International Journal of Biological Macromolecules 254 (2024) 128037

Contents lists available at ScienceDirect

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
Collagen is one of the most ubiquitous and abundant protein found in
all animal bones and skin, accounting for about 30 % of the total protein
content [1]. Blood vessels, tendons, cartilage, bone and animal skin are
all composed of collagen [2]. The basement membranes and extracel­
lular matrix are formed through their fibrillar and microfibrillar net­
works. Connective tissues such as skin, tendon, cartilage, and bone
contain fibrillar protein [3]. In addition, the structure and stability of
various organs and tissues are enhanced by high tensile and stable
insoluble fibrils of collagen [4]. The collagen and gelatin market value
exceeded ~4.7 billion USD in 2020, of which 80 % are used by the
health and food industries, and it is estimated to grow over ~7 billion
USD by 2027 [5].
Collagen and gelatin can be used for the development of functional
foods and to improve the quality of processed foods [6]. According to
Gómez-Guillén, Giménez, López-Caballero and Montero [7], collagen
properties can be classified into two categories: first, the properties
linked with their gelling behavior, such as water binding capacity, gel
formation, thickening, and texturizing of collagen; second, the proper­
ties associated with surface behavior, such as film-forming, protective
colloid function, adhesion and cohesion, stabilization, foam formation,
and emulsion [6]. Recently, collagen has been widely used in agricul­
tural, tissue engineering, biomedical, cosmetic, pharmaceutical, and
food industries due to its excellent degradability and biological
compatibility [8,9]. Collagen can form stable and durable fibers due to
its ability to crosslink and self-aggregate, making it ideal for use in drug
delivery systems [10,11]. Additionally, the natural properties of
collagen make it suitable for use in pharmacology and medicine,
including biodegradability, hemostatic activity, and low allergenicity
with high biocompatibility and antigenicity [12].
A considerable number of collagen molecules can be self-assembled
into highly diverse shapes with intact triple-helical structures under
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.
the collagen triple helix are broken during the extraction process,
resulting in a polypeptide mixture called gelatin, i.e., collagen partially
degrades to form gelatin [13]. Film forming, foaming, emulsifying, and
gelling are all associated with the functional properties of collagen and
gelatin [7,14]. These properties make them suitable for use as a wide
range of food products, or edible packaging materials [12,15]. Edible
packaging materials, including those based on collagen, have emerged
as an essential component of the global food industry [16]. The unique
nature of their creation, often derived from hide or pig skins, offer
remarkable in their ability to act as systems of delivery, underpinned by
enhanced barrier and mechanical properties, augmenting the protection
of food products. Their functionality is not just limited to preserving
freshness but also extends to manipulating sensory experiences. For
instance, the control-release of active ingredients can enhance flavors
while also offers nutritional benefits. Moreover, sausages are often
produced with collagen casings, which is an edible film. Compared to
pork casings, collagen casings significantly reduced biogenic amines
produced during fermentation, improving the quality characteristics of
sausages [17]. Added functionality, such as antimicrobial properties,
can also be conferred with collagen casings [18]. The co-extrusion of
sausage casing entails the involvement of collagen and alginate, two
resources that serve to solidify the shape of sausage immediately after
extrusion process [19]. Although both materials have their advantages
and disadvantages, collagen capability of imparting a superior snap is
noteworthy. Still, it does necessitate a higher investment for fiber
alignment to emulate natural casing. Recently, Suurs, van den Brand, ten
Have, Daamen and Barbut [20] produced co-extrusion sausage casing
using cattle skin collagen with enhanced viscoelastic and mechanical
properties. A variety of benefits can also be derived from collagen
consumption, including improved skin health [21], and alleviating the
risk of cardiovascular diseases [22,23]. Additionally, collagen and
gelatin release bioactive peptides encoded in their sequences during the
digestion process of food products in the gastrointestinal tract [24].
Moreover, peptides prepared from a variety of animal by-products can
be facilitated by low molecular weight collagen hydrolysates, which
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].
2
International Journal of Biological Macromolecules 254 (2024) 128037
show greater bioavailability and digestibility compared with collagen or
gelatin [8].
To fully exploit the application potential of collagen and gelatin in
food industry, it is essential to understand their basic structure, appli­
cation features, and key functional properties. In this review, the recent
research regarding the structure, functional properties, as well as cur­
rent applications in food industry of collagen and gelatin are summa­
rized, expecting to provide a detailed understanding of their
characteristics and applications in food industry.
2. Structure of collagen and gelatin
2.1. Structure of collagen
In 1954, Ramachandran and Karta proposed the structure of
collagen, which led to a better understanding of collagen structural and
functional properties [25]. Even though different types of collagen differ
significantly in distribution, function, and size within tissues [26], the
general structure of collagen is characterized by a triple helix that ex­
tends from the middle and is usually composed of three parallel
α-chains, each presenting a left-handed conformation similar to poly­
proline II (PPII) (Fig. 1) [27,28]. A non-fibrillar collagen molecule is
known as tropocollagen [29]. Over 1000 amino acids are present in the
mature fibrillar collagen, including short telopeptides at each end that
play a critical role in binding to the matrix [10]. The triple helix of non-
fibrillar collagens contains imperfections (one or three residues) or in­
terruptions (containing large numbers of residues) [28]. Moreover,
many collagen molecules contain repeating amino acid motifs as part of
their structure, where pro and 4-Hyp often occupy X and Y in Gly-X-Y,
respectively. Triple helix of collagen is centered on every third amino
acid residue, so the primary structure of the three positions is occupied
by the smallest amino acid, Gly [30]. Moreover, collagen folds more
efficiently when Hyp and Pro residues are abundant, since the hy­
droxyproline and proline sequences are pre-arranged into a PPII
conformation, thereby reducing the entropic cost. For collagen triple
M.I. Ahmad et al.
helix stability, amino groups of Gly residues form hydrogen bonds with
carboxyl groups of adjacent residues at the X position. Also, the ster­
eoelectronic effect stabilizes the collagen triple helix at 4-Hyp in the Y
position [31]. Proteins encoded by collagen mRNA become protein
chains at the ribosomes through translation. The lumen of the endo­
plasmic reticulum undergoes post-translational modifications (such as
glycosylation and hydroxylation) of the procollagen α-chains by
removal of the N-terminal signal peptide [32]. The catalysis of protein
disulfide isomerase takes place at the C-terminal domains of α-chains of
disulfide bonds to modified procollagen α-chains align during the pro­
cess of triple helix formation. Then a procollagen molecule is formed as a
result of α-chains triple helix extension from the C to the N-terminus
[10].
The cleavage of procollagen C-proteinase (PCP) and procollagen N-
proteinase (PNP), which are known as biological restrictive enzymes,
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 molecules [33]. The N-propeptide of type I procollagen is
cleaved by PCP between Asp and Ala sites, whereas PNP cleaves between
Ala-Gln and Pro-Gln. PCP belongs to the Tolloid-like proteinases/bone
morphogenetic protein-1 (BMP-1) family, while PNP is classified as a
metalloproteinase and disintegrin with thrombospondin motifs
(ADAMTS) [34]. In collagen microfibrils, tropocollagen molecules are
longitudinally integrated after the N-/C- propeptides are enzymatically
removed [13]. Upon interdigitating, collagen fibrils are formed by
crosslinking the microfibrils. Ligaments and tendons are structurally
based on collagen fibers, which are made up of fibrils and proteoglycans
[35].
2.2. Structure of gelatin
Gelatin with molecular weights ranging from 15 to 250 kDa is pro­
duced by partial hydrolysis of collagen [36]. It is possible to have two
types of gelatin, called type A and B, depending on the pre-treatment
procedures, such as acid or alkaline pretreatment conditions. The pro­
duction of gelatin also involves enzyme pre-treatment that targets spe­
cific labile peptide bonds [37]. In the final gelatin product, polypeptides
of different conformations and sizes appear due to the combination of
different pre-treatment and extraction procedures. It may consist of
higher molecular weights fractions, e.g., γ-chains (covalently linked
α-chain trimmers), β-chains (covalently linked α-chains dimers), and
microgels with very higher orders [38]. A gelatin molecule contains the
same amino acids as collagen molecules, since gelatin is derived from
collagen that has been denatured. The deamination of glutamine and
asparagine occurs when collagen is hydrolyzed into gelatin. During the
manufacturing process of gelatin, collagen loses its native structure and
Table 1
Differences between collagen and gelatin properties.
Property Collagen
Origin Animals/ humans
Precursor Fibroblast
Peptide structure Triple helix of polypeptide chain
Number of amino Approximately 1050
acids
Types Fibril-forming and non-fibril forming
Aromatic radicals Present
Physical Elastic, tough and versatile structural protein
characteristics
Solubility NaCl solution/ dilute acid
Mechanical strength Poor
Gelling properties No
In vitro degradation Serine protease, pepsin cleaving enzyme, gelatinease and collagenase
In vivo degradation Endopeptidase
Digestion Difficult
Protease Resistant
Usage Burns, hemostasis, tissue defects, regeneration of nerves, wound dressings, artificial dermis
skin replacement
3
International Journal of Biological Macromolecules 254 (2024) 128037
denatures, which results in the formation of triple helical structures
[39]. By adjusting the temperature above its critical gel temperature,
gelatin gels can change from gel to sol, which is a cold setting and
thermo-reversible gel [40]. For gelatin, gel formation is a result of
collagen-like triple helices from randomly coiling polypeptide chains
(Table 1). A triple helix region called a junction zone formed, when
different chains intertwine with each other upon cooling [41]. Then the
collagen-like triple helical structure of gelatin molecules partially re­
verts. In addition to hydrogen bonds, electrostatic and hydrophobic
interactions have also been found to play an important role in stabilizing
these triple helix [38].
