A Review on Fish Skin-Derived Gelatin: Elucidating the Gelatin Peptides—Preparation, Bioactivity, Mechanistic Insights, and Strategies for Stability Improvement
Abstract
:1. Introduction
2. Collagen: The Precursor Molecule to Gelatin
3. Collagen-to-Gelatin Extraction Protocol
4. Rationale behind the Search for Alternatives to Commercial Gelatin
5. Exploring Fish Gelatin as a Feasible Replacement for Mammalian Gelatin
6. Characteristics of Fish Gelatin
6.1. Physical Attributes
- a.
- Melting and gelling temperature: Gelatin creates and maintains stable three-dimensional gels through hydrogen bonds with water [51]. The temperatures at which gelatin melts and gels are directly related to the levels of proline and hydroxyproline present in the initial collagen [11]. These specific amino acids significantly influence the thermal properties of gelatin, determining how it behaves under different temperature conditions. Higher concentrations of proline and hydroxyproline typically result in gelatin with higher melting and gelling points, reflecting the stability and structural integrity derived from the original collagen source. The key difference between mammal and fish gelatins lies in their gelation temperatures. Mammal gelatin has about 30%, warm-water fish gelatin has 22–25%, and cold-water fish gelatin has about 17% proline and hydroxyproline. Cold-water fish gelatin has lower melting and gelling points due to the lower proline and hydroxyproline content, as in the case of cod fish, which reduces the propensity for intermolecular helix formation. Warm-water fish gelatin like that from tilapia and Nile perch behaves like mammalian gelatin due to the comparable proline and hydroxyproline content. For instance, Nile perch (Lates niloticus) skin has the potential to serve as an excellent source of gelatin due to its rich imino acid content, which imparts strong gelling properties. Research by Norziah et al. [52] found cod skin gelatin had lower melting points than bovine and shortfin scad gelatins. The ability of gelatin to melt below body temperature is advantageous for the food industry, which improves the flavor release during consumption and influences the sensory experience in food products. The study by Choi and Regenstein [53] demonstrated that the decreased melting point of cold-water fish gelatin contributes to an improved flavor release, enhanced fruit aroma, and faster melt rate in water-based gel desserts.
- b.
- Gel strength: An important physical property of gelatin is its gel strength, which is affected by several factors, including the molecular weight and complex interactions determined by the amino acid composition and the ratio of α/β-chains within the gelatin matrix [54]. Schrieber and Gareis [55] detailed that gel strength largely depends on the concentration of components with molecular weights around 100,000 g/mol. Moreover, gelatin with a higher content of α-chains generally exhibits greater gel strength. In contrast, an increased presence of peptides with molecular weights either significantly above or below those of α-chains tends to reduce the gel strength [56]. The gelation strength of commercial gelatins is quantified through the bloom values. The higher the bloom value, the stronger the gel. The bloom value can be categorized into three groups: high (220 to 300 bloom), medium (150 to 220 bloom), or low (<150 bloom). Furthermore, gelatin possessing a higher viscosity is deemed more commercially desirable and, as a result, commands a premium price in the market [57]. Yellowfin tuna skin is considered a suitable raw material for producing gelatin with high gel strength [58]. Table 2 illustrates the diverse functional attributes of gelatin-based food products as determined by their gel strength.
- c.
- Viscosity: Viscosity is a crucial functional characteristic for process control. A gelatin solution’s ability to gel depends on the temperature and the viscosity of the gelatin in the water [60]. The species of fish, habitat, origin, and amino acid content are a few of the variables that might affect whether fish gelatin has gelling or non-gelling qualities [3]. The viscosity of gelatin derived from cold-water fish is very high, which may not be appropriate for numerous applications [61]. In contrast to the gel strength, the viscosity demonstrates a weaker correlation with textural characteristics. The molecular weight distribution predominantly influences the viscosity. Gelatin samples characterized by substantial molecular weight fractions yield elevated viscosity; however, this does not inevitably translate to equally high gel strength [61].
- d.
- pH: The pH is an important physical parameter that influences the quality of gelatin. The production process influences the pH of gelatin, and this pH range determines the types of gelatins:
- e.
