Preparation and Physicochemical Properties of Collagen from Skin or Scale of Hypophthalmichthys molitrix
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Abstract:
The acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted from the skin or scale of Hypophthalmichthys molitrix, and four different collagen samples were obtained. The molecular structure and thermostability of the four collagen samples were compared, and this study provides a theoretical basis for the preparation of collagen materials from fresh fish. The study shows that the four collagen samples showed similar ultraviolet absorption spectra, FT-IR spectra, and circular dichroism spectra. Their spatial structures were similar, and they showed a natural triple helical conformation, matching the typical characteristics of type I collagen. The amino acid composition and proportion of the four collagen samples are quite similar. In the molecular structure of ASC, the content of dimeric (β-chains) subunits was relatively high, and the molecular weights of the α1 and α2 chains were the same. In the molecular structure of PSC, the content of dimeric (β-chains) subunits was relatively low. Significant differences were observed in three of the α chains, and α chain distributions in the collagen samples from PSC skin and PSC scale were different. The viscosity of ASC collagen solutions was greater than that of PSC collagen solutions, and the viscosity of the ASC skin collagen solution was greater than that of the ASC scale collagen solution. Finally, the thermal denaturation temperatures of the four H. molitrix collagens were different; that is, differences were present in the thermal stability of the collagen samples extracted from different parts by different methods.