3. Properties of collagen and gelatin
3.1. Self-assembly
Collagen has the inherent ability to self-assemble. A type I collagen
fiber bundle can be formed in vivo by self-assembling into microfibrils
and subsequently into fibrils, which can be organized in different ways
according to organs and tissues [51]. In vitro, fibrils with the charac­
teristic D-periodicity can also form spontaneously and orderly from
collagen molecules that contain intact triple-helical domain [52]. There
is a great deal of similarity between the in vivo and in vitro structure of
the fibrils. Collagen can self-assemble into sponges, gels, and fibrils
depending on the environmental conditions. Self-assembled aggregates
are characterized by their distinct multi-hierarchical organization that
contributes both to their biological and physical properties (Fig. 2)
[27,53].
Collagen self-assembles through nucleation growth, i.e., several
collagen molecules are gathered together to form cores, which are then
transformed into mature fibrils [54]. A two-phase kinetic process is
involved with the self-assembly, namely, the growth of nucleus center,
and the formation of nucleus center [55]. The typical process of collagen
self-assembly includes a lag phase (cores are formed following the ag­
gregation of monomer molecules), a growth phase (fibrils are formed
when cores grow in length and diameter), and a linear plateau phase
(saturation of fibrils) [56]. Gisbert, Benaglia, Uhlig, Proksch and Garcia
[2] used a high-speed biomodal atomic force microscope (AFM) to
recognize the four stages of collagen self-assembly: (1) a collagen pre­
cursor is nucleated, (2) grows into tropocollagen molecules, (3) then
assembles into microfibers, (4) and finally the formation of
microribbons.
Collagen self-assembly may be affected by a variety of factors [56].
The concentration [55], extraction method [57], and source [58] can
have a significant impact on the self-assembly of collagen. Ultrasonic
treatment, phytic acid, sulfonated chitosan, molecular chirality, amino
Gelatin References
Collagen from bones/ skin [42,43]
Collagen type 1 [44]
Small peptides [44]
<20 [7]
A and B [44]
Absent [45]
Smooth and gel-like substances [7]
H2O [7]
Poor [46]
Yes [7]
Collagenase [47,48]
MMP-2 and MMP-9 [47]
Easy [49]
Susceptible [50]
Adhesive of soft tissues, artificial skin, wound [47]
dressings
M.I. Ahmad et al.
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
factors that affects the self-assembly of collagen molecules [59,60].
Electrostatic interactions, hydrophobic interactions, and hydrogen
bonding may modify the kinetics of self-assembly, as well as the struc­
ture and properties of the self-assembled aggregates [61]. For example,
as the temperature increases (20–37 ◦ C), collagen transforms from a
hydration-rich PPII structure to an ordered sheet structure, which pro­
motes the self-assembly of collagen molecules and enhances hydro­
phobic effects [53]. A pH closer to the isoelectric point will allow
collagen molecules to self-assemble more readily, which reduces the
electrostatic repulsion leading to faster collagen intermolecular in­
teractions as the net charge of the protein decreases [62].
3.2. Gel forming, water retaining, and thickening ability
The complete native structure of collagen is destroyed during the
processing of gelatin, but the resulting fragments still keep partially
4
International Journal of Biological Macromolecules 254 (2024) 128037
linked through polypeptide chains [39]. Above setting temperature, the
gelatin solution appears as sol and these polypeptide chains are random
coils. However, upon cooling, some of the chains intertwine to form
partially ordered collagen-like triple helical structures, resulting in a gel
network [41]. Particularly, gelatin can form a thermal-reversible gel
with a gel-melting temperature < 37 ◦ C. This feature provides a melt-in-
the-mouth property, which can provide a fat-like sense to food, offering
innovative product development opportunities [8]. This enables the
application of gelatin in gel foods, e.g., surimi products, sausages, aspic
products, confectionaries, etc. [63,64]. Besides, soluble collagen and
gelatin usually show good water binding capacity, which makes them
suitable for keeping juiciness and reducing drip loss in frozen muscle
products [65,66]. Viscosity is another important property of gelatin.
Combined with other hydrocolloids, gelatin can be applied as a thick­
ener in dressing, yogurt and beverage for satisfactory sensory properties
[67]. Recently, it has been used for developing 3D printing foods. The
gelatin solution above its gelling temperature is easy to push into the
M.I. Ahmad et al.
nozzle, and form a stable gel in a circumstance with a temperature lower
than a gelling point after printing out from the nozzle, showing an
excellent printing capacity [68].
3.3. Emulsifying and foaming ability
As a polymer with charged and amphiphilic groups, gelatin shows
active surface behaviors, especially emulsifying and foaming properties.
Intact collagen is an ineffective emulsifier, but acid-/pepsin-soluble
collagen containing sufficient hydrophilic and hydrophobic amino acid
residues, which can absorb oil-water interfaces and promote emulsion
formation by lowering interfacial tension [69]. The electrostatic repul­
sion could prevent the aggregation of emulsion droplets. Meanwhile,
emulsion stability is also improved by gel formation and viscosity of
gelatin. Thus, the treated collagen or gelatin has been commonly applied
in emulsified muscle foods, such as patty, sausage, and surimi products
[66,70,71]. Gelatin and soluble collagen can exhibit fairly good foaming
properties, which are mainly attributed to their capacity of reducing the
surface tension at liquid-air interface. Moreover, gelatin can form a
three-dimensional network to increase the continuous phase, which
could stabilize foams. Therefore, gelatin has been used for the manu­
facture of aerated confectionaries, like marshmallows or soft gel candies
[72] [73], and for improving the texture and structure of ice cream [74]
and bakery products [75].
3.4. Stabilizing ability
It is known that the three-dimensional network formed by gelatin
can increase the continuous phase, which can stabilize emulsions and
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
NH2- and OH-, gelatin can form hydrogen bonds with compounds in
food mixtures, which often increases food stability. It has been reported
that gelatin could reduce the formation of sugar crystals and inhibit the
relative separation of oil and water in syrup [76]. Syneresis led by
temperature fluctuations or pasteurization in yogurt may be inhibited by
gelatin due to its strong water-binding capacity and gel structure [77].
For frozen food, gelatin and its hydrolysates can inhibit the formation of
large size ice crystals, which could be helpful for maintaining the quality
of ice cream and surimi products [78,79]. Additionally, gelatin as a
binder can reduce brittleness, and facilitate molding and cutting during
the manufacture of confectionery [76].
3.5. Fining ability
Clarity is an important structural criterion for many liquid foods,
such as beer, wine, and fruit juices. At a pH lower than the isoelectric
point, gelatin is positively charged. It would react with the negatively
charged polyphenols and anthocyanins in the food matrix by electro­
static interactions to form precipitated complexes that can absorb
turbidity-forming substances, causing them to co-precipitate [80].
Therefore, gelatin has been widely applied as a fining agent to clarify the
cloud in beer, wine, or fruit juices.
4. Colloids structures
4.1. Emulsions
The structure formation properties of collagen and gelatin depend on
the charged groups in the protein side chains and the partial collagen
sequence containing either hydrophilic or hydrophobic amino acids
[81]. The amphiphilic nature of this protein results in effective migra­
tion from the water phase to the oil-water interface, and subsequently
form an interfacial layer, showing a great potential application in
emulsion systems [82].
The emulsifying properties of collagen have attracted much attention
5
International Journal of Biological Macromolecules 254 (2024) 128037
to enhance the emulsion stability for food applications [15,83]. Dey,
Kadharbasha, Bajaj, Das, Chakraborty, Bhat and Banerjee [83] obtained
two collagen hydrolysates (CH) with higher surface activity from Pacu
skin and Tilapia bones by screening seven fish processing by-products.
Santana, Perrechil, Sato and Cunha [15] evaluated the emulsifying
properties of collagen fibers under different conditions of pH, protein
content and type of emulsification device. At a low pH value (3.5), the
electrostatic interactions were responsible for the emulsion stability,
while steric hindrance and interface film dominated the emulsion sta­
bility at higher pH values (4.5–7.5).
Despite the impressive emulsifying ability of gelatin, it is still
considered to be a relatively weak emulsifier compared to other surface-
active biopolymers such as globular proteins and gum Arabic [84,85].
Thus, some strategies have been used to improve the stability of gelatin
emulsions. Feng, Dai, Ma, Fu, Yu, Zhu, Wang, Sun, Tan and Zhang [84]
investigated the effect of three drying methods (hot air, freeze and spray
drying) on the solubility and amphiphilicity of gelatin, and found that
the spray dried gelatin had a better amphiphilicity (92.48◦ ) which is
beneficial for stabilizing emulsions. Zhang, Sun, Ding, Li, Tao, Wang and
Zhong [85] found that the emulsion stabilized by bovine bone gelatin
was more stable than commercial cold-water fish skin gelatin, due to the
differences in secondary structures and thickness of gelatin film-like
nanostructures. Additionally, the gelatin emulsion stabilization has
been proven to be affected by different extraction methods, which lead
to different protein secondary structure, molecular interaction, and thus
affecting the formed emulsion droplet structure, and emulsion stability
[86].
4.2. Films or coatings
Collagen is a degradable material with suitable film-forming prop­
erty, and the recent development of film materials for packaging based
on collagen has been extensively investigated [87]. Collagen can rely on
a large number of hydrophilic carboxyl and hydroxyl groups on its
surface to form a dense hydrogen bond network, which offers an
appropriate template for biologically active cargo. For example, the
collagen solution mixed with lysozyme can be applied to prepare the
coatings for preserving salmon fillets, in which the formed collagen film
encapsulates lysozyme to prevent the growth of microorganisms [88]. At
the same time, the dense hydrogen bond network in the coatings can
prevent the exchange of gases on both sides to improve the shelf life of
fish products [88]. In order to strengthen the physical and chemical
properties of the collagen-based films, bioactive substances have often
been added into the films with specific functions by compounding with
collagen. Song et al. [87] reported that the strong hydrogen bonding
between collagen, zein, and gallic acid could lock gallic acid in the
collagen-zein fibers by electrostatic spinning, thus making the antioxi­
dant property of gallic acid effective in the fiber film and significantly
improving the shelf life of film-packed fish fillets. Besides, collagen can
be utilized as a structural enhancer to improve the film attributes of
other film-forming food-grade macromolecules. Liu et al. [89] reported
that the digestible collagen extracted from blue shark skin could
significantly boost the fresh-keeping effect of chitosan-based protective
films on fresh red porgy during storage, and the hydrogen bonding be­
tween collagen and polysaccharides played an essential role in the film-
forming process.
