Study On The Preparation And Physical And Chemical Properties Of Silver Carp Skin And Fish Scale Collagen
Keywords
Hypophthalmichthys Molitrix Collagen Preparation Physicochemical Properties
Abstract
Acid-soluble and enzyme-soluble collagen were extracted and purified from silver carp skin and fish scales respectively, and four different collagens were obtained. The similarities and differences of the four collagens in terms of molecular composition, spatial structure, thermal stability, etc. were analyzed, and the results were based on freshwater fish sources. Provide a theoretical basis for the construction of collagen materials. The study found that the UV spectra, infrared spectra and circular dichroism spectra of the four collagens are similar, that is, the spatial structures are similar, and they all have a natural triple helix spatial conformation, which is consistent with the characteristics of typical type I collagen; the amino acid compositions of the four collagens and The ratio is close; the molecular structure of acid-soluble collagen (ASC) contains more dimer ¦Â-chains, and the molecular weights of ¦Á1 chain and ¦Á3 chain are the same, while the molecular structure of enzyme-soluble collagen (PSC) contains less dimer ¦Â-chains, with three The ¦Á chain distinction is obvious, and the molecular weight distribution of the ¦Á chain of fish skin PSC and fish scale PSC is different; the viscosity of the ASC solution is greater than that of PSC, and the viscosity of the fish skin ASC solution is greater than that of fish scale ASC; the thermal denaturation temperatures of the four silver carp collagens are different, that is, they are used in different Methods The thermal stability of collagen extracted from different parts is different. 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 (¦Â-chains) subunits was relatively high, and the molecular weights of the ¦Á1 and ¦Á2 chains were the same. In the molecular structure of PSC, the content of dimeric (¦Â-chains) subunits was relatively low. Significant differences were observed in three of the ¦Á chains, and ¦Á 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.
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Original research was done by Li Yue
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