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Rajabimashhadi, Z.;  Gallo, N.;  Salvatore, L.;  Lionetto, F. Collagen Derived from Fish Industry Waste. Encyclopedia. Available online: https://encyclopedia.pub/entry/40871 (accessed on 20 May 2024).
Rajabimashhadi Z,  Gallo N,  Salvatore L,  Lionetto F. Collagen Derived from Fish Industry Waste. Encyclopedia. Available at: https://encyclopedia.pub/entry/40871. Accessed May 20, 2024.
Rajabimashhadi, Zahra, Nunzia Gallo, Luca Salvatore, Francesca Lionetto. "Collagen Derived from Fish Industry Waste" Encyclopedia, https://encyclopedia.pub/entry/40871 (accessed May 20, 2024).
Rajabimashhadi, Z.,  Gallo, N.,  Salvatore, L., & Lionetto, F. (2023, February 06). Collagen Derived from Fish Industry Waste. In Encyclopedia. https://encyclopedia.pub/entry/40871
Rajabimashhadi, Zahra, et al. "Collagen Derived from Fish Industry Waste." Encyclopedia. Web. 06 February, 2023.
Collagen Derived from Fish Industry Waste
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Fish collagen garnered significant academic and commercial featuring prospective applications in a variety of health-related industries, including food, medicine, pharmaceutics, and cosmetics. Due to its distinct advantages over mammalian-based collagen, including the reduced zoonosis transmission risk, the absence of cultural-religious limitations, the cost-effectiveness of manufacturing process, and its superior bioavailability, the use of collagen derived from fish wastes (i.e., skin, scales) quickly expanded. Moreover, by-products are low cost and the need to minimize fish industry waste’s environmental impact paved the way for the use of discards in the development of collagen-based products with remarkable added value.

fish collagen fish industry waste collagen extraction

1. Introduction

In order to exploit natural resources as much as possible, a long-term plan titled “Blue Growth” was approved by the European Commission and has been implemented to pay particular attention to fish resources in order to preserve the environment from industrial pollution. The enormous amount of valuable protein that could be extracted [1][2][3][4][5] (about 30–40% of the total weight), is one of the most appealing aspects of seafood by-products. More than 20 million tons of them are produced annually from the fish tissues that are discarded as waste, including fins, heads, skin, and viscera [6][7][8]. Because of their elevated protein content, absence of disease transmission risks, high bioactivity, and less considerable religious and ethical restrictions, the use of fish by-products as a new source of collagen has drawn increasing attention [9][10][11].
The importance of both aquaculture and fishing to food security is expanding continuously, particularly in light of the rising global fish production and the United Nations’ 2030 program of sustainable development [12]. Approximately 70% of fish and other seafood are processed before being sold, resulting in enormous amounts of solid waste from processes such as beheading, de-shelling, degutting, separating fin and scales, and filleting [13][14]. More than half of the weight of fresh fish becomes by-products of the fish industry. Most of these by-products are buried or burned, causing environmental, health, and economic issues. A minor portion are employed as inexpensive ingredients in animal feeds. Fish waste is a rising problem that requires quick, creative methods and solutions. Numerous initiatives and programs have been performed globally to prevent food waste. In addition to reducing the cost of waste disposal, investing in waste from the fish industry can offer the opportunity to recover other important substances such as oils, proteins, pigments, bioactive peptides, amino acids, collagen, chitin, gelatin, etc. [15][16][17].
More than two decades ago, research on the extraction of collagen from fish waste started to be conducted. Collagens are one of the most abundant proteins in animals, which are found in the extracellular matrix of connective tissues, including skin, bones, tendons, ligaments, cartilage, intervertebral discs, and blood vessels [18]. Collagens are not only implicated in tissue architecture maintenance and strength, but they also cover regulatory roles (i.e., through mechano-chemical transduction mechanisms) during tissue growth and repair [19][20]. Thanks to their nature, collagens are intrinsically bioactive, biocompatible, and biodegradable [21]. Hence, collagens are valued as the most commonly required and used biomaterials in many fields, including medical, cosmetic, nutraceutical, food and pharmaceutical industries in the forms of injectable solutions, thin substrates, porous sponges, nanofibrous matrices, and micro- and nano-spheres [22][23][24][25]. Recent studies revealed many similarities in the molecular structure and biochemical properties between collagen derived from fish and mammalian sources, despite the fact that fish collagen typically has a lower molecular weight and lower denaturation temperature than mammalian collagen [8][12][20][22][24][26][27][28]. Various extraction techniques for fish collagen have been developed depending on the selected tissue type and fish species. Hence, a considerable collection of literature has been developed on this subject [29][30][31]. Only in the past five years have researchers concentrated on innovative materials with improved characteristics in addition to developing extraction techniques for mass manufacture.
Collagen nanotechnology has a bright outlook because science in this area is always progressing and will continue to do so in the future. Nano collagen is ordinary collagen that has been sized down to a nanometer scale [32][33]. According to its nano-scale-based technology, which offers a high surface-area-to-volume ratio, an optimal penetration into wound sites and higher cell interaction is enabled. [34]. Moreover, nano collagen has the ability to deliver drugs and to supply a durable microenvironment at wounded sites to promote cellular regrowth and healing [35]. Collagen nanotechnology still presents many shortcomings, including the fact that only a small minority of therapeutic compounds have received commercial approval and that there are still numerous unsolved problems [32]. The complexity of pathophysiological symptoms and the lack of data on its real physiological effects is a further challenge for nanotechnology. Despite these downsides, nanotechnology is still a growing trend, with a huge amount of unrealized potential. This gives rise to the expectation that further research will assist in minimizing these downsides, leading to the creation of secure and efficient nano-based systems. In order to create approved therapeutic agents that take advantage of nanotechnology, additional research and studies must be performed [32]. Indeed, Figure 1 reveals the continuous increasing research interest on collagen, fish collagen, and nano collagen investigation in the last twenty years. In particular, it appears clear that there has been a significant increase in scientific works in the last five years. Nano collagen can be used for a variety of improvements and treatments, such as bone grafting, drug delivery, nerve tissue formation, vascular grafting, articular cartilage regeneration, cosmetics, and wound healing [21][22][36]. It is clear that nano collagen is a progressed type of nanotechnology; thus, further investigation must be attempted to advance this technology with the expectation that, in the future, nano collagen scaffolds will be more widely available [37].
Figure 1. Increasing research interest in fish collagen (MC) and nano collagen (NC) compared with collagen (C), according to scientific papers analyzed by publication year in the last twenty years up to 2022 (from Scopus database: www.scopus.com, accessed on 15 September 2022).