The applications of many active ingredients in collagen or gelatin-
based composite films have been studied (Table 2), such as 3-phenylace­
tic acid, pomegranate peel extract, cellulose nanoparticles, and grape
seed extract, which have been proven to effectively inhibit the oxidation
and growth of food-borne pathogens to maintain the quality of foods as
active packaging materials [90–92]. For example, the pH-sensitive
anthocyanin substance has been reported to be incorporated into the
collagen-based films to detect the freshness of meat in real-time through
the color changes of the films. With the decline in meat quality, the
surficial pH of meat products changes significantly, as anthocyanin is a
M.I. Ahmad et al. International Journal of Biological Macromolecules 254 (2024) 128037

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

6
M.I. Ahmad et al.
fibers interacts with the collagen molecules or supramolecular structures
filled therein to form a film structure (Fig. 3a) [95].
In food field, researchers believe that the formation of collagen
fibrous film is related to the self-assembly of collagen [52]. Yang, Shi, Li,
Wang, Wang and Luo [96] employed counter-rotating extrusion tech­
nology to fabricate collagen fibers from insoluble collagens, which had a
tensile strength comparable to natural rat Achilles tendons. Xu, Liu, Goff
and Zhong [52] successfully prepared collagen fiber films by casting,
and studied the effect of pH on the film-forming properties of collagen
fiber dispersions (Fig. 3b, c). Wu, Liu, Yu, Ma, Goff, Ma and Zhong [97]
immersed the neutralized collagen fiber paste in a carboxymethyl cel­
lulose composite film, and found that the addition of glycerol increased
the distance between collagen molecules and decreased the relative
triple helix content. Ma, Teng, Zhao, Zhang, Zhao, Duan, Li, Guo and
Wang [98] prepared micro/nanocollagen fibers using a high-pressure
homogenization technique to study the effect of fiber size on the final
film properties. With the decrease in fiber size, the mechanical proper­
ties and water vapor barrier properties of collagen film were improved,
which may be due to the physical entanglement and non-covalent bond
enhancement caused by fiber size reduction (Fig. 3d).
Recently, the gelatin films have been also extensively studied for
food applications (Fig. 4a) [99]. Herrera-Vázquez, Dublán-García,
Arizmendi-Cotero, Gómez-Oliván, Islas-Flores, Hernández-Navarro and
Ramírez-Durán [100] evaluated the effects of gelatin fiber, whey protein
and chitosan concentrations on the properties of the prepared composite
films by response surface methodology, and found that the maximum
gelatin films resulted in better mechanical property, lower water content
and solubility of the composite films. In addition, gelatin films can
exhibit excellent barrier behavior to gas, oxygen and aromatic pene­
tration under a relatively low or moderate humidity. Abedinia, Ariffin,
Huda and Mohammadi Nafchi [99] successfully prepared a duck feet
gelatin film to replace bovine gelatin film, and found that the duck feet
gelatin film had a lower water vapor permeability, which was attributed
to the difference in Hyp content that could form hydrogen bonds with
water. Liu, Majeed, Antoniou, Li, Ma, Yokoyama, Ma and Zhong [101]
proposed that the mechanical properties of the TGase-modified gelatin
films could be tuned by changing the relative number of triple helices
and covalent bonds, which in turn was controlled by changing the
drying temperature around the gelation temperature of gelatin (Fig. 4b).
4.4. Gel formation
Changes in temperature, pH, or ionic conditions can initiate collagen
gel formation, which includes fibril intertwining in vitro, self-assembly,
and fibril formation [102]. Collagen gels are composed of elastic
collagen fibril network that are responsible for three-dimensional
structure [103]. An average collagen gel network has a diameter of
~100 nm, and possess D-periodicity structures to natural collagen fi­
brils. Collagen gel formation is controlled by the conditions that initiate
the sol-gel transition of collagen. Tian, Ren, Shi, Hao, Chen and Weng
[60] observed that an increase in NaCl concentration in a simulated
body fluid led to a denser fibril network structure in collagen gels.
During collagen fibril formation, collagen fibrils are heterogeneous and
tightly packed due to the neutralizing effects of the chloride ion since it
neutralizes the surface charge of collagen molecules. Moreover, collagen
fibrils with D-periodic structures may be formed by chloride anions
[54]. In a study by Shi, Tian, Wang, Hao, Chen and Weng [104], pH was
studied as a factor in determining the diameter and number of fibrils in a
collagen gel. The researchers observed increased collagen gel fibrils
numbers and diameters with increasing pH ranging from 5.0 to 8.0.
Moreover, increasing ambient temperature from 4 to 37 ◦ C resulted in a
decreased fibril diameter and pore space in the collagen gel network
[105]. Xu, Wei, Shu, Li, Wang, Li, Li, Li, Zhang and Wang [106] recently
used low temperature ultraviolet radiation to develop a collagen gel.
This process degraded collagen molecules and cross-linked them, pro­
moting the intertwining of collagen fibers and leading to more
7
International Journal of Biological Macromolecules 254 (2024) 128037
“branches” in collagen fibrils.
Gelatin gels are formed at a low temperature as a result of confor­
mational transformation from coil to helix and the structure of collagen
triple helix is similar to that of gelatin helices. Depending on the
annealing temperature and the concentration of gelatin, the final helix
configuration will be either non-looped or single-looped helix [107].
The gelatin formed gel at lower temperature than the sol-gel transition
temperature when the concentration of gelatin is >1 % [40]. Fish gelatin
of cold water has a lower gel formation temperature (~4–12 ◦ C) than
fish gelatin of warm water (~18–19 ◦ C), both of which are lower than
those of poultry gelatin and mammalian gelatin (~30 ◦ C). Differences in
amino acid composition may account for the different gel formation
temperatures among the various types of gelatin [36]. In situ measure­
ment of optical rotation of gel is the best method for monitoring the gel
formation mechanism of gelatin, which is related to the helix to coil
conformation transition from collagen [108]. The amount of helices in
the gelatin chains can be directly determined by normalizing the optical
rotation value [109]. In a study conducted by Qiao, Wang, Zhang and
Yao [41], kosmotropic ions promoted gel formation of gelatin solution
in the presence of different Hofmeister salts using a polarimeter, but
chaotropoic ions hindered this process.
5. Food applications
5.1. Muscle foods
Sausage, patty, and burger are emulsified muscle protein matrices
with a unique gel structure and texture [110]. Collagen or gelatin is
commonly applied to improve its emulsifying stability, hardness, resil­
ience, and water binding capacity. Lee and Chin [111] reported that
low-fat sausages (<2 g/100 g) with the addition of pork gelatin had a
good water holding capacity, leading to the reduced cooking loss, but
the addition of cuttlefish skin gelatin increased meat emulsion stability,
and chewiness of the formulated sausage [110]. This can be attributed to
the ability of pork gelatin to form protein-water bridges in the emulsion,
resulting in the better texture and improved overall yield. However, the
inclusion of 1 % gelatin or gelatin hydrolysate might not be sufficient to
fully exploit these properties. This suggests that higher levels of gelatin
may be needed to form a gel matrix that effectively traps moisture in
meat sausage, resulting in better water retention. Gao, Qiu, Nan, Wang,
Yang, Zhang and Yu [112] substituted fat with ultra-high pressure-
assisted-prepared cowhide gelatin in beef patty (42 %–56 %), and found
the addition of gelatin lowered the cooking loss and increased the
moisture. This aligns with previous findings that suggest gelatin can
serve as an effective fat replacer, improving the water-holding capacity
of meat products [113]. Moreover, Essa and Elsebaie [64] reported that
low-fat burgers containing complex gels comprised of gelatin and solu­
ble dietary fibers as a fat replacer achieved a softened texture close to the
fat group. This finding suggest that the use of such gels can effectively
mimic the texture of traditional burgers while significantly reducing the
fat content. Furthermore, the incorporation gelatin and soluble dietary
fibers not only provides a healthier alternative but also enhances the
overall eating experience by maintaining the desired softness in the
burgers (Fig. 5). Surimi products are gel foods containing a high content
of myofibrillar protein [66], and have been often mixed with bovine or
fish gelatin at an appropriate level to improve the textural properties
[114]. Fish gelatin has been found to increase the moisture content but
decrease the nutrient loss in fish balls, and improve the texture by
decreasing hardness and chewiness [66]. Huang Yuping, Weng Wuyin
and Xichun [115] reported that the breaking force and water holding
capacity of silver carp surimi gels were increased by 20 % and 35 % by
the addition of 10 % fish skin gelatin. Since surimi products are usually
stored under frozen condition, the cryoprotective effect of gelatin hy­
drolysates on surimi is of great interest. It was reported that the gelatin
hydrolysate from the skin of black tip sharks prevented the denaturation
of surimi protein, which was comparable to the commercial
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].

8
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

9
M.I. Ahmad et al.
and improving the overall texture of the ice cream. The unique char­
acteristics of fish gelatin, such as its higher viscosity and lower immu­
nogenicity compared to the mammalian gelatin, contribute to these
desirable properties. Likewise, Damodaran and Wang [78] reported that
fish gelatin hydrolysate prepared by Alcalase endo-protease was able to
inhibit ice crystal growth in ice-cream, significantly improving texture
consistency and stability. Duquenne, Vergauwen, Capdepon, Boone, De
Schryver, Van Hoorebeke, Van Weyenberg, Stevens and De Block [79]
also reported that gelatin hydrolysate fortified the microstructure in
frozen mousse and inhibited the growth of ice crystals.