- Thermoreversibility: Gelatin falls into the group of physical gels involving Van der Waals forces and hydrogen bonds; the interactions or bonds between the constituent chains are primarily of a physical nature, with an energy of approximately 2 Kcal/mol. The bonding energy within gelatin is relatively modest, which enables gelatin to form thermoreversible gels. When compared to other gel-forming substances like proteins and polysaccharides, gelatin has greater thermoreversibility due to the non-random presence of imino acids (such as proline or hydroxyproline) [64,65,66]. This implies that it achieves softness, transforms into a liquid state, and also reverses to a gel-like consistency upon cooling.
- f.
- Texture: Gelatin is vitreous in gel form, with a taste and smell that are nearly imperceptible. Its dried appearance ranges from pale yellow to white. It is offered in a variety of physical configurations, including sheets, fine powders, and coarse granules [1].
- g.
- Stability: Gelatin remains stable for at least five years when stored [67] properly in sealed containers under typical storage conditions to prevent moisture changes. The bloom value can vary slightly due to modest changes in the moisture levels. These bloom variations, nevertheless, may be precisely computed from the moisture content and do not signify a change in the underlying intensity or quality of the bloom [68].
6.2. Chemical Attributes
- Amino acid composition: The amino acid content significantly affects the melting and setting temperatures of gelatin derived from various sources. Proline and hydroxyproline exert notable impacts on both the gel strength and the temperature at which gelling occurs [67]. Furthermore, the levels of aspartic acid, glutamic acid, arginine, histidine, lysine, and hydroxylysine are crucial for the formation of cross-links and electrostatic interactions [77].
- Peptide size and quality: Collagen tissues are treated with acid/alkali, heat, and water to disrupt the fibrils, yielding gelatin’s irreversibly. Gelatin comprises collagen fractions above 30 kDa; lower-molecular-weight forms are gelatin hydrolysates, aiding in gel formation. Heat at ~40 °C frees the α-chains via bond breakage in new collagen while the mature bonds of collagen endure. Higher heat breaks the covalent bonds, yielding smaller α-chains and varied weights. Diverse collagen amino acids cause random bond breaks, causing variability. Raw materials add impurities like proteins, lipids, and minerals; the water in commercial gelatin (9–14%) varies based on the production and storage.
7. Versatile Uses and Applications of Gelatin
7.1. Food Industry
7.2. Pharmaceutical and Medical Industry
7.3. Nutritional and Health Benefits
8. Challenges Associated with Fish-Derived Gelatin
9. Enhancing Fish Gelatin: Solutions for Its Limitations
- Developing composite gelation systems involves blending fish gelatin with high-bloom gelatins, as substantiated by the research conducted by P. Gilsenan [106], P. M. Gilsenan and Ross-Murphy [107] and Zhou et al. [108]. Alternatively, these systems can incorporate appropriate plant hydrocolloids, as exemplified by Haug et al. [109] and Pranoto et al. [110]. These methods promise to augment the gel strength, improve the gelling properties, and elevate the melting temperature.
- Modifying the properties of gelatin through the introduction of solutes, such as various types of salts, as deliberated by Elysée-Collen and Lencki [111].
10. Bioactive Peptides Derived from Gelatin: Their Potential Efficacies
11. Production Methods for Fish Gelatin Hydrolysates and Peptides
- a.
- Ultrasonication
- b.
- Microwave pretreatment
- c.
- Hydrothermal pretreatment
- d.
- High pressure (HP)
- e.
- Autolysis
- f.
- Thermal Hydrolysis
- g.
- Bacterial Fermentation
- h.
- Enzymatic hydrolysis
- i.
- Subcritical water hydrolysis
12. Fish Gelatin Hydrolysates and Its Significance for Food and Biomedical Applications
13. Bio-Functionalities of Peptides Derived from Distinct Fish Skin Gelatin Sources
- a.
- Antioxidant
- b.
- Antihypertensive
- c.
- Antimicrobial
- d.