2. Collagen: Structure and Properties

Collagens represent about 30% of a mammal’s weight [18][38]. Based on the historical order of their discovery, 28 types of collagens—type I through type XXVIII—have been identified and described up to the current day [39]. The oldest collagen identified to date was found in the soft tissue of a fossilized Tyrannosaurus rex bone that dates back 68 million years [40][41].
The molecular organization of collagens is highly variable, notwithstanding their general triple-helical structure and the triplet (Gly-X-Y)n repetition, where X and Y can be any amino acid, although proline and hydroxyproline are the most frequent occupants of these locations (Figure 2) [42][43]. Collagen’s unit is composed of three α-chains, the amino acid composition of which varies among collagen types. Furthermore, function and distribution in tissues play a role in the diversity of collagen, as well as molecular and supramolecular organization, such as occurrence and length of triple helical domains, packing of the triple helices, etc. [27][44].
Figure 2. Exemplary amino acid repetition of the triplet (Gly-X-Y)n characteristic of type I collagen.
The most prevalent and thoroughly studied types of collagens are type I (almost present in all tissues and organs), type II (present in the cartilage, vitreous body, and nucleus pulposus), and type III (present in the skin, blood vessels, lungs, liver, and spleen) [45], which are used in tissue engineering and reconstructive medicine as well as in the pharmaceutical industry as compounds that extend the effects of drugs. Types I, II, and III collagens, especially type I, are also used as plastics in medicine and cosmetology. Type I collagen represents over 70% of the entire collagen family and makes up more than 90% of the collagen in the human body. It is mainly found in connective tissues such as body joints, cartilages, bones, sclerae, ligaments, tendons, intervertebral discs, corneas, adventitia of blood vessels, skin, and most hollow organs including gastrointestinal and genitourinary tracts [24][39][46]. In contrast, types II, III, and IV collagen are frequently seen. Type II collagen, for instance, is a structurally important part of the hyaline cartilage that lines the adult’s articular surfaces in addition to being present in other tissues including the intervertebral disc’s nucleus pulposus and the retina, sclera, and lens of the eye. Skin, lungs, intestinal walls, and blood vessel walls all contain type III collagen.
Type I collagen is composed of three polypeptide chains, two identical α1(I) chains and one α1(I) chain, each of which has roughly 1000 amino acid residues [47]. Hydroxylation of proline residues is a typical post-traditional modification of type I collagen that accounts for about 11–14% of amino acid residues and it is commonly used as a marker to detect and quantify collagen in tissues [48][49]. Whereas proline and hydroxyproline are essential for maintaining the triple helical structure under physiological conditions by forming hydrogen bonds that inhibit uncontrolled rotation, glycine is critical for packing the three helices [50][51].
The idea that the type I collagen molecule is made up of a single extended polypeptide chain with all amide bonds was brought forward by Astbury and Bell in 1940 [51]. In 1951, Pauling and Corey provided the correct structures for the α-helix and β-sheet [52]. In that proposal structure, three polypeptide chains were connected in a helical configuration by hydrogen bonds. These hydrogen bonds necessitated the production of two of the three peptide bonds and involved four of the six main chain heteroatoms inside each amino acid triplet [52]. The collagen triple helix structure was reconstructed in 1954 by Ramachandran and Kartha as a right-handed triple helix of three staggered, left-handed helices with one peptide bond and two hydrogen bonds within each triplet [53]. In 1955, this structure was improved by Rich and Crick, North, and Colleagues thanks to which the triple-helical structure that is still used today was unveiled. This structure has helical symmetry and just one crosslinking hydrogen bond per triplet [54]. Changes in the proposed structure of collagen from the beginning and its modification to the final structure accepted by the scientific community are shown in Figure 3.
Figure 3. Changes in the proposed structure of type I collagen from the beginning and its modification to the final accepted structure. Adapted from [52]. Reproduced from [51] with permission from springer Nature, 1940. Reproduced from [53] with permission from springer Nature, 1954. Reproduced from [54] with permission from Elsevier, 1955.
As is shown in Figure 4, three polypeptide α-chains form the trimeric molecule that represents the type I collagen unit (length ≈ 300 nm, diameter ≈ 1.5 nm). Three parallel, left-handed polyproline-II helices are arranged in a right-handed bundle [55][56]. Multiple collagen units are assembled into fibrils (length ≈ μm, diameter ≈ 100 nm) and then fibers (length ≈ mmm diameter ≈ 10 μm) with dimensions and orientation that are strictly tissue-dependent [28][57].