5.3. Confectionary and desserts
Gelatin is one of the most important ingredients for confectionary
[129]. The confectionery appearance, texture and stability are greatly
affected by gelatin (Fig. 5). Gummy candy has resilience with melting-
in-mouth sensory properties, attracting children, old people and many
age groups. Mutlu, Tontul and Erbaş [63] reported that the addition of
5–10 % gelatin increased the hardness, chewiness, resilience and
melting temperature of gummy candies. This finding highlights the
importance of using gelatin as a texture modifying agent in confec­
tionary products. Furthermore, it suggests that manufacturers can adjust
the concentration of gelatin to meet specific texture preferences and
create unique sensory experiences for consumers. Marshmallow is an
aerated confectionery product. Gelatin is often used as a crucial foaming
and gelling agent. By using 2.2 % gelatin, marshmallows showed the
highest hardness but great moisture loss by the end of 25-week storage
[129].
Jelly dessert is a kind of ready-to-eat gel food with good sensory
properties. The main component is gelatin. The texture properties of
jelly desserts are often modified by manipulating the recipe containing
gelatin and other hydrocolloids. Besides, spread is a food with a large
amount of fat, carbohydrate or protein. Usually, the product contains
ingredients able to provide excellent emulsifying and stabilizing func­
tions. Almeida and Lannes [130] reported that the addition of 0.3–1.2 %
chicken feet gelatin improved the consistency of a chocolate spread. This
suggest that gelatin can be used as functional ingredient to enhance the
texture and mouthfeel of products like chocolate spreads. The gelatin
likely acts as a stabilizer, helping to prevent separation and maintain a
smooth and creamy consistency.
5.4. Beverages
Generally, beer and wine form a cloudy complex to increase the
turbidity during processing, leading to the decline in the final quality of
products. Gelatin can react with compounds causing clouds or work as
an adsorbent to remove the turbid substances in the matrix (Fig. 5).
Duan, Zhang, Liu, Cui and Regenstein [74] compared the fining function
of catfish skin gelatin and commercial bovine gelatin in beer, and found
that both of them distinctly increased the clarity of beer, but the catfish
skin gelatin showed better effects. It was also reported by Ghanem,
Taillandier, Rizk, Rizk, Nehme, Souchard and El Rayess [131] that
gelatin showed the good clarifying effect during fining young red wine.
For fruit juice, Lassoued et al. [132] reported that the pepsin-aided
extracted gelatin from thornback ray skin showed a stronger clarifying
ability to apple juice than bovine gelatin, but the nutritional components
of clarified apple juice were practically not changed. In another study, it
was found that a combination of gelatin-bentonite could fine apple juice
at a high efficiency [133]. Fang, Zhang, Du and Sun [134] also reported
that gelatin combined with bentonite and ultrafiltration could greatly
reduce the haze in fining bayberry juice. This study further supports the
notion that gelatin and bentonite, when used in conjunction with ul­
trafiltration, can effectively remove unwanted compounds such as
polyphenols and proteins, which are known to contribute to the for­
mation of haze in juice. By implementing this method, the bayberry juice
not only achieves improved clarity, but also retains a higher
10
International Journal of Biological Macromolecules 254 (2024) 128037
concentration of valuable anthocyanin’s and other beneficial
compounds.
5.5. Bakery products
Since gelatin exhibits good water binding, gel-stabilizing, and even
ice crystal inhibitioncapabilities, it may be applied in bakery products to
provide improved structure and texture (Fig. 5). Yu, Xu, Zhang, Guo,
Hong, Zhang, Jin and Xu [75] found that the presence of pigskin gelatin
formed a high resistant gluten structure against the distortion of ice
crystals, embodying a larger bread volume and more uniform bread
crumb. Further studies showed that pigskin gelatin restricted the water
transfer and hindered the chain reassociation of starch molecules,
retarding the staling of bread [119]. This mechanism plays a crucial role
in retarding the deterioation of bread quality overtime. The gelatin act
as a barrier, preventing the migration of water within the bread and
inhibiting the formation of new molecular structures that contribute to
the hardening of the bread crumb. Sang, Ou, Fu, Su, Jin and Xu [135]
reported that the addition of 1 % fish gelatin enhanced the strength and
gas-retention capacity of dough, resulting in improved porosity and
volume of bread, and starch retrogradation was also retarded. In another
study, the additon of gelatin along with duck egg white decreased the
freezable water content and water fluidity of dough, and increased the
elastic and viscous modulus during the frozen storage process [136].
This indicates that the dough becomes more elastic and exhibits more
resistance to deformation during storage and freezing.
6. Conclusion
A promising resource for protein can be found in collagen and gelatin
derived from animal byproducts. Their special characteristics, as well as
biodegradability, edibility, and bioavailability make them widely
applicable in food industry. Collagen and gelatin are reviewed in this
paper concerning the structural, biochemical, and physical properties.
However, a lack of standardized preparation procedures and a limited
number of species sources limit the availability of collagen and gelatin.
The impact of collagen and gelatin on food products during storage and
processing, and their possible interactions with other food components,
needs to be further investigated. Collagen and gelatin-based food
packaging materials have a lot of amino acid residues in the side chains
that may allow for enzymatic, chemical, and physical modifications to
overcome the current limitations [137]. Researchers need to explore the
mechanical, physicochemical, and controlled release of collagen-based
active food packaging materials. Furthermore, alternatives in mamma­
lian gelatin such as fins, bones, warm and cold-water fish skins are
available from marine sources [138]. Byproducts of the fish-processing
industry such as fish skin can provide a valuable source of gelatin.
There are several advantages of using marine gelatin sources, including
the fact that they are not associated with outbreaks of Bovine Spongi­
form Encephalopathy, and Muslims are allowed to use fish gelatin, but
there are a few restrictions in Jews and Hindus. In order to improve
collagen and gelatin applications in the food industry, more efforts must
be made to meet the above mentioned challenges.
Funding
This work was supported by National Natural Science Foundation of
China (32250410297), Talent Introduction Program of Postdoctoral
International Exchange Program to Excellent International Young Re­
searchers by the Office of China Postdoc Council (OCPC) and the postdoc
office of the Zhejiang University, Hangzhou, China.
CRediT authorship contribution statement
Muhammad Ijaz Ahmad: Conceptualization, Investigation, Writing
– original draft. Yonghui Li: Investigation, Writing – review & editing.
M.I. Ahmad et al.
Jinfeng Pan: Investigation, Writing – review & editing. Fei Liu:
Investigation, Writing – review & editing. Hongjie Dai: Investigation,
Writing – review & editing. Yu Fu: Investigation, Writing – review &
editing. Tao Huang: Investigation, Writing – review & editing. Shahzad
Farooq: Investigation, Writing – review & editing. Hui Zhang: Re­
sources, Supervision, Writing – review & editing.
Declaration of competing interest
The authors declare that they have no competing interests.
Data availability
The datasets used and/or analyzed during the current study are
available from the corresponding author on reasonable request.
Acknowledgments
Not applicable.
References
[1] X. Shen, M. Zhang, B. Bhandari, Z. Gao, Novel technologies in utilization of
byproducts of animal food processing: a review, Crit. Rev. Food Sci. Nutr. 59 (21)
(2019) 3420–3430, https://doi.org/10.1080/10408398.2018.1493428.
[2] V.G. Gisbert, S. Benaglia, M.R. Uhlig, R. Proksch, R. Garcia, High-speed
nanomechanical mapping of the early stages of collagen growth by bimodal force
microscopy, ACS Nano 15 (1) (2021) 1850–1857, https://doi.org/10.1021/
acsnano.0c10159.
[3] Z.R. Li, B. Wang, C.F. Chi, Q.H. Zhang, Y.D. Gong, J.J. Tang, H.Y. Luo, G.F. Ding,
Isolation and characterization of acid soluble collagens and pepsin soluble
collagens from the skin and bone of Spanish mackerel (Scomberomorous
niphonius), Food Hydrocoll. 31 (1) (2013) 103–113, https://doi.org/10.1016/j.
foodhyd.2012.10.001.
[4] T. Hennet, Collagen glycosylation, Curr. Opin. Struct. Biol. 56 (2019) 131–138,
https://doi.org/10.1016/j.sbi.2019.01.015.
[5] C. Cao, Z. Xiao, C. Ge, Y. Wu, Animal by-products collagen and derived peptide,
as important components of innovative sustainable food systems-a
comprehensive review, Crit. Rev. Food Sci. Nutr. (2021) 1–25, https://doi.org/
10.1080/10408398.2021.1931807.
[6] L. Zhang, S. Zhang, H. Song, B. Li, Ingestion of collagen hydrolysates alleviates
skin chronological aging in an aged mouse model by increasing collagen
synthesis, Food Funct. 11 (6) (2020) 5573–5580, https://doi.org/10.1039/
D0FO00153H.
[7] M. Gómez-Guillén, B. Giménez, M.A. López-Caballero, M. Montero, Functional
and bioactive properties of collagen and gelatin from alternative sources: a
review, Food Hydrocoll. 25 (8) (2011) 1813–1827, https://doi.org/10.1016/j.
foodhyd.2011.02.007.
[8] L.C. Lv, Q.Y. Huang, W. Ding, X.H. Xiao, H.Y. Zhang, L.X. Xiong, Fish gelatin: the
novel potential applications, J. Funct. Foods 63 (2019), 103581, https://doi.org/
10.1016/j.jff.2019.103581.
[9] J. Cao, Q. Wang, T. Ma, K. Bao, X. Yu, Z. Duan, X. Shen, C. Li, Effect of EGCG-
gelatin biofilm on the quality and microbial composition of tilapia fillets during
chilled storage, Food Chem. 305 (2020), 125454, https://doi.org/10.1016/j.
foodchem.2019.125454.
[10] A. Sorushanova, L.M. Delgado, Z. Wu, N. Shologu, A. Kshirsagar, R. Raghunath,
A.M. Mullen, Y. Bayon, A. Pandit, M. Raghunath, The collagen suprafamily: from
biosynthesis to advanced biomaterial development, Adv. Mater. 31 (1) (2019)
1801651, https://doi.org/10.1002/adma.201801651.