- Antidiabetic
14. Stability Improvement Strategies for Peptides
15. Conclusions
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Conflicts of Interest
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Fish | Extraction Method | Yield (%) | Reference |
---|---|---|---|
Black tilapia (Oreochromis mossambicus) Red tilapia (Oreochromis nilotica) | Pretreatment with NaOH (2%, w/v), H2SO4 (2%, w/v) and citric acid (1%, w/v); hot water 45 °C for 12 h | 5.39 7.81 | [36] |
Nile perch (Lates niloticus) | Pretreated with H2SO4 (0.01 M); hot water 50, 60 and 70 °C for 5 h | 1.2–4.9 | [37] |
Shortfin scad (Decapterus macrosomia Sin croaker (Johnius dussumieri) | Pretreatment with NaOH (0.2%, w/v), H2SO4 (0.2%, w/v) and citric acid (1%, w/v); hot water 40–50 °C for 12 h | 7.25 14.3 | [38] |
Grass carp (Catenopharyngodon Idella) | HCl (1.19%, 24 h) pretreatment followed by hot water extraction at 52.61 °C for 5.12 h | 19.83 | [39] |
Farmed giant catfish (Pangasianodon gigas) | NaOH (0.2 M)-treated skin soaked in acetic acid (0.05 M) and stirred for 3 h at 25 °C | 20.1 | [40] |
Hoki (Macruronus novaezelandiae) | 0.75 M NaCl pretreatment for 9 min and hot water extraction at 49.3 °C for 60 min | 17.6 | [41] |
Nile tilapia (Oreochromis niloticus) | Alkali-treated (NaOH 3.2% w/v, 2.3 h) skin soaked in HCl (0.7%, 84 min) followed by hot water extraction 60 °C for 3 h | 19.3 | [42] |
Rainbow trout (Oncorhynchus mykiss) | Pretreated with NaOH (0.19 N) and acetic acid (0.121 N) for 3 h, followed by hot water extraction of 50 °C for 16 h | 9.36 | [43] |
Pink perch (Nemipterus japonicas) Tiger-toothed croaker (Otoliths ruber) | Pretreated with NaOH (0.2%, w/v), H2SO4 (0.2%, w/v), and citric acid (1%, w/v) for 40 min, followed by hot water extraction at 45 °C for 12 h | 5.57 7.56 | [44] |
Splendid squid (Loligo formosana) | Skin soaked in NaOH (0.05 M, 6 h) and phosphoric acid (0.05 M, 24 h) followed by hot water extraction at different temperatures (50, 60, 70, and 80 °C) for 12 h. | 8.8–45.3 | [45] |
Cuttlefish (Sepia officinalis) | Alkali-pretreated skin (NaOH, 0.05 M) subjected to 5, 10 and 15 U pepsin/g for 18 h at 4 °C, pH 2 | 6.59–9.22 | [46] |
Dog shark (Scoliodon sorrakowah) Rohu (Labeo rohita) Skipjack tuna (Katsuwonus pelamis) | Pretreated with NaOH (0.1 M) and acetic acid (0.2 M) followed by hot water at 45 °C for 12 h | 19.7 11.3 17.2 | [47] |
Farmed amur sturgeon (Acipenser schrenckii) | Alkali (NaOH, 0.1 M for 6 h, 4 °C) and acid (acetic acid, 0.05–0.2 M, 3–6 h)-treated skin followed by extraction at 50 °C for 1 h | 5.04–24.11 | [48] |
Octopus (Octopus vulgaris) | Alkali (0.05 M NaOH, 1 h at 4 °C)-treated skin soaked in glycine-HCl buffer (10 h at 4 °C) added pepsin (0–15 U) incubated at 40 °C for 4 h. | 3.21–7.78 | [49] |
Kumakuma (Brachyplatystoma flamentosum) | Pretreatment with NaCl (0.6 M) followed by NaOH (0.3 M), followed by acetic acid treatment (0.02 M) for min | 19.7 | [50] |
Application | Bloom Strength (g) | Concentration and Function |
---|---|---|
Gelatin desserts and gummy bears | 175–275 | 7–9% as gel formation [59]. |
Sausages, broths, meat products, and canned meats | 175–275 | 1–5% as an emulsion stabilizer and binding agent |
Dairy products | 150–250 | 0.2–1.0% as syneresis stabilizer [59]. |
Frozen foods | 200–250 | 0.1–0.5% reducing water loss agent [59]. |
