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Barracuda fish (Sphyraena sp.) bone and fins could be a source of aquatic collagen. Marine collagen has recently gained popularity due to its lack of infectious infections. This collagen extraction yields 1.99 % acetic acid-soluble collagen (AAC), 2.36 % lactic acid-soluble collagen (LAC), and 3.26 % citric acid-soluble collagen (CAC). AAC has a high L* value compared to LAC and CAC, indicating great brightness in color. For hydroxyproline content, the amount of collagen was 82.70, 81.31, and 80.93 for AAC, LAC, and CAC. AAC and LAC have maximum collagen solubility at pH 3, and CAC at pH 5. The effects of collagen solubility on NaCl concentrations drop substantially at 30 g/L for all collagen samples. All extracted collagen structures are type I collagen consisting of two chains (a1 and a2) based on SDS-PAGE analysis and possessing a complete triple helical structure based on UV absorption (229.5 nm) and Fourier Transformation Infrared Spectrometry (ATR-FTIR) showed all collagen samples had amide A, B, amide I, II, and III peaks. All collagens demonstrate strong heat resistance and structural stability as Tmax is above 30°C. LAC demonstrated higher absorption of water (0.50 0.01±mL/mg) and oil (0.70±0.07 mL/mg) than AAC and CAC. At pH 7, CAC and AAC reduced foam and foam case capacity. In emulsion properties, only AAC does not demonstrate important emulsion stability. AAC showed superior collagen than LAC and CAC based on physicochemical and functional qualities. Therefore, all collagen samples can be employed as replacements for terrestrial collagen in diverse applications. [ABSTRACT FROM AUTHOR]

The by-product of needlefish (Tylosurus acus melanotus) waste possesses important characteristics that could be used in food applications. Fish by-product collagen may be used in place of mammalian collagen due to ethical and religious considerations over environmental degradation. Different forms of acid-soluble collagen (ASC) were successfully extracted from needlefish skin. Based on dry weight, the collagen extracted using acetic acid (AAC), lactic acid (LAC), and citric acid (CAC) treatments was 3.13% with a significantly difference (p < 0.05), followed by 0.56% and 1.03%, respectively. Based on proximate analysis, the needlefish skin composition was found to be significantly different (p < 0.05) between compositions, with the highest moisture content at 61.65%, followed by protein (27.39%), fat (8.59%), and ash (2.16%). According to the SDS-PAGE results, all extracted collagen were identified as a type 1 collagen. Additionally, ATR-FTIR revealed that all collagens had amide A, B, amide I, II, and III peaks. AAC significantly outperforms LAC and CAC in terms of yield following physicochemical characterisation, including pH determination, colour (L* value), and hydroxyproline content. All collagens demonstrated strong heat resistance and structural stability with Tmax above 38 °C. Collagen was most soluble at pH 5 for AAC, pH 3 for LAC, and pH 7 for CAC. The effect of collagen solubility on NaCl concentration was discovered to be significantly reduced to 50 g/L for all collagen samples. All collagens can be used as alternatives to terrestrial collagen in a diverse range of applications. [ABSTRACT FROM AUTHOR]

Fish processing waste is a prospective source of collagen and a cost-effective environmental pollutant. The skin of the purple-spotted bigeye snapper (Priacanthus tayenus) was extracted utilising various acid soluble collagens (ASC) including acetic acid (AAC), lactic acid (LAC), citric acid (CAC) and pepsin soluble collagens (PSC). In this study, PSC (6.65%) had the highest collagen yield, followed by AAC (5.79%), CAC (4.15%), and LAC (3.19%). The maximum temperatures (Tmax) denaturation of AAC, LAC, CAC, and PSC were 31.4, 31.7, 31.5, and 33.2 °C, respectively. UV-VIS absorption spectra showed all extracted collagens had a range of absorbance at 230 nm, due to the presence of glycine, proline, hydroxyproline, and triple-helical collagen. Additionally, they exhibited amide A, B, amide I, II, and III peaks. SDS–PAGE identified all extracted collagens as type I. The PSC had a significantly higher (p < 0.05) hydroxyproline content than acidic extraction 66.3 ± 1.03 (mg/g sample). Furthermore, all samples were extremely soluble in acetic conditions at pH 5, and all collagen was soluble in NaCl up to 3% (w/v). Therefore, PSC was the best treatment since it did not impact collagen triple helical and acetic acid yielded the most collagen in ASC extraction. Overall, the analysis revealed that fish skin waste might be used as an alternate source of collagen in diverse applications, particularly in food applications. [ABSTRACT FROM AUTHOR]

Collagen is a structural protein naturally found in mammals. Vertebrates and other connective tissues comprise about 30% of an animal's overall protein. Collagen is used in a variety of applications including cosmetics, biomedical, biomaterials, food, and pharmaceuticals. The use of marine-based collagen as a substitute source is rapidly increasing due to its unique properties, which include the absence of religious restrictions, a low molecular weight, no risk of disease transmission, biocompatibility, and ease of absorption by the body system. This review discusses recent research on collagen extraction from marine-based raw material, specifically fish by-products. Furthermore, pretreatment on various sources of fish materials, followed by extraction methods, was described. The extraction procedures for acid soluble collagen (ASC) and pepsin soluble collagen (PSC) for fish collagen isolation are specifically discussed and compared. As a result, the efficacy of collagen yield was also demonstrated. The recent trend of extracting fish collagen from marine biomaterials has been summarized, with the potential to be exploited as a wound healing agent in pharmaceutical applications. Furthermore, background information on collagen and characterization techniques primarily related to the composition, properties, and structure of fish collagen are discussed. [ABSTRACT FROM AUTHOR]