[11] A.B. Shori, A.S. Baba, L.S. Hoen Solear, Allium sativum and fish collagen
enhanced proteolysis pattern of milk protein during cheddar cheese ripening,
J. Agric. Food Res. 2 (2020), 100059, https://doi.org/10.1016/j.
jafr.2020.100059.
[12] A.M.M. Ali, K. de la Caba, T. Prodpran, S. Benjakul, Quality characteristics of
fried fish crackers packaged in gelatin bags: effect of squalene and storage time,
Food Hydrocoll. 99 (2020), 105378, https://doi.org/10.1016/j.
foodhyd.2019.105378.
[13] A.R. Bunsell, Handbook of Properties of Textile and Technical Fibres, Woodhead
Publishing, 2018.
[14] A. Salem, N. Fakhfakh, M. Jridi, O. Abdelhedi, M. Nasri, F. Debeaufort, N. Zouari,
Microstructure and characteristic properties of dogfish skin gelatin gels prepared
by freeze/spray-drying methods, Int. J. Biol. Macromol. 162 (2020) 1–10,
https://doi.org/10.1016/j.ijbiomac.2020.06.033.
[15] R. Santana, F. Perrechil, A. Sato, R. Cunha, Emulsifying properties of collagen
fibers: effect of pH, protein concentration and homogenization pressure, Food
Hydrocoll. 25 (4) (2011) 604–612, https://doi.org/10.1016/j.
foodhyd.2010.07.018.
11
International Journal of Biological Macromolecules 254 (2024) 128037
[16] F. Liu, Z. Yu, B. Wang, B.S. Chiou, Changes in structures and properties of
collagen fibers during collagen casing film manufacturing, Foods 12 (9) (2023)
1847, https://doi.org/10.3390/foods12091847.
[17] X. Yan, L. Yang, Y. Zhang, W. Han, Y. Duan, Effect of collagen casing on the
quality characteristics of fermented sausage, PloS One 17 (2) (2022), e0263389.
[18] J. Tantala, K. Vangnai, P. Rachtanapun, C. Rachtanapun, Active antimicrobial
collagen casing, Ital J Food Sci (2019) 171–175.
[19] P. Suurs, S. Barbut, Collagen use for co-extruded sausage casings–a review,
Trends Food Sci. Technol. 102 (2020) 91–101, https://doi.org/10.1016/j.
tifs.2020.06.011.
[20] P. Suurs, H. van den Brand, R. ten Have, W.F. Daamen, S. Barbut, Evaluation of
cattle skin collagen for producing co-extrusion sausage casing, Food Hydrocol.
140 (2023), 108595, https://doi.org/10.1016/j.foodhyd.2023.108595.
[21] X. Zhao, X. Zhang, D. Liu, Collagen peptides and the related synthetic peptides: a
review on improving skin health, J. Funct. Foods 86 (2021), 104680, https://doi.
org/10.1016/j.jff.2021.104680.
[22] S. Cao, Y. Wang, Y. Hao, W. Zhang, G. Zhou, Antihypertensive effects in vitro and
in vivo of novel angiotensin-converting enzyme inhibitory peptides from bovine
bone gelatin hydrolysate, J. Agric. Food Chem. 68 (3) (2019) 759–768, https://
doi.org/10.1021/acs.jafc.9b05618.
[23] C. Tometsuka, N. Funato, K. Mizuno, Y. Taga, Long-term intake of ginger
protease-degraded collagen hydrolysate reduces blood lipid levels and adipocyte
size in mice, Curr. Res. Nutr. 4 (2021) 175–181, https://doi.org/10.1016/j.
crfs.2021.03.003.
[24] T.Y. Wang, C.H. Hsieh, C.C. Hung, C.L. Jao, M.C. Chen, K.C. Hsu, Fish skin gelatin
hydrolysates as dipeptidyl peptidase IV inhibitors and glucagon-like peptide-1
stimulators improve glycaemic control in diabetic rats: a comparison between
warm-and cold-water fish, J. Funct. Foods 19 (2015) 330–340, https://doi.org/
10.1016/j.jff.2015.09.037.
[25] G.N. Ramachandran, G. Kartha, Structure of collagen, Nature 174 (4423) (1954)
269–270.
[26] K. Gelse, E. Pöschl, T. Aigner, Collagens-structure, function, and biosynthesis,
Adv. Drug Deliv. Rev. 55 (12) (2003) 1531–1546, https://doi.org/10.1016/j.
addr.2003.08.002.
[27] C. Tang, K. Zhou, Y. Zhu, W. Zhang, Y. Xie, Z. Wang, H. Zhou, T. Yang, Q. Zhang,
B. Xu, Collagen and its derivatives: from structure and properties to their
applications in food industry, Food Hydrocoll. 107748 (2022), https://doi.org/
10.1016/j.foodhyd.2022.107748.
[28] J.Y. Exposito, U. Valcourt, C. Cluzel, C. Lethias, The fibrillar collagen family, Int.
J. Mol. Sci. 11 (2) (2010) 407–426, https://doi.org/10.3390/ijms11020407.
[29] D. Hulmes, Collagen diversity, synthesis and assembly, in: Collagen, Springer,
2008, pp. 15–47.
[30] J. Gaar, R. Naffa, M. Brimble, Enzymatic and non-enzymatic crosslinks found in
collagen and elastin and their chemical synthesis, Org. Chem. Front. 7 (18)
(2020) 2789–2814, https://doi.org/10.1039/D0QO00624F.
[31] X. Liu, C. Zheng, X. Luo, X. Wang, H. Jiang, Recent advances of collagen-based
biomaterials: multi-hierarchical structure, modification and biomedical
applications, Mater. Sci. Eng.: C 99 (2019) 1509–1522, https://doi.org/10.1016/
j.msec.2019.02.070.
[32] M. Yamauchi, M. Sricholpech, M. Terajima, K.B. Tomer, I. Perdivara,
Glycosylation of Type I Collagen, Post-Translational Modification of Proteins,
Springer, 2019, pp. 127–144.
[33] M.J. Mienaltowski, D.E. Birk, Structure, physiology, and biochemistry of
collagens, Progress in heritable soft connective tissue diseases, Adv. Exp. Med.
Biol. (2014) 5–29, https://doi.org/10.1007/978-94-007-7893-1_2.
[34] R. Kelwick, I. Desanlis, G.N. Wheeler, D.R. Edwards, The ADAMTS (a disintegrin
and metalloproteinase with thrombospondin motifs) family, Genome Biol. 16 (1)
(2015) 1–16, https://doi.org/10.1016/j.bcp.2019.03.033.
[35] A. Gautieri, S. Vesentini, A. Redaelli, M.J. Buehler, Hierarchical structure and
nanomechanics of collagen microfibrils from the atomistic scale up, Nano Lett. 11
(2) (2011) 757–766, https://doi.org/10.1021/nl103943u.
[36] A. Abedinia, A.M. Nafchi, M. Sharifi, P. Ghalambor, N. Oladzadabbasabadi,
F. Ariffin, N. Huda, Poultry gelatin: characteristics, developments, challenges,
and future outlooks as a sustainable alternative for mammalian gelatin, Trends
Food Sci 104 (2020) 14–26, https://doi.org/10.1016/j.tifs.2020.08.001.
[37] S. Zhu, J. Yu, S. Liu, Y. Ding, W. Wang, X. Zhou, A bottom-up evaluation on
cryoprotective potentials of gelatine from fish scale, Food Hydrocoll. 124 (2022),
107243, https://doi.org/10.1016/j.foodhyd.2021.107243.
[38] A. Duconseille, T. Astruc, N. Quintana, F. Meersman, V. Sante-Lhoutellier, Gelatin
structure and composition linked to hard capsule dissolution: a review, Food
Hydrocoll. 43 (2015) 360–376, https://doi.org/10.1016/j.foodhyd.2014.06.006.
[39] Y. Maki, M. Annaka, Gelation of fish gelatin studied by multi-particle tracking
method, Food Hydrocoll. 101 (2020), 105525, https://doi.org/10.1016/j.
foodhyd.2019.105525.
[40] P.R. Avallone, E. Raccone, S. Costanzo, M. Delmonte, A. Sarrica, R. Pasquino,
N. Grizzuti, Gelation kinetics of aqueous gelatin solutions in isothermal
conditions via rheological tools, Food Hydrocoll. 111 (2021), 106248, https://
doi.org/10.1016/j.foodhyd.2020.106248.
[41] C. Qiao, X. Wang, J. Zhang, J. Yao, Influence of salts in the Hofmeister series on
the physical gelation behavior of gelatin in aqueous solutions, Food Hydrocoll.
110 (2021), 106150, https://doi.org/10.1016/j.foodhyd.2020.106150.
[42] S. Ricard-Blum, Cold spring harbor perspect, Biol 3 (1) (2011), a004978.
[43] J. Alipal, N.M. Pu’Ad, T. Lee, N. Nayan, N. Sahari, H. Basri, M. Idris, H. Abdullah,
A review of gelatin: properties, sources, process, applications, and
commercialisation, Materials Today: Proceedings 42 (2021) 240–250, https://
doi.org/10.1016/j.matpr.2020.12.922.
M.I. Ahmad et al.
[44] S. Gorgieva, V. Kokol, Collagen vs. gelatine-based biomaterials and their
biocompatibility: review and perspectives, Biomater. Appl.nanomedicin. 2 (2011)
17–52.
[45] G.O. Phillips, P.A. Williams, Handbook of Food Proteins, Elsevier, 2011, https://
doi.org/10.5772/24118.
[46] C.N. Grover, R.E. Cameron, S.M. Best, Investigating the morphological,
mechanical and degradation properties of scaffolds comprising collagen, gelatin
and elastin for use in soft tissue engineering, J. Mech. Behav. Biomed. Mater. 10
(2012) 62–74, https://doi.org/10.1016/j.jmbbm.2012.02.028.
