Characterization And Biological Performance Of Anglerfish Collagen And Bovine Collagen

Comparing the physicochemical properties and cell compatibility of marine-derived (anglerfish) and mammalian-derived (bovine) collagen to evaluate biomedical potential, while addressing production cost reduction and disease transmission prevention. Pepsin was used to extract collagen from anglerfish skins and bovine skins, and the pH was adjusted using NaH₂PO₄·2H₂O and NaOH to facilitate gelation. The physicochemical properties of anglerfish and bovine collagen were analyzed using UV-vis spectroscopy, FTIR, CD, SDS-PAGE, and DSC. Amino acid composition was assessed to determine structural differences. Cell compatibility was evaluated by examining the growth and proliferation of MC3T3-E1 cells cultured with both collagen types. Both anglerfish and bovine collagens displayed loose, porous fibrous networks and were identified as Type I collagen with preserved triple-helix structures. Thermal analysis showed that anglerfish collagen had lower denaturation temperatures than bovine collagen, potentially due to differences in amino acid composition. Furthermore, both collagen types significantly enhanced MC3T3-E1 cell proliferation, confirming their excellent biocompatibility. Marine-derived collagen (anglerfish) shares high structural and functional similarity with mammalian collagen. Its lower thermal stability and rapid degradability make it suitable for low-temperature applications, expanding its potential in biomedical and tissue engineering. This study provides a scientific basis for the sustainable utilization of marine collagen resources.