Beverage industry | 100–20 | 0.002–0.015% as clarifying agent [59]. |
Skin Source | Gel Strength (Bloom Grams) | Gelling Temp (°C) | Melting Temp (°C) | Viscosity (cP) | Water Holding (%) | Fat Binding (%) | Emulsion | Foaming | Reference | ||
---|---|---|---|---|---|---|---|---|---|---|---|
EAI (m2/g) | ESI (min) | FE (%) | FS (%) | ||||||||
Cold-water fish gelatin | |||||||||||
Rohu | 124 | 13.8 | 18.2 | 2.50 | 163 | 360 | NA | NA | 17.4 | 10.5 | [47] |
Gray triggerfish | 168.3 | NA | NA | NA | ~190 | ~340% | 21.44 | 42.77 | 123.04 | 117.22 | [69] |
Chum salmon | 87.7 | NA | NA | NA | NA | NA | ~24 | ~100 | ~119 | ~103 | [70] |
Indian carp | 367.66 | NA | NA | NA | NA | NA | 0.87 * | 90 | 61.8 | [71] | |
Rohu | 258.0 | NA | NA | NA | NA | NA | 0.552 * | ND | 92 | 72.9 | |
White carp | 343.0 | NA | NA | NA | NA | NA | 0.669 | NA | 80 | 77.1 | |
Warm-water fish gelatin | |||||||||||
Yellowfin tuna | 426 | 18.7 | 24.3 | NA | NA | NA | NA | NA | NA | NA | [58] |
Skipjack tuna | 177 | 18.7 | 24.2 | 4.37 | 452 | 452 | NA | NA | 19.2 | 14.4 | [47] |
Dog shark | 206 | 20.8 | 25.8 | 5.6 | 256 | 347 | NA | NA | 21.5 | 17.6 | |
Unicorn leatherjacket | 149.77 | NA | NA | NA | NA | NA | 39.17 | 8.58 | 116.35 | 111.11 | [72] |
Snakehead | 311.18 | NA | NA | 3.40 | NA | NA | NA | NA | NA | NA | [73] |
Catfish | 278.72 | NA | NA | 5.24 | NA | NA | NA | NA | NA | NA | |
Pangasius catfish | 324.53 | NA | NA | 3.82 | NA | NA | NA | NA | NA | NA | |
Red tilapia | 487.61 | NA | NA | 1.73 | NA | NA | NA | NA | NA | NA | |
Porcine gelatin | |||||||||||
Porcine | 295 | 25.6 | 36.5 | NA | NA | NA | NA | NA | NA | NA | [58] |
Bovine gelatin | |||||||||||
Hoki | 197 | NA | 16.6 | 10.8 | NA | NA | NA | NA | NA | NA | [41] |
Shortfin scad | 177 | 9.9 | 23.8 | NA | NA | NA | NA | NA | NA | NA | [38] |
Bovine | 216 | 23.8 | 33.8 | NA | NA | NA | NA | NA | NA | NA | [58] |
Poultry gelatin | |||||||||||
Chicken | 270.5 | NA | 39.83 | NA | NA | NA | NA | NA | NA | NA | [74] |
Duck | 210–260 | NA | 31.2–33.8 | 56.9–77.8 | NA | NA | NA | NA | NA | NA | [75] |
Chicken leg | 75–85 | NA | NA | 7 to 8.9 | NA | NA | NA | NA | NA | NA | [76] |
Modification | Fish Skin Source | Tailored Properties | Reference |
---|---|---|---|
Sucrose, glucose and fructose addition | Tilapia | Characteristics of the structure, the functions, and the capability of stabilizing the emulsion | [24] |
Octenyl succinic anhydride modification | Cold-water fish | Structural, functional, and emulsion stability | [112] |
Sodium alginate addition | Cod, pollock, and haddock | Foam and emulsion stabilization | [113] |
Spray drying with citric acid, adding pretreatment | Seabass (L. calcarifer) | Physico-chemical properties and fishy odor | [114] |
NaH2PO4, MgCl2, CaCl2, and glycerol addition | Yellowfin tuna | Physicochemical properties | [115] |
Basil and citronella essential oils addition | Alaska pollock | Structural, morphological, and thermal properties | [116] |
Proteins (chitosan) addition | Baltic cod | Physico-chemical properties | [117] |
Chitosan and calcium acetate addition | Catfish (Pungaseous fungaseous) | Physico-functional and mechanical properties | [118] |
Coenhancers (MgSO4, sucrose, and transglutaminase) addition | Tiger-toothed croaker | Gel strength and melting point | [119] |