[47] D. Liu, M. Nikoo, G. Boran, P. Zhou, J.M. Regenstein, Collagen and gelatin, Annu
Rev Food Sci. Technol. 6 (2015) 527–557, https://doi.org/10.1146/annurev-
food-031414-111800.
[48] J. Ratanavaraporn, S. Damrongsakkul, N. Sanchavanakit, T. Banaprasert,
S. Kanokpanont, Comparison of gelatin and collagen scaffolds for fibroblast cell
culture, J. Met. Mater. Miner. 16 (1) (2006).
[49] Z. Zhang, G. Li, B. Shi, Physicochemical properties of collagen, gelatin and
collagen hydrolysate derived from bovine limed split wastes, J. Soc. Leath. Tech.
Ch. 90 (1) (2006) 23.
[50] M.I. Avila Rodríguez, L.G. Rodríguez Barroso, M.L. Sánchez, Collagen: a review
on its sources and potential cosmetic applications, J. Cosmet. Dermatol. 17 (1)
(2018) 20–26, https://doi.org/10.1111/jocd.12450.
[51] Y. Jiang, H. Wang, M. Deng, Z. Wang, J. Zhang, H. Wang, H. Zhang, Effect of
ultrasonication on the fibril-formation and gel properties of collagen from grass
carp skin, Mater. Sci. Eng. C 59 (2016) 1038–1046, https://doi.org/10.1016/j.
msec.2015.11.007.
[52] J. Xu, F. Liu, H.D. Goff, F. Zhong, Effect of pre-treatment temperatures on the
film-forming properties of collagen fiber dispersions, Food Hydrocoll. 107 (2020),
105326, https://doi.org/10.1016/j.foodhyd.2019.105326.
[53] S. Zhu, X. Yu, J. You, T. Yin, Y. Lin, W. Chen, L. Dao, H. Du, R. Liu, S. Xiong, Study
of the thermodynamics and conformational changes of collagen molecules upon
self-assembly, Food Hydrocoll. 114 (2021), 106576, https://doi.org/10.1016/j.
foodhyd.2020.106576.
[54] S. Zhu, Q. Yuan, T. Yin, J. You, Z. Gu, S. Xiong, Y. Hu, Self-assembly of collagen-
based biomaterials: preparation, characterizations and biomedical applications,
J. Mater. Chem. B 6 (18) (2018) 2650–2676, https://doi.org/10.1039/
C7TB02999C.
[55] M. Yan, B. Li, X. Zhao, S. Qin, Effect of concentration, pH and ionic strength on
the kinetic self-assembly of acid-soluble collagen from walleye Pollock (Theragra
chalcogramma) skin, Food Hydrocoll. 29 (1) (2012) 199–204, https://doi.org/
10.1016/j.foodhyd.2012.02.014.
[56] D. Gunasekaran, R. Thada, G.F.S. Jeyakumar, N.P. Manimegalai, G. Shanmugam,
U.T. Sivagnanam, Physicochemical characterization and self-assembly of human
amniotic membrane and umbilical cord collagen: a comparative study, Int. J.
Biol. Macromol. 165 (2020) 2920–2933, https://doi.org/10.1016/j.
ijbiomac.2020.10.107.
[57] M. Yan, S. Qin, J. Li, Study on the self-assembly property of type I collagen
prepared from tilapia (Oreochromis niloticus) skin by different extraction methods,
Int. J. Food Sci. Technol. 50 (9) (2015) 2088–2096, https://doi.org/10.1111/
ijfs.12870.
[58] L. He, W. Lan, Y. Wang, S. Ahmed, Y. Liu, Extraction and characterization of self-
assembled collagen isolated from grass carp and crucian carp, Foods 8 (9) (2019)
396, https://doi.org/10.3390/foods8090396.
[59] Y. Ran, W. Su, L. Ma, X. Wang, X. Li, Insight into the effect of sulfonated chitosan
on the structure, rheology and fibrillogenesis of collagen, Int. J. Biol. Macromol.
166 (2021) 1480–1490, https://doi.org/10.1016/j.ijbiomac.2020.11.027.
[60] H. Tian, Z. Ren, L. Shi, G. Hao, J. Chen, W. Weng, Self-assembly characterization
of tilapia skin collagen in simulated body fluid with different salt concentrations,
Process Biochem. 108 (2021) 153–160, https://doi.org/10.1016/j.
procbio.2021.06.013.
[61] Y. Li, A. Asadi, M.R. Monroe, E.P. Douglas, pH effects on collagen fibrillogenesis
in vitro: electrostatic interactions and phosphate binding, Mater. Sci. Eng. C 29
(5) (2009) 1643–1649, https://doi.org/10.1016/j.msec.2009.01.001.
[62] L. Zhu, J. Li, Y. Wang, X. Sun, B. Li, S. Poungchawanwong, H. Hou, Structural
feature and self-assembly properties of type II collagens from the cartilages of
skate and sturgeon, Food Chem. 331 (2020), 127340, https://doi.org/10.1016/j.
foodchem.2020.127340.
[63] C. Mutlu, S.A. Tontul, M. Erbaş, Production of a minimally processed jelly candy
for children using honey instead of sugar, LWT 93 (2018) 499–505, https://doi.
org/10.1016/j.lwt.2018.03.064.
[64] R.Y. Essa, E.M. Elsebaie, New fat replacement agent comprised of gelatin and
soluble dietary fibers derived from date seed powder in beef burger preparation,
LWT 156 (2022), 113051, https://doi.org/10.1016/j.lwt.2021.113051.
[65] M.C. Gómez-Guillén, B. Giménez, M.E. López-Caballero, M.P. Montero,
Functional and bioactive properties of collagen and gelatin from alternative
sources: a review, Food Hydrocoll. 25 (8) (2011) 1813–1827, https://doi.org/
10.1016/j.foodhyd.2011.02.007.
[66] X. Feng, C. Fu, H. Yang, Gelatin addition improves the nutrient retention, texture
and mass transfer of fish balls without altering their nanostructure during boiling,
LWT 77 (2017) 142–151, https://doi.org/10.1016/j.lwt.2016.11.024.
[67] Z. Pang, H. Deeth, H. Yang, S. Prakash, N. Bansal, Evaluation of tilapia skin
gelatin as a mammalian gelatin replacer in acid milk gels and low-fat stirred
yogurt, J. Dairy Sci. 100 (5) (2017) 3436–3447, https://doi.org/10.3168/
jds.2016-11881.
[68] N. Carvajal-Mena, G. Tabilo-Munizaga, M. Pérez-Won, R. Lemus-Mondaca,
Valorization of salmon industry by-products: evaluation of salmon skin gelatin as
12
International Journal of Biological Macromolecules 254 (2024) 128037
a biomaterial suitable for 3D food printing, LWT 155 (2022), 112931, https://doi.
org/10.1016/j.lwt.2021.112931.
[69] A.N. Akram, C. Zhang, Effect of ultrasonication on the yield, functional and
physicochemical characteristics of collagen-II from chicken sternal cartilage,
Food Chem. 307 (2020), 125544, https://doi.org/10.1016/j.
foodchem.2019.125544.
[70] T.K. Kim, K.E. Hwang, J.M. Sung, J.D. Park, M.H. Kim, K.H. Jeon, Y.B. Kim, Y.
S. Choi, Replacement of pork back fat with pre-emulsion of wheat (Triticum
aestivum L.) sprout and collagen and its optimization for reduced-fat patties 42 (4)
(2018), e13576, https://doi.org/10.1111/jfpp.13576.
[71] Moncef Nasri, Mourad Jridi, B. Slama, Rim Rabeb, Nabil Souissi, N.J.L.F. Science,
Technology, Effects of the edible cuttlefish gelatin on textural, sensorial and
physicochemical quality of octopus sausage, LWT (2016) 18–24, https://doi.org/
10.1016/j.lwt.2015.07.051.
[72] D.S. Atik, M. Demirci, Ö.S. Toker, I. Palabiyik, Development of a novel
rheological method for determining melting properties of gelatin-based gummies,
Int. J. Biol. Macromol. 209 (2022) 385–395, https://doi.org/10.1016/j.
ijbiomac.2022.04.002.
[73] M. Mardani, S. Yeganehzad, N. Ptichkina, Y. Kodatsky, O. Kliukina,
N. Nepovinnykh, S. Naji-Tabasi, Study on foaming, rheological and thermal
properties of gelatin-free marshmallow, Food Hydrocoll. 93 (2019) 335–341,
https://doi.org/10.1016/j.foodhyd.2019.02.033.
[74] R. Duan, J. Zhang, L. Liu, W. Cui, J.M. Regenstein, The functional properties and
application of gelatin derived from the skin of channel catfish (Ictalurus
punctatus), Food Chem. 239 (2018) 464–469, https://doi.org/10.1016/j.
foodchem.2017.06.145.
[75] W. Yu, D. Xu, H. Zhang, L. Guo, T. Hong, W. Zhang, Y. Jin, X. Xu, Effect of pigskin
gelatin on baking, structural and thermal properties of frozen dough:
comprehensive studies on alteration of gluten network, Food Hydrocoll. 102
(2020), 105591, https://doi.org/10.1016/j.foodhyd.2019.105591.
[76] J. Alipal, N.A.S. Mohd Pu’ad, T.C. Lee, N.H.M. Nayan, N. Sahari, H. Basri, M.
I. Idris, H.Z. Abdullah, A review of gelatin: properties, sources, process,
applications, and commercialisation, Mater. Today: Proc. 42 (2021) 240–250,
https://doi.org/10.1016/j.matpr.2020.12.922.
[77] Z. Pang, H. Deeth, R. Sharma, N. Bansal, Effect of addition of gelatin on the
rheological and microstructural properties of acid milk protein gels, Food
Hydrocoll. 43 (2015) 340–351, https://doi.org/10.1016/j.foodhyd.2014.06.005.
