Cryoprotective effect of gelatin hydrolysate from shark skin on denaturation of frozen surimi compared with that from bovine skin

Limpisophon, Kanokrat; Iguchi, Hitomi; Tanaka, Munehiko; Suzuki, Toru; Okazaki, Emiko; Saito, Toshiki; Osako, Kazufumi

doi:10.1007/s12562-014-0844-5

Cited by 32 publications

(11 citation statements)

References 30 publications

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“…In addition, shark skin is very rich in collagen type I, while shark cartilage is rich in collagen type II. Collagen from shark tissues have been used to prepare a gel matrix for in vivo culturing of fibroblasts as a food supplement to create functional foods, and to also increase the cryoprotection of foods [115]. Moreover, the antioxidant capacity of type II collagens (i.e., type II ASC, CIIA and PSC, CIIP) was also assessed by 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging capacity, showing that the reducing power of CIIP was greater than that of CIIA [116].…”

Section: Fish Wastementioning

confidence: 99%

Marine Collagen from Alternative and Sustainable Sources: Extraction, Processing and Applications

et al. 2020

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Due to its unique properties, collagen is used in the growing fields of pharmaceutical and biomedical devices, as well as in the fields of nutraceuticals, cosmeceuticals, food and beverages. Collagen also represents a valid resource for bioplastics and biomaterials, to be used in the emerging health sectors. Recently, marine organisms have been considered as promising sources of collagen, because they do not harbor transmissible disease. In particular, fish biomass as well as by-catch organisms, such as undersized fish, jellyfish, sharks, starfish, and sponges, possess a very high collagen content. The use of discarded and underused biomass could contribute to the development of a sustainable process for collagen extraction, with a significantly reduced environmental impact. This addresses the European zero-waste strategy, which supports all three generally accepted goals of sustainability: sustainable economic well-being, environmental protection, and social well-being. A zero-waste strategy would use far fewer new raw materials and send no waste materials to landfills. In this review, we present an overview of the studies carried out on collagen obtained from by-catch organisms and fish wastes. Additionally, we discuss novel technologies based on thermoplastic processes that could be applied, likewise, as marine collagen treatment.2 of 23 protective colloid functions and film-forming capacity. Also, collagen is a good surface-active agent, with its ability to penetrate lipid-free interfaces [2].Collagen can be utilized in a variety of applications because of its biocompatibility and excellent degradability [3,4]. Furthermore, it is known that collagen is a molecule with weak immunogenicity, which decreases the possibilities of rejection when it is ingested or injected into a different body. Although this molecule has already low antigenicity, this property can be enhanced by modifying it to suppress any immune response [5,6]. Additionally, collagen peptides and gelatin (denatured collagen) have been widely utilized in different fields such as food, medicine, cosmetics, leather and film industries, diagnostic imaging, and therapeutic delivery [7].For many years, most available collagen was extracted from discards from the bovine and porcine processing industries, but during the last few decades the use of collagen from these sources has been limited. The use of porcine and bovine-derived products is occasionally prevented by dietary regimes, due to specific needs or personal choices. It is forbidden by religious constraints, to Muslims, Hindus and Jews who make up 38.4% of the global population [8]. Moreover, the use of bovine-derived products became a concern for a wider section of the population during the bovine spongiform encephalopathy (BSE), transmissible spongiform encephalopathy (TSE) and foot-and-mouth disease (FMD) crises that occurred over the last few decades in all areas of the world, mostly in the United Kingdom and Asia. Bovine-derived products might be a vehicle of transmission of these diseases ...