Adjust extraction conditions (alkali and acid treatment, water extraction) | Silver carp | Sensory and instrumental characteristics | [120] |
Addition of glycerol and sorbitol | Sole (Solea spp.) | Sensory characteristics | [121] |
Source of Skin Gelatin | Enzyme | Mechanism | Peptide Sequence | Reference |
---|---|---|---|---|
(a) Antioxidant activity | ||||
Silver carp | Alcalase, papain and flavoenzyme | Flavorsome hydrolysate has the highest DPPH-scavenging activity | NA | [151] |
Catfish | Protamex |
| NA | [152] |
Shark | Alcalase |
| NA | [153] |
Carp | Protamex |
| Ala-Tyr dipeptide | [23] |
Sole fish | Alcalase |
| NA | [154] |
Oneknife unicornfish | Crude protease from Bacillus sp. |
| NA | [155] |
Nile tilapia | Ginger protease |
| Gly-Pro-Y-type X-Hyp-Gly-type | [156] |
Giant catfish | Viscera peptidase of gait catfish |
| NA | [157] |
Giant catfish | Visceral alkaline proteases from giant catfish, Izyme AL and trypsin |
| NA | [158] |
Amur sturgeon | Alcalase or flavoenzyme |
| NA | [159] |
Unicorn leatherjacket | Protease from Bacillus amyloliquefaciens and Alcalase |
| NA | [160] |
Tilapia | Papaya crude extract |
| NA | [161] |
Atlantic mackerel | Pepsin |
| NA | [162] |
Amur sturgeon | Alcalase and flavoenzyme |
| Pro–Ala–Gly–Tyr (PAGT) | [163] |
Thornback ray | - |
| AVGAT | [164] |
Horse mackerel | - |
| NHRYDR | [165] |
(b) Antihypertensive | ||||
Skate | Subtilisin and actinidin |
| 1. GRPGNRGE (IC50 0.74 mg/mL) 2. AKDYEVDAT (IC50 0.52 mg/mL) | [166] |
Oneknife unicornfish | Crude protease from Bacillus sp. |
| NA | [155] |
Nile tilapia | Alcalase |
| GIV, GAP*GF, GFA*GPA, SGNIGFP*GPK, GIPGPIGPP*GRP | [167] |
Giant catfish | Viscera peptidase of gait catfish |
| NA | [157] |
Atlantic mackerel | Pepsin |
| NA | [162] |
Pacific cod | Pepsin |
| GASSGMPG (6.9 µM) LAYA (1.45 µM) | [168] |
Skate | Alcalase/protease |
| MVGSAPGVL LGPLGHQ | [169] |
Salmon | Trypsin |
| GLPLNLP | [170] |
Alaska pollock | - |
| GPL | [171] |
(c) Antimicrobial activity | ||||
Skate | Subtilisin and actinidin |
| 1. GRPGNRGE 2. AKDYEVDAT | [166] |
(d) Antidiabetic activity | ||||
Barbel | Commercial proteases |
| ND | [172] |
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© 2024 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
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Joy, J.M.; Padmaprakashan, A.; Pradeep, A.; Paul, P.T.; Mannuthy, R.J.; Mathew, S. A Review on Fish Skin-Derived Gelatin: Elucidating the Gelatin Peptides—Preparation, Bioactivity, Mechanistic Insights, and Strategies for Stability Improvement. Foods 2024, 13, 2793. https://doi.org/10.3390/foods13172793
Joy JM, Padmaprakashan A, Pradeep A, Paul PT, Mannuthy RJ, Mathew S. A Review on Fish Skin-Derived Gelatin: Elucidating the Gelatin Peptides—Preparation, Bioactivity, Mechanistic Insights, and Strategies for Stability Improvement. Foods. 2024; 13(17):2793. https://doi.org/10.3390/foods13172793
Chicago/Turabian StyleJoy, Jean Mary, Amruth Padmaprakashan, Akshay Pradeep, Preethy Treesa Paul, Rosemol Jacob Mannuthy, and Suseela Mathew. 2024. "A Review on Fish Skin-Derived Gelatin: Elucidating the Gelatin Peptides—Preparation, Bioactivity, Mechanistic Insights, and Strategies for Stability Improvement" Foods 13, no. 17: 2793. https://doi.org/10.3390/foods13172793