore space in the collagen gel network the addition of 10 % fish skin gelatin. Since surimi products are usually
[105]. Xu, Wei, Shu, Li, Wang, Li, Li, Li, Zhang and Wang [106] recently stored under frozen condition, the cryoprotective effect of gelatin hy­
used low temperature ultraviolet radiation to develop a collagen gel. drolysates on surimi is of great interest. It was reported that the gelatin
This process degraded collagen molecules and cross-linked them, pro­ hydrolysate from the skin of black tip sharks prevented the denaturation
moting the intertwining of collagen fibers and leading to more of surimi protein, which was comparable to the commercial

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M.I. Ahmad et al. International Journal of Biological Macromolecules 254 (2024) 128037

Fig. 3. (a) Collagen fiber film with 3D hierarchical structure composed of multi-scale fibers. Reproduced with permission from reference [95]. (b-c) The effect of pH
on swelling rate and mechanical properties of collagen fiber film. Reproduced with permission from reference [52]. (d) The effect of collagen fiber size on mechanical
properties of collagen fiber film. Reproduced with permission from reference [98].

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M.I. Ahmad et al. International Journal of Biological Macromolecules 254 (2024) 128037

Fig. 4. (a) Preparation and characterization of a novel bio-composite film based on duck feet gelatin. Reproduced with permission from reference [99]. (b) Effect of
drying temperature on mechanical properties of gelatin film. Reproduced with permission from reference [101].

Fig. 5. The functions of collagen and gelatin for use in various foods.

cryoprotectant [116,117]. maintaining a creamy and smooth consistency is crucial. A further study
confirmed that the addition of 0.4 % tilapia skin gelatin completely
prevented whey separation from the acid milk yogurt, ensuring a more
5.2. Dairy products
homogeneous and appealing product [67]. The properties of tilapia skin
gelatin make it an ideal candidate for stabilizing yogurt. Not only does it
Yogurt is fermented from raw milk [67]. Gelatin has been also used
prevent whey separation, but it also enhances the viscosity, texture,
to increase the viscosity and water-binding capacity of yogurt, pre­
creaminess, and the mouthfeel of the yogurt.
venting the clumping and expelling of whey (Fig. 5). Yin, Yang, Lai and
Ice cream and mousse are based on three-phase emulsions containing
Yang [118] added 0.4 g/100 g xanthan-modified fish gelatin to yogurt,
air, oil, and water. Gelatin can decrease water surface tension to facili­
and observed a better water-holding capacity, acceptable viscosity and
tate foam generation, and enclose the fine distribution of air bubbles
consistency. Pang, Deeth, Sharma and Bansal [77] reported that gelatin
within a lattice to stabilize foams [80]. This might also control the size
could enhance the water-holding capacity without increasing the firm­
and distribution of ice crystals. Duan, Zhang, Liu, Cui and Regenstein
ness of acid milk. The researchers concluded that gelatin unique prop­
[74] added channel catfish skin gelatin into ice cream, and found that
erties make it an ideal stabilizer in acid milk products, as its allows for
the product showed the improved texture stability and smooth mouth-
better moisture retention without compromising the texture of the milk.
feel. The gelatin acted as a stabilizer, preventing the crystal formation
This is particularly important in the production of yogurts, where

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M.I. Ahmad et al. International Journal of Biological Macromolecules 254 (2024) 128037

