鳕鱼（大头鳕）皮中胶原蛋白的物理化学特性比较。
Comparison of physical and chemical characteristics of collagen from the skin of cod (Gadus macrocephaius).
作者信息
Shu Y, Ren H, Ao R, Qi W C, Zhang Z S
机构信息
College of Food Science and Technology, , , China.
The Yaojiazhuang Town Government, Qiaodong District, Zhangjiakou, China.
出版信息
Genet Mol Res. 2017 Jun 29;16(2):gmr-16-02-gmr.16027940. doi: 10.4238/gmr16027940.
Acid and pepsin-soluble collagen (ASC and PSC, respectively) were extracted from cod (Gadus macrocephaius) skin, and yields of 37.36 and 55.96% were obtained for ASC and PSC, respectively. The total yield of ASC and PSC was 93.92%, based on the lyophilized dry weight, which is higher than that obtained from other sources. Electrophoresis revealed that both ASC and PSC consisted of two different α-chains (α1 and α2), which were characterized as type I collagen. Analysis of amino acids showed that both the ASC and PSC contained imino acids (216.1 and 190.6 residues/1000 residues, respectively) and the Fourier transform infrared spectroscopy spectra of both collagens were similar with pepsin hydrolysis having no effect on their triple-helical structure. The thermal denaturation temperature of ASC and PSC, as measured by viscometry, was 26.8° and 25.6°C, respectively.
分别从鳕鱼（大头鳕）皮中提取酸溶性胶原蛋白（ASC）和胃蛋白酶溶性胶原蛋白（PSC），ASC和PSC的得率分别为37.36%和55.96%。基于冻干干重，ASC和PSC的总得率为93.92%，高于从其他来源获得的得率。电泳显示，ASC和PSC均由两种不同的α链（α1和α2）组成，其特征为I型胶原蛋白。氨基酸分析表明，ASC和PSC均含有亚氨基酸（分别为216.1和190.6个残基/1000个残基），两种胶原蛋白的傅里叶变换红外光谱相似，胃蛋白酶水解对其三螺旋结构无影响。通过粘度测定法测得，ASC和PSC的热变性温度分别为26.8℃和25.6℃。
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