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Section: Fish Wastementioning

confidence: 99%

Marine Collagen from Alternative and Sustainable Sources: Extraction, Processing and Applications

et al. 2020

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“…Of the 389 patients who were orally administrated 10 g of either HC or a placebo for 6 months in a clinical trial, only 12 dropped out because of side effects and, among those, 9 had been orally treated with the placebo . Second, HC displays a wide range of bioactivities such as antitumor, immunomodulatory, antioxidative, , antihypertensive, − and cryoprotective . Among the various research topics, the role of gelatin in bone health and disease may be one of the most interesting.…”

Section: Introductionmentioning

confidence: 99%

Cell Proliferation Stimulation Ability and Osteogenic Activity of Low Molecular Weight Peptides Derived from Bovine Gelatin Hydrolysates

Wang

Zhang

et al. 2020

J. Agric. Food Chem.

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It has been recognized that collagen peptides of MW 878 Da (CP1) promote osteoblast proliferation and mineralization. The objective of this study is to identify the peptides responsible for proliferation of osteoblast growth, enhancement of ALP (alkaline phosphatase) activity in osteoblasts and promotion of osteoblast mineralization. To this end, the CP1 were fractioned by a series of chromatography procedures, and 51 peptides from the fraction possessing the most powerful cell proliferation ability were identified by LC–MS–MS. The peptides, GPAGPSGPAGK and GPPGSPGPR, were validated on a simultaneous basis as possessing enhanced bioactivity-inducing properties. In particular, the ALP activity of the cells treated with these two peptides was almost twice that of the control cells. Hydrogen bonds were formed, and the hydrophobic interactions with the EGFR (epidermal growth factor receptor) might be responsible for the osteoblast proliferation activity. On this basis, the two peptides might be potential lead compounds against osteoporosis and osteoarthritis.

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“…The hydrolysates derived from the unicorn leather jacket skin comprised a higher concentration of hydrophilic amino acids, which may enhance the antioxidative abilities and enhance the functional properties of surimi gel by limiting the movement of water molecules in proteins, thereby reducing the crystallization process [66]. Gelatin tripeptide avoided the denaturation of myosin and ultimately reduced water loss from MPs [67]. Krill protein hydrolysates were documented with strong antioxidative abilities, which increased the functional properties of surimi gel by reducing free radicals, the formation of ice crystals and inhibiting decline in Ca 2+ ATPase activity during frozen storage.…”

Section: Protein Hydrolysate-based Gelmentioning

confidence: 99%

Role of Food Hydrocolloids as Antioxidants along with Modern Processing Techniques on the Surimi Protein Gel Textural Properties, Developments, Limitation and Future Perspectives

et al. 2022

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Texture is an important parameter in determining the quality characteristics and consumer acceptability of seafood and fish protein-based products. The addition of food-based additives as antioxidants (monosaccharides, oilgosaccharides, polysaccharides and protein hydrolysates) in surimi and other seafood products has become a promising trend at an industrial scale. Improvement in gelling, textural and structural attributes of surimi gel could be attained by inhibiting the oxidative changes, protein denaturation and aggregation with these additives along with new emerging processing techniques. Moreover, the intermolecular crosslinking of surimi gel can be improved with the addition of different food hydrocolloid-based antioxidants in combination with modern processing techniques. The high-pressure processing (HPP) technique with polysaccharides can develop surimi gel with better physicochemical, antioxidative, textural attributes and increase the gel matrix than conventional processing methods. The increase in protein oxidation, denaturation, decline in water holding capacity, gel strength and viscoelastic properties of surimi gel can be substantially improved by microwave (MW) processing. The MW, ultrasonication and ultraviolet (UV) treatments can significantly increase the textural properties (hardness, gumminess and cohesiveness) and improve the antioxidative properties of surimi gel produced by different additives. This study will review potential opportunities and primary areas of future exploration for high-quality surimi gel products. Moreover, it also focuses on the influence of different antioxidants as additives and some new production strategies, such as HPP, ultrasonication, UV and MW and ohmic processing. The effects of additives in combination with different modern processing technologies on surimi gel texture are also compared.

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Cryoprotective effect of gelatin hydrolysate from shark skin on denaturation of frozen surimi compared with that from bovine skin

Cited by 32 publications

References 30 publications

Marine Collagen from Alternative and Sustainable Sources: Extraction, Processing and Applications

Marine Collagen from Alternative and Sustainable Sources: Extraction, Processing and Applications

Cell Proliferation Stimulation Ability and Osteogenic Activity of Low Molecular Weight Peptides Derived from Bovine Gelatin Hydrolysates

Role of Food Hydrocolloids as Antioxidants along with Modern Processing Techniques on the Surimi Protein Gel Textural Properties, Developments, Limitation and Future Perspectives

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