Figure 4. Type I collagen hierarchical organization.
Thus, type I collagen is a hierarchically organized protein. The primary structure of type I collagen consists of three α helices: two identical α1(I) and one α2(I) helices of approximately 1000 amino acids and a molecular weight of about 130–140 kDa and 110–120 kDa, respectively. The collagen molecule has a triple helical part and two non-helical parts at both ends (called telopeptides), with a molecular weight of 300–400 kDa, a length of 280 nm, and a width of 1.4 nm [58][59]. The secondary structure consists of each of these chains twisted in the form of a left-handed helix with three amino-acid repetitions in each turn. The tertiary structure, the inflexible structure, is created when the chains are then twisted three times around one another. Finally, in the quaternary structure, collagen molecules assemble into fibrils and then fibers. Because of the intermolecular and intramolecular interactions, this collagen organization is very stable [25][60]. Obviously, the collagen structure’s stability is directly dependent on its chemical composition. For instance, the triple helix of collagen grows stronger as the percentage of amino acids is higher, such as proline and hydroxyproline. The pyrrolidine rings are directly responsible for the polypeptide chain’s movement reduction [22][61]. Preservation of collagen’s structural integrity results in an improvement in physical properties, an increase in thermal stability, and a decrease in the denaturation temperature [62][63][64].
Theoretical examination of the mechanical characteristics of collagen at several levels, including the main monomer, individual collagen fibrils, and collagen fibers, is possible by studying collagen’s structured nature. Studying main monomers and fibrils made from type I collagen has likely provided the most direct measurements of the mechanical properties of collagen. Over the recent decades, researchers have used a variety of biophysical and theoretical methods, and recent developments in the Atomic Force Microscopy (AFM) approach have made it possible to perform more accurate evaluations [65]. According to estimates, the fracture strength of individual collagen triple helices is 11 GPa, which is much higher than that of collagen fibrils, which is 0.5 GPa [66]. This difference makes sense because, whereas the breaking of a fibril does not always entail the breakdown of covalent bonds, the breaking of individual collagen triple helices necessitates the unwinding of the triple helix and ultimately breaking of the covalent bonds [67]. In contrast to dehydrated type I collagen fibrils from mammalian sources, which have a Young’s modulus of about 5 GPa according to AFM tests, individual collagen triple helices monomers have a Young’s modulus between 6 and 7 GPa. Because collagen fibrils are anisotropic, another crucial measure of a collagen fibril’s strength is its shear modulus, which determines stiffness [68].
Furthermore, AFM indicated that the shear modulus of dehydrated fibrils of type I collagen from mammalian sources is between 30 and 35 MPa. These fibrils’ shear modulus was drastically decreased by hydration, but was increased by cross-linking. It is important to note that while some cross-linking is beneficial for the mechanical qualities of collagen fibrils, excessive cross-linking causes collagen fibrils to become highly brittle, which is a common sign of aging [69]. Investigation of the mechanical properties of collagen fibrils demonstrated that the length of the individual collagen triple helices monomer has been chosen by nature in a way to maximize the strength of the produced collagen fibril through effective energy dissipation. Simulations indicate that individual collagen triple helices monomers either longer or shorter than the length of a type I collagen triple helix, which is 300 nm, would form collagen fibrils with low mechanical properties [62]. The thermal and structural stability of the collagen triple helix is strongly influenced by the chemical composition of amino acid and its type, which is caused by the type of animal and the living conditions. Indeed, hydroxyproline stabilizes and strengthens the collagen structure [70]. In addition to preserving collagen’s structure and enhancing its mechanical properties, hydroxyproline also plays an important role in its thermal stability. The denaturation temperature and denaturation enthalpy of collagen increases due to the presence of the hydroxyl group in hydroxyproline and the bonding with the pyrrolidine ring. The quantity of hydrogen bonds formed between hydroxyproline and pyrrolidine significantly influences the increment in enthalpy of denaturation. Therefore, the triple helix does have greater thermal stability the more water molecules that there are surrounding it [25][71].
One of the most basic roles of collagen in the body is to provide connective tissues with stability, structure, and resistance to stresses [19][20]. Moreover, collagen has the ability to manage a wide range of nonstructural activities, including cell proliferation, migration, differentiation, and communication [60][72].

