摘要
Collagen of squid （Ommastrephes bartrami） skin was examined in the present study. Histology showed that collagen fiber in the skin was partially cross-linked with muscle fiber. Acid-solubilized collagen （ASC） and pepsin-solubilized collagen （PSC） were extracted from the skin and characterized. The results of amino acid composition and electrophoretic patterns revealed that ASC and PSC were both type 1 collagen, containing α1 and α2 chains. FTIR （fourier transform infrared spectroscopy） investigations confirmed the existence of helical arrangements in PSC of squid skin. The denaturation temperature （Td） and shrinkage temperature （T5） of PSC were 29.4℃ and 52.8℃, respectively.
Collagen of squid(Ommastrephes bartrami) skin was examined in the present study. Histology showed that collagen fiber in the skin was partially cross-linked with muscle fiber. Acid-solubilized collagen(ASC) and pepsin-solubilized collagen(PSC) were extracted from the skin and characterized. The results of amino acid composition and electrophoretic patterns revealed that ASC and PSC were both type Ⅰ collagen,containing α1 and α2 chains. FTIR(fourier transform infrared spectroscopy) investigations confirmed the existence of helical arrangements in PSC of squid skin. The denaturation temperature(Td) and shrinkage temperature(Ts) of PSC were 29.4℃ and 52.8℃,respectively.
基金
supported by the High Technology Research and Development Programme of China (No. 2006AA09Z438)
the National Natural Science Foundation of China (No.30871943).
