Characterization of Collagen Derived From Tropical Freshwater Carp Fish Scale Wastes and Its Amino Acid Sequence

Chinh, Nguyễn Thúy; Manh, Vu Quoc; Trung, Vũ Quốc; Лам, Тран Дай; Huynh, Mai Duc; Tung, Nguyen Quang; Trinh, Nguyen Duy; Hoàng, Thái

doi:10.1177/1934578x19866288

Cited by 61 publications

(51 citation statements)

References 34 publications

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“…Fish skin typically contains type I collagen with a high degree of purity (around 70%) depending on the species age and season [ 37 ]. Collagen from fish skin demonstrates an excellent capacity to retain water (about 6% of its weight in exposure to 63% humidity for 24 h) and exhibits no irritant potential, thus being suitable for dermal applications [ 38 ].…”

Section: Collagen Formation Stability and Molecular Structurementioning

confidence: 99%

“…Collagen from fish skin demonstrates an excellent capacity to retain water (about 6% of its weight in exposure to 63% humidity for 24 h) and exhibits no irritant potential, thus being suitable for dermal applications [ 38 ]. A study by Blanco et al [ 37 ] on collagen from the skin of two species of teleost and two species of Chondrichthyes showed a collagen denaturation temperature in the range of 23 to 33 °C while collagen isolated from codfish skin denatured around 16 °C, which possibly could be due to the habitat of the species [ 39 ]. However, collagen from the skin of tilapia, catfish, pomfret, and mackerel requires a low extraction temperature (slightly lower than 13.26 °C), long extraction time (74 h), and generates yields of 2.27% (based on dry mass content) [ 40 ].…”

Section: Collagen Formation Stability and Molecular Structurementioning

confidence: 99%

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Fish Collagen: Extraction, Characterization, and Applications for Biomaterials Engineering

et al. 2020

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The utilization of marine-based collagen is growing fast due to its unique properties in comparison with mammalian-based collagen such as no risk of transmitting diseases, a lack of religious constraints, a cost-effective process, low molecular weight, biocompatibility, and its easy absorption by the human body. This article presents an overview of the recent studies from 2014 to 2020 conducted on collagen extraction from marine-based materials, in particular fish by-products. The fish collagen structure, extraction methods, characterization, and biomedical applications are presented. More specifically, acetic acid and deep eutectic solvent (DES) extraction methods for marine collagen isolation are described and compared. In addition, the effect of the extraction parameters (temperature, acid concentration, extraction time, solid-to-liquid ratio) on the yield of collagen is investigated. Moreover, biomaterials engineering and therapeutic applications of marine collagen have been summarized.

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Section: Collagen Formation Stability and Molecular Structurementioning

confidence: 99%

Section: Collagen Formation Stability and Molecular Structurementioning

confidence: 99%

Fish Collagen: Extraction, Characterization, and Applications for Biomaterials Engineering

et al. 2020

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“…Due to its high-water absorption capacity, collagen is a good candidate for texturizing, thickening and gel formation. Moreover, it has interesting properties related to surface behavior, which involves emulsion, foam formation, stabilization, adhesion and cohesion, Fish waste is very abundant worldwide and several studies, projects, and local and international authorities have focused on how to use this valuable waste [10,12,[34][35][36][37][38][39][40]. Its utilization has recently increased in order to enhance the economic value of by-catch and fish by-products for biotechnological applications, and also because of the urgent need to reduce the amount of waste for contemporary societies.…”

Section: Introductionmentioning

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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“…The different molecular weight of α chain in collagen might be due to the different class of Sipuncula Sedgwick . The patterns of the two α chains and one β dimer were similar to most collagens from fishes [ 27 , 28 ]. Type-I collagen could be applied in pharmaceutical, food and biomedical industries [ 29 ].…”

Section: Resultsmentioning

confidence: 65%

Collagen Peptides Derived from Sipunculus nudus Accelerate Wound Healing

et al. 2021

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Marine collagen peptides have high potential in promoting skin wound healing. This study aimed to investigate wound healing activity of collagen peptides derived from Sipunculus nudus (SNCP). The effects of SNCP on promoting healing were studied through a whole cortex wound model in mice. Results showed that SNCP consisted of peptides with a molecular weight less than 5 kDa accounted for 81.95%, rich in Gly and Arg. SNCP possessed outstanding capacity to induce human umbilical vein endothelial cells (HUVEC), human immortalized keratinocytes (HaCaT) and human skin fibroblasts (HSF) cells proliferation and migration in vitro. In vivo, SNCP could markedly improve the healing rate and shorten the scab removal time, possessing a scar-free healing effect. Compared with the negative control group, the expression level of tumor necrosis factor-α, interleukin-1β and transforming growth factor-β1 (TGF-β1) in the SNCP group was significantly down-regulated at 7 days post-wounding (p < 0.01). Moreover, the mRNA level of mothers against decapentaplegic homolog 7 (Smad7) in SNCP group was up-regulated (p < 0.01); in contrast, type II TGF-β receptors, collagen I and α-smooth muscle actin were significantly down-regulated at 28 days (p < 0.01). These results indicate that SNCP possessed excellent activity of accelerating wound healing and inhibiting scar formation, and its mechanism was closely related to reducing inflammation, improving collagen deposition and recombination and blockade of the TGF-β/Smads signal pathway. Therefore, SNCP may have promising clinical applications in skin wound repair and scar inhibition.

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Characterization of Collagen Derived From Tropical Freshwater Carp Fish Scale Wastes and Its Amino Acid Sequence

Cited by 61 publications

References 34 publications

Fish Collagen: Extraction, Characterization, and Applications for Biomaterials Engineering

Fish Collagen: Extraction, Characterization, and Applications for Biomaterials Engineering

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

Collagen Peptides Derived from Sipunculus nudus Accelerate Wound Healing

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