and improving the overall texture of the ice cream. The unique char­ concentration of valuable anthocyanin’s and other beneficial
acteristics of fish gelatin, such as its higher viscosity and lower immu­ compounds.
nogenicity compared to the mammalian gelatin, contribute to these
desirable properties. Likewise, Damodaran and Wang [78] reported that 5.5. Bakery products
fish gelatin hydrolysate prepared by Alcalase endo-protease was able to
inhibit ice crystal growth in ice-cream, significantly improving texture Since gelatin exhibits good water binding, gel-stabilizing, and even
consistency and stability. Duquenne, Vergauwen, Capdepon, Boone, De ice crystal inhibitioncapabilities, it may be applied in bakery products to
Schryver, Van Hoorebeke, Van Weyenberg, Stevens and De Block [79] provide improved structure and texture (Fig. 5). Yu, Xu, Zhang, Guo,
also reported that gelatin hydrolysate fortified the microstructure in Hong, Zhang, Jin and Xu [75] found that the presence of pigskin gelatin
frozen mousse and inhibited the growth of ice crystals. formed a high resistant gluten structure against the distortion of ice
crystals, embodying a larger bread volume and more uniform bread
5.3. Confectionary and desserts crumb. Further studies showed that pigskin gelatin restricted the water
transfer and hindered the chain reassociation of starch molecules,
Gelatin is one of the most important ingredients for confectionary retarding the staling of bread [119]. This mechanism plays a crucial role
[129]. The confectionery appearance, texture and stability are greatly in retarding the deterioation of bread quality overtime. The gelatin act
affected by gelatin (Fig. 5). Gummy candy has resilience with melting- as a barrier, preventing the migration of water within the bread and
in-mouth sensory properties, attracting children, old people and many inhibiting the formation of new molecular structures that contribute to
age groups. Mutlu, Tontul and Erbaş [63] reported that the addition of the hardening of the bread crumb. Sang, Ou, Fu, Su, Jin and Xu [135]
5–10 % gelatin increased the hardness, chewiness, resilience and reported that the addition of 1 % fish gelatin enhanced the strength and
melting temperature of gummy candies. This finding highlights the gas-retention capacity of dough, resulting in improved porosity and
importance of using gelatin as a texture modifying agent in confec­ volume of bread, and starch retrogradation was also retarded. In another
tionary products. Furthermore, it suggests that manufacturers can adjust study, the additon of gelatin along with duck egg white decreased the
the concentration of gelatin to meet specific texture preferences and freezable water content and water fluidity of dough, and increased the
create unique sensory experiences for consumers. Marshmallow is an elastic and viscous modulus during the frozen storage process [136].
aerated confectionery product. Gelatin is often used as a crucial foaming This indicates that the dough becomes more elastic and exhibits more
and gelling agent. By using 2.2 % gelatin, marshmallows showed the resistance to deformation during storage and freezing.
highest hardness but great moisture loss by the end of 25-week storage
[129]. 6. Conclusion
Jelly dessert is a kind of ready-to-eat gel food with good sensory
properties. The main component is gelatin. The texture properties of A promising resource for protein can be found in collagen and gelatin
jelly desserts are often modified by manipulating the recipe containing derived from animal byproducts. Their special characteristics, as well as
gelatin and other hydrocolloids. Besides, spread is a food with a large biodegradability, edibility, and bioavailability make them widely
amount of fat, carbohydrate or protein. Usually, the product contains applicable in food industry. Collagen and gelatin are reviewed in this
ingredients able to provide excellent emulsifying and stabilizing func­ paper concerning the structural, biochemical, and physical properties.
tions. Almeida and Lannes [130] reported that the addition of 0.3–1.2 % However, a lack of standardized preparation procedures and a limited
chicken feet gelatin improved the consistency of a chocolate spread. This number of species sources limit the availability of collagen and gelatin.
suggest that gelatin can be used as functional ingredient to enhance the The impact of collagen and gelatin on food products during storage and
texture and mouthfeel of products like chocolate spreads. The gelatin processing, and their possible interactions with other food components,
likely acts as a stabilizer, helping to prevent separation and maintain a needs to be further investigated. Collagen and gelatin-based food
smooth and creamy consistency. packaging materials have a lot of amino acid residues in the side chains
that may allow for enzymatic, chemical, and physical modifications to
5.4. Beverages overcome the current limitations [137]. Researchers need to explore the
mechanical, physicochemical, and controlled release of collagen-based
Generally, beer and wine form a cloudy complex to increase the active food packaging materials. Furthermore, alternatives in mamma­
turbidity during processing, leading to the decline in the final quality of lian gelatin such as fins, bones, warm and cold-water fish skins are
products. Gelatin can react with compounds causing clouds or work as available from marine sources [138]. Byproducts of the fish-processing
an adsorbent to remove the turbid substances in the matrix (Fig. 5). industry such as fish skin can provide a valuable source of gelatin.
Duan, Zhang, Liu, Cui and Regenstein [74] compared the fining function There are several advantages of using marine gelatin sources, including
of catfish skin gelatin and commercial bovine gelatin in beer, and found the fact that they are not associated with outbreaks of Bovine Spongi­
that both of them distinctly increased the clarity of beer, but the catfish form Encephalopathy, and Muslims are allowed to use fish gelatin, but
skin gelatin showed better effects. It was also reported by Ghanem, there are a few restrictions in Jews and Hindus. In order to improve
Taillandier, Rizk, Rizk, Nehme, Souchard and El Rayess [131] that collagen and gelatin applications in the food industry, more efforts must
gelatin showed the good clarifying effect during fining young red wine. be made to meet the above mentioned challenges.
For fruit juice, Lassoued et al. [132] reported that the pepsin-aided
extracted gelatin from thornback ray skin showed a stronger clarifying Funding
ability to apple juice than bovine gelatin, but the nutritional components
of clarified apple juice were practically not changed. In another study, it This work was supported by National Natural Science Foundation of
was found that a combination of gelatin-bentonite could fine apple juice China (32250410297), Talent Introduction Program of Postdoctoral
at a high efficiency [133]. Fang, Zhang, Du and Sun [134] also reported International Exchange Program to Excellent International Young Re­
that gelatin combined with bentonite and ultrafiltration could greatly searchers by the Office of China Postdoc Council (OCPC) and the postdoc
reduce the haze in fining bayberry juice. This study further supports the office of the Zhejiang University, Hangzhou, China.
notion that gelatin and bentonite, when used in conjunction with ul­
trafiltration, can effectively remove unwanted compounds such as CRediT authorship contribution statement
polyphenols and proteins, which are known to contribute to the for­
mation of haze in juice. By implementing this method, the bayberry juice Muhammad Ijaz Ahmad: Conceptualization, Investigation, Writing
not only achieves improved clarity, but also retains a higher – original draft. Yonghui Li: Investigation, Writing – review & editing.

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M.I. Ahmad et al. International Journal of Biological Macromolecules 254 (2024) 128037

Jinfeng Pan: Investigation, Writing – review & editing. Fei Liu: [16] F. Liu, Z. Yu, B. Wang, B.S. Chiou, Changes in structures and properties of
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