[78] S. Damodaran, S. Wang, Ice crystal growth inhibition by peptides from fish
gelatin hydrolysate, Food Hydrocoll. 70 (2017) 46–56, https://doi.org/10.1016/
j.foodhyd.2017.03.029.
[79] B. Duquenne, B. Vergauwen, C. Capdepon, M.A. Boone, T. De Schryver, L. Van
Hoorebeke, S. Van Weyenberg, P. Stevens, J. De Block, Stabilising frozen dairy
mousses by low molecular weight gelatin peptides, Food Hydrocoll. 60 (2016)
317–323, https://doi.org/10.1016/j.foodhyd.2016.04.001.
[80] R. Schrieber, H. Gareis, Gelatine Handbook: Theory and Industrial Practice, John
Wiley & Sons, 2007.
[81] O.S. Deshmukh, D. van den Ende, M.C. Stuart, F. Mugele, M.H. Duits, Hard and
soft colloids at fluid interfaces: adsorption, interactions, assembly & rheology,
Adv. Colloid Interface Sci. 222 (2015) 215–227, https://doi.org/10.1016/j.
cis.2014.09.003.
[82] T. Zhang, J. Xu, Y. Zhang, X. Wang, J.M. Lorenzo, J. Zhong, Gelatins as
emulsifiers for oil-in-water emulsions: extraction, chemical composition,
molecular structure, and molecular modification, Trends Food Sci 106 (2020)
113–131, https://doi.org/10.1016/j.tifs.2020.10.005.
[83] P. Dey, S. Kadharbasha, M. Bajaj, J. Das, T. Chakraborty, C. Bhat, P. Banerjee,
Contribution of quasifibrillar properties of collagen hydrolysates towards
lowering of interface tension in emulsion-based food leading to shelf-life
enhancement, Food Bioproc. Tech. 14 (8) (2021) 1566–1586, https://doi.org/
10.1007/s11947-021-02640-z.
[84] X. Feng, H. Dai, L. Ma, Y. Fu, Y. Yu, H. Zhu, H. Wang, Y. Sun, H. Tan, Y. Zhang,
Effect of drying methods on the solubility and amphiphilicity of room
temperature soluble gelatin extracted by microwave-rapid freezing-thawing
coupling, Food Chem. 351 (2021), 129226, https://doi.org/10.1016/j.
foodchem.2021.129226.
[85] T. Zhang, R. Sun, M. Ding, L. Li, N. Tao, X. Wang, J. Zhong, Commercial cold-
water fish skin gelatin and bovine bone gelatin: structural, functional, and
emulsion stability differences, LWT 125 (2020), 109207, https://doi.org/
10.1016/j.lwt.2020.109207.
[86] T. Zhang, R. Sun, M. Ding, L. Tao, L. Liu, N. Tao, X. Wang, J. Zhong, Effect of
extraction methods on the structural characteristics, functional properties, and
emulsion stabilization ability of Tilapia skin gelatins, Food Chem. 328 (2020),
127114, https://doi.org/10.1016/j.foodchem.2020.127114.
[87] Z. Song, H. Liu, A. Huang, C. Zhou, P. Hong, C. Deng, Collagen/zein electrospun
films incorporated with gallic acid for tilapia (Oreochromis niloticus) muscle
preservation, J. Food Eng. 317 (2022), 110860, https://doi.org/10.1016/j.
jfoodeng.2021.110860.
[88] Z. Wang, S. Hu, Y. Gao, C. Ye, H. Wang, Effect of collagen-lysozyme coating on
fresh-salmon fillets preservation, LWT 75 (2017) 59–64, https://doi.org/
10.1016/j.lwt.2016.08.032.
[89] J. Liu, M. Shibata, Q. Ma, F. Liu, Q. Lu, Q. Shan, T. Hagiwara, J. Bao,
Characterization of fish collagen from blue shark skin and its application for
chitosan-collagen composite coating to preserve red porgy (Pagrus major) meat,
J. Food Biochem. 44 (8) (2020), e13265.
[90] E. Mohebi, Y. Shahbazi, Application of chitosan and gelatin based active
packaging films for peeled shrimp preservation: a novel functional wrapping
design, LWT 76 (2017) 108–116, https://doi.org/10.1016/j.lwt.2016.10.062.
M.I. Ahmad et al.
[91] Y. Xiong, M. Chen, R.D. Warner, Z. Fang, Incorporating nisin and grape seed
extract in chitosan-gelatine edible coating and its effect on cold storage of fresh
pork, Food Control 110 (2020), 107018, https://doi.org/10.1016/j.
foodcont.2019.107018.
[92] Y. Liu, R. Wang, D. Wang, Z. Sun, F. Liu, D. Zhang, D. Wang, Development of a
food packaging antibacterial hydrogel based on gelatin, chitosan, and 3-phenyl­
lactic acid for the shelf-life extension of chilled chicken, Food Hydrocoll. 127
(2022), 107546, https://doi.org/10.1016/j.foodhyd.2022.107546.
[93] T. Zhang, Z. Yu, Y. Ma, B.S. Chiou, F. Liu, F. Zhong, Modulating physicochemical
properties of collagen films by cross-linking with glutaraldehyde at varied pH
values, Food Hydrocoll. 124 (2022), 107270, https://doi.org/10.1016/j.
foodhyd.2021.107270.
[94] S.R. Kanatt, Development of active/intelligent food packaging film containing
Amaranthus leaf extract for shelf life extension of chicken/fish during chilled
storage, Food Packag. Shelf Life 24 (2020), 100506, https://doi.org/10.1016/j.
fpsl.2020.100506.
[95] X. Ye, H. Xiao, Y. Wang, L. Ke, W. Luo, X. Huang, B. Shi, Efficient separation of
viscous emulsion through amphiprotic collagen nanofibers-based membrane,
J. Membr. Sci. 588 (2019), 117209, https://doi.org/10.1016/j.
memsci.2019.117209.
[96] S. Yang, X. Shi, X. Li, J. Wang, Y. Wang, Y. Luo, Oriented collagen fiber
membranes formed through counter-rotating extrusion and their application in
tendon regeneration, Biomaterials 207 (2019) 61–75, https://doi.org/10.1016/j.
biomaterials.2019.03.041.
[97] J. Wu, F. Liu, Z. Yu, Y. Ma, H.D. Goff, J. Ma, F. Zhong, Facile preparation of
collagen fiber–glycerol-carboxymethyl cellulose composite film by immersing
method, Carbohydr. Polym. 229 (2020), 115429, https://doi.org/10.1016/j.
carbpol.2019.115429.
[98] Y. Ma, A. Teng, K. Zhao, K. Zhang, H. Zhao, S. Duan, S. Li, Y. Guo, W. Wang,
A top-down approach to improve collagen film’s performance: the comparisons of
macro, micro and nano sized fibers, Food Chem. 309 (2020), 125624, https://doi.
org/10.1016/j.foodchem.2019.125624.
[99] A. Abedinia, F. Ariffin, N. Huda, A. Mohammadi Nafchi, Preparation and
characterization of a novel biocomposite based on duck feet gelatin as alternative
to bovine gelatin, Int. J. Biol. Macromol. 109 (2018) 855–862, https://doi.org/
10.1016/j.ijbiomac.2017.11.051.
[100] S.E. Herrera-Vázquez, O. Dublán-García, D. Arizmendi-Cotero, L.M. Gómez-
Oliván, H. Islas-Flores, M.D. Hernández-Navarro, N. Ramírez-Durán,
Optimization of the physical, optical and mechanical properties of composite
edible films of gelatin, whey protein and chitosan, Molecules 27 (3) (2022) 869,
https://doi.org/10.3390/molecules27030869.
[101] F. Liu, H. Majeed, J. Antoniou, Y. Li, Y. Ma, W. Yokoyama, J. Ma, F. Zhong,
Tailoring physical properties of transglutaminase-modified gelatin films by
varying drying temperature, Food Hydrocoll. 58 (2016) 20–28, https://doi.org/
10.1016/j.foodhyd.2016.01.026.
[102] M. Djabourov, J.P. Lechaire, F. Gaill, Structure and rheology of gelatin and
collagen gels, Biorheology 30 (3–4) (1993) 191–205, https://doi.org/10.3233/
bir-1993-303-405.
[103] M. Yan, X. Jiang, G. Wang, A. Wang, X. Wang, X. Wang, X. Zhao, H. Xu, X. An,
Y. Li, Preparation of self-assembled collagen fibrillar gel from tilapia skin and its
formation in presence of acidic polysaccharides, Carbohydr. Polym. 233 (2020),
115831, https://doi.org/10.1016/j.carbpol.2020.115831.
[104] L. Shi, H. Tian, Y. Wang, G. Hao, J. Chen, W. Weng, Effect of pH on properties of
golden pompano skin collagen-based fibril gels by self-assembly in vitro, J. Sci.
Food Agric. 100 (13) (2020) 4801–4807, https://doi.org/10.1002/jsfa.10539.
[105] C.B. Raub, V. Suresh, T. Krasieva, J. Lyubovitsky, J.D. Mih, A.J. Putnam, B.
J. Tromberg, S.C. George, Noninvasive assessment of collagen gel microstructure
and mechanics using multiphoton microscopy, Biophys. J. 92 (6) (2007)
2212–2222, https://doi.org/10.1529/biophysj.106.097998.
[106] C. Xu, X. Wei, F. Shu, X. Li, W. Wang, P. Li, Y. Li, S. Li, J. Zhang, H. Wang,
Induction of fiber-like aggregation and gelation of collagen by ultraviolet
irradiation at low temperature, Int. J. Biol. Macromol. 153 (2020) 232–239,
https://doi.org/10.1016/j.ijbiomac.2020.03.012.
[107] L. Guo, R.H. Colby, C.P. Lusignan, T.H. Whitesides, Kinetics of triple helix
formation in semidilute gelatin solutions, Macromolecules 36 (26) (2003)
9999–10008, https://doi.org/10.1021/ma034264s.
