Fish collagen is derived from processing residues of marine and freshwater fish (such as fish skin, scales, and bones), primarily composed of amino acids including glycine, proline, and hydroxyproline. It functions include maintaining tissue integrity and promoting cell proliferation and repair. Extraction methods primarily include acid, alkali, enzymatic, and physical approaches, while purification techniques involve gel filtration chromatography, ultrafiltration, and precipitation. Furthermore, thermal instability, insufficient mechanical strength, immunological concerns, and biocompatibility limitations restrict its application across various fields. This review summarizes the composition, extraction, purification, and existing challenges of fish collagen, proposing improvement strategies. It systematically addresses issues related to fish collagen's biocompatibility, filling a gap in the literature. However, effectively enhancing its biocompatibility remains an urgent priority. Approaches such as nanotechnology and composite material development offer novel avenues for improving biocompatibility and future applications.
Yang et al. (Sat,) studied this question.
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