Study Of The Material Property Of Fish Scale Collagen By Composing With Other Collagens
Keywords
Fish Scale Collagen Mixture Modificationfish Scale Collagen Mixture Modification
Abstract
This study uses fish scale type I collagen as the matrix and mixes it with beef tendon and pig skin collagen respectively. The performance changes of collagen sponge after fish scale collagen, beef tendon and pig skin collagen are mixed and reorganized. Infrared analysis shows that the special three characteristics of the mixed and recombined collagen are The spiral structure is intact, and the absorption performance shows that the water absorption of the recombinant collagen sponge appears at the optimal value. The scanning electron microscope shows that the structure of the fish scale collagen fibers is tighter after the mixing and reorganization, and the enzymatic hydrolysis, thermal denaturation and heat treatment, which represent a significant increase in the cross-linking degree of the collagen. The weight loss results showed that the enzymatic stability and thermal stability of the mixed collagen sponge were significantly improved. In the present study, porcine and bovine collagen were mixed respectively with the matrix composed of fish scale type I collagen, and then the properties of the reconstructed collagen sponge were tested. The fourier transform infrared spectroscopy (FTIR) analysis showed intact retention of the classical triple-helix structure after reconstruction with perfect water absorption capacity. The micro-fibril structure of the fish scale type I collagen in the mixture was observed more compact by scanning electron microscope(SEM), and significant improvements in thermostability and enzymatic hydrolysis stability were also detected by tests of enzymatic hydrolysis, differential scanning calorimetry (DSC), and thermogravimetry (TG)
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Original research was done by Du Tianming, Chen Zihao, Tang Xiangyu, Wu Jimin
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