[108] C. Joly-Duhamel, D. Hellio, M. Djabourov, All gelatin networks: 1. Biodiversity
and physical chemistry, Langmuir 18 (19) (2002) 7208–7217, https://doi.org/
10.1021/la020189n.
[109] M. Djabourov, J. Leblond, P. Papon, Gelation of aqueous gelatin solutions. I.
Structural investigation, Journal de Physique 49 (2) (1988) 319–332.
[110] M. Jridi, O. Abdelhedi, N. Souissi, M. Kammoun, M. Nasri, Mohamed A. Ayadi,
Improvement of the physicochemical, textural and sensory properties of meat
sausage by edible cuttlefish gelatin addition, Food Biosci. 12 (2015) 67–72,
https://doi.org/10.1016/j.fbio.2015.07.007.
[111] C.H. Lee, K.B. Chin, Effects of pork gelatin levels on the physicochemical and
textural properties of model sausages at different fat levels, LWT 74 (2016)
325–330, https://doi.org/10.1016/j.lwt.2016.07.032.
[112] Y. Gao, Y. Qiu, H. Nan, L. Wang, D. Yang, L. Zhang, Q. Yu, Ultra-high pressure-
assisted preparation of cowhide gelatin as a promising fat substitute: improve the
nutrition ratio and antioxidant capacity of beef patties, Food Res. Int. 157 (2022),
111260, https://doi.org/10.1016/j.foodres.2022.111260.
[113] C.H. Lee, K.B. Chin, Development of low-fat sausages using basil seed gum
(Ocimum bacilicum L.) and gelatin as a fat replacer, Int. J. Food Sci. 52 (3) (2017)
733–740, https://doi.org/10.1111/ijfs.13328.
13
International Journal of Biological Macromolecules 254 (2024) 128037
[114] P. Kaewudom, S. Benjakul, K. Kijroongrojana, Effect of bovine and fish gelatin in
combination with microbial transglutaminase on gel properties of threadfin
bream surimi, Int. Aquat. Res. 4 (1) (2012) 12, https://doi.org/10.1186/2008-
6970-4-12.
[115] H. Yuping, W. Wuyin, Z. Xichun, Effects of fish skin gelatin on gel property of
surimi from freshwater fish, J. Chin. Inst. Food Sci. Technol. 12 (11) (2013)
51–58, https://doi.org/10.1016/j.foodhyd.2009.07.002.
[116] P. Kittiphattanabawon, S. Benjakul, W. Visessanguan, F. Shahidi, Cryoprotective
effect of gelatin hydrolysate from blacktip shark skin on surimi subjected to
different freeze-thaw cycles, LWT 47 (2) (2012) 437–442, https://doi.org/
10.1016/j.lwt.2012.02.003.
[117] K. Limpisophon, H. Iguchi, M. Tanaka, T. Suzuki, E. Okazaki, T. Saito,
K. Takahashi, K. Osako, Cryoprotective effect of gelatin hydrolysate from shark
skin on denaturation of frozen surimi compared with that from bovine skin,
Fisheries Sci. 81 (2) (2015) 383–392, https://doi.org/10.1007/s12562-014-0844-
5.
[118] M. Yin, D. Yang, S. Lai, H. Yang, Rheological properties of xanthan-modified fish
gelatin and its potential to replace mammalian gelatin in low-fat stirred yogurt,
LWT 147 (2021), 111643, https://doi.org/10.1016/j.lwt.2021.111643.
[119] W. Yu, D. Xu, D. Li, L. Guo, X. Su, Y. Zhang, F. Wu, X. Xu, Effect of pigskin-
originated gelatin on properties of wheat flour dough and bread, Food Hydrocol.
94 (2019) 183–190, https://doi.org/10.1016/J.FOODHYD.2019.03.016.
[120] J. Bi, H. Li, H. Wang, Delayed bitterness of citrus wine is removed through the
selection of fining agents and fining optimization, Front. Chem. 7 (2019) 185,
https://doi.org/10.3389/fchem.2019.00185.
[121] P.F. Almeida, S.C.D.S. Lannes, Effects of chicken by-product gelatin on the
physicochemical properties and texture of chocolate spread, J. Texture Stud. 48
(5) (2017) 392–402, https://doi.org/10.1111/jtxs.12242.
[122] M.G. Gallego, M.H. Gordon, F. Segovia, M.P. Almajano Pablos, Gelatine-Based
antioxidant packaging containing Caesalpinia decapetala and tara as a coating for
ground beef patties, Antioxidants (Basel, Switzerland) 5 (2) (2016), https://doi.
org/10.3390/antiox5020010.
[123] M. Aitboulahsen, S. Zantar, A. Laglaoui, H. Chairi, A. Arakrak, M. Bakkali,
M. Hassani Zerrouk, Gelatin-based edible coating combined with Mentha pulegium
essential oil as bioactive packaging for strawberries, J. Food Qual. 2018 (2018),
https://doi.org/10.1155/2018/8408915.
[124] G.P. Cardoso, M.P. Dutra, P.R. Fontes, A.D.L.S. Ramos, L.A. de Miranda Gomide,
E.M. Ramos, Selection of a chitosan gelatin-based edible coating for color
preservation of beef in retail display, Meat Sci. 114 (2016) 85–94, https://doi.
org/10.1016/j.meatsci.2015.12.012.
[125] Á.M. Lima, M.A. Cerqueira, B.W. Souza, E.C.M. Santos, J.A. Teixeira, R.
A. Moreira, A.A. Vicente, New edible coatings composed of galactomannans and
collagen blends to improve the postharvest quality of fruits–influence on fruits gas
transfer rate, J. Food Eng. 97 (1) (2010) 101–109, https://doi.org/10.1016/j.
jfoodeng.2009.09.021.
[126] P. Dey, S. Kadharbasha, M. Bajaj, J. Das, T. Chakraborty, C. Bhat, P. Banerjee,
Contribution of Quasifibrillar properties of collagen hydrolysates towards
lowering of Interface tension in emulsion-based food leading to shelf-life
enhancement, Food Bioproc. Tech. 14 (2021) 1566–1586, https://doi.org/
10.1007/s11947-021-02640-z.
[127] S.C. Sousa, S.P. Fragoso, C.R. Penna, N.M. Arcanjo, F.A. Silva, V.C. Ferreira, M.
D. Barreto, Í.B. Araújo, Quality parameters of frankfurter-type sausages with
partial replacement of fat by hydrolyzed collagen, LWT 76 (2017) 320–325,
https://doi.org/10.1016/j.lwt.2016.06.034.
[128] X. Chen, J.H. Wu, L. Li, S.Y. Wang, The cryoprotective effects of antifreeze
peptides from pigskin collagen on texture properties and water mobility of frozen
dough subjected to freeze–thaw cycles, Eur. Food Res. Technol. 243 (2017)
1149–1156, https://doi.org/10.1007/s00217-016-2830-x.
[129] J.M. Tan, M.H. Lim, Effects of gelatine type and concentration on the shelf-life
stability and quality of marshmallows, Int. J. Food Sci. Technol. 43 (9) (2008)
1699–1704, https://doi.org/10.1111/j.1365-2621.2008.01756.x.
[130] P.F. Almeida, S.C.D.S. Lannes, Effects of chicken by-product gelatin on the
physicochemical properties and texture of chocolate spread, J. Texture Stud. 48
(5) (2017) 392–402, https://doi.org/10.1111/jtxs.12242.
[131] C. Ghanem, P. Taillandier, M. Rizk, Z. Rizk, N. Nehme, J.P. Souchard, Y. El
Rayess, Analysis of the impact of fining agents types, oenological tannins and
mannoproteins and their concentrations on the phenolic composition of red wine,
LWT 83 (2017) 101–109, https://doi.org/10.1016/j.lwt.2017.05.009.
[132] I. Lassoued, M. Jridi, R. Nasri, A. Dammak, M. Hajji, M. Nasri, A. Barkia,
Characteristics and functional properties of gelatin from thornback ray skin
obtained by pepsin-aided process in comparison with commercial halal bovine
gelatin, Food Hydrocoll. 41 (2014) 309–318, https://doi.org/10.1016/j.
foodhyd.2014.04.029.
[133] M. Ramezani, G. Ferrentino, K. Morozova, S.M.H. Kamrul, M. Scampicchio,
Clarification of apple juices with vegetable proteins monitored by multiple light
scattering, J. Food Sci. 85 (2) (2020) 316–323, https://doi.org/10.1111/1750-
3841.14984.
[134] Z. Fang, M. Zhang, W. Du, J. Sun, Effect of fining and filtration on the haze
formation in bayberry (Myrica rubra Sieb. Et Zucc.) juice, J. Agric. Food Chem. 55
(1) (2007) 113–119, https://doi.org/10.1021/jf062699j.
[135] W. Yu, D. Xu, D. Li, L. Guo, X. Su, Y. Zhang, F. Wu, X. Xu, Effect of pigskin-
originated gelatin on properties of wheat flour dough and bread, Food Hydrocoll.
94 (2019) 183–190, https://doi.org/10.1016/j.foodhyd.2019.03.016.
M.I. Ahmad et al. International Journal of Biological Macromolecules 254 (2024) 128037

[136] S. Sang, C. Ou, Y. Fu, X. Su, Y. Jin, X. Xu, Complexation of fish skin gelatin with [138] A.A. Karim, R. Bhat, Fish gelatin: properties, challenges, and prospects as an
glutentin and its effect on the properties of wheat dough and bread, Food Chem: X alternative to mammalian gelatins, Food Hydrocoll. 23 (3) (2009) 563–576,
14 (2022), 100319, https://doi.org/10.1016/j.fochx.2022.100319. https://doi.org/10.1016/j.foodhyd.2008.07.002.
[137] B. Zhou, Y. Dai, D. Guo, J. Zhang, H. Liang, B. Li, J. Sun, J. Wu, Effect of desalted
egg white and gelatin mixture system on frozen dough, Food Hydrocoll. 132
(2022), 107889, https://doi.org/10.1016/j.foodhyd.2022.107889.

14