3. Fish Collagen

Collagen sources, types, pre-extraction conditions, and process methods are the main parameters that determine extracted product properties, including molecular weight of the peptide chain, amino acid composition, molecular structure, solubility, and functional activity. Although native type I collagen could be extracted from different mammalian sources, the main source of extraction is bovine due to availability and biocompatibility. [73]. There are other alternative sources for extracting type I collagen, among which pig, horse, sheep, and rat can be mentioned [74][75][76][77]. It is possible to obtain mammalian collagen from a wide range of tissues, notably skin, bones, tendons, lung tissue, and connective tissues. Due to some restrictions in terms of health, cultural, social, and religious issues that are implied by traditional sources, research has concentrated on the development of a new source of extraction. Various resources from the sea, including vertebrates as well as invertebrates, have been studied and considered as collagen extraction sources. In particular, several fish species (e.g., Rachycentron canadum, Esoxlucius, Spotless smooth hound, Sciaenops ocellatus, Sardinella fimbriata, Coryphaena hippurus, Alaska pollock, Takifugu flavidus, Pacu, Labeo rohita, Labeo catla, Tuna, Thunnus obesus, Scomber japonicus, Gadus morhua, Prionace glauca, Cichla ocellaris, Cyprinus carpio, Oreochromis niloticus, etc.) aquatic reptiles (such as the soft-shelled turtles), sponges, corals, octopuses, squids, starfish, jellyfish, cuttlefish and sea cucumbers, sea anemones, sea urchins, mussels, and shells were considered.
Skin, scales, bones, skull, swimming bladder, and remaining viscera, are by-products of fish that may be used as sources of collagen (Figure 5). Among all fish by-products, skin traditionally has been reported as the best source of fish collagen extraction [12][78][79][80][81].
Figure 5. By-products of fish as potential sources of collagen extraction.
Fish collagen physicochemical properties were found to be similar to mammalian collagen, but with some advantages such as (1) capability of purification and extraction; (2) aquaculture and accessibility to fishing by-product; (3) lower risk of disease transmission compared to mammalian collagen due to high ontogenetic difference between fish and humans; (4) lack of religious and cultural limitation; (5) slightly different chemical composition; (6) low viscosity; (7) non toxicity; (8) reasonable homeostatic properties; (9) bio-resorbability; (10) more simple extraction method; (11) more adaptable and metabolic compatibility; and (12) minimal inflammatory response (Figure 6) [82][83][84][85]. Although fish collagen has several advantages, it suffers from several disadvantages such as low denaturation temperature, low mechanical properties, and high degradation rate [78]. The major drawback of fish collagen compared to mammalian collagen is the lower denaturation temperature, which limits its medical applications [70]. During denaturation, collagen turns into gelatin, where the hydrogen bonds that support the helical structure are partially or completely destroyed, and it loses its structural role and its conformation-related biological activity [42][43]. The second main drawback of fish-derived collagen is its low mechanical resistance which limits its applications. Many efforts have been made to improve its mechanical properties and degradation profiles, including chemical or enzymatic cross-linking [86][87]. The different advantages and disadvantages of fish collagen are shown in Figure 6.
Figure 6. Advantages and disadvantages of fish collagen.

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