Comparative Study On The Properties And Self-Aggregation Behavior Of Grass Carp Scales And Grass Carp Skin Collagen
Keywords
Grass Carp Skin, Grass Carp Scales, Collagen Properties, Self-Aggregation
Abstract
Abstract Using grass carp as raw material, an acid-enzyme combination method was used to extract collagen from fish scales and skin. Ultraviolet spectrum (UV), polyacrylamide gel electrophoresis (Sodium dodecylsulphate-polyacrylamide gel electrophoresis, SDS-PAGE), and Fourier transform were used to extract collagen. Fourier transform infrared spectroscopy (FTIR) and differential scanning calorimetry (DSC) were used to compare their structural properties, and turbidity experiments, aggregation degree experiments and scanning electron microscopy (SEM) were used to compare the two. Self-aggregation behavior of collagen in vitro. The results show that the two extracted collagens have two ¦Á chains, are typical type I collagen, and maintain a good triple helix structure. The denaturation temperatures of fish scales and fish skin are 34.99 ¡ãC and 39.75 ¡ãC respectively. Under the conditions of neutral salt solution at 30 ¡ãC, both collagens can produce self-aggregation behavior, and the aggregation degrees of fish skin and fish scale collagen are 28% and 27.33% respectively. It was observed by SEM that both collagens from both sources can self-aggregate to form interwoven fibers. Among them, fish scale collagen has a more obvious network fiber structure and has periodic striated D bands of collagen fibrils, while fish skin collagen self-aggregates. The collagen fiber structure has some collapse and no D-band
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Original research was done by 10.13995/j.cnki.11-1802/ts.014818
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