摘要
针对鱼皮胶原蛋白ASC(acid soluble collagen)和PSC(pepsin soluble collagen)的提取和性质进行研究。经过SDS-凝胶电泳初步确定其为Ⅰ型胶原,蛋白的组成为(α1)2α2,氨基酸分析两种蛋白质都具有胶原蛋白的典型特征。两种蛋白之间在分子构型、氨基酸组成等方面的差异不明显。但从黏度变化、DSC分析来看,二者之间存在一定的差异。推测差异产生的原因与蛋白质制备方法有关,非螺旋区域对三螺旋的稳定性起着重要作用,非螺旋区域的分解大大降低了PSC对热的耐受性。
The fish skin of Cyprinus carpio was employed as raw material to extract collagen. Two types of collagen ASC and PSC were studied in the paper. It can be seen that the difference between ASC and PSC was not prominent from amino acid and SDS-page analysis. On the other hand, the properties of ASC and PSC was different from DSC and viscosity experiments. The difference may be caused by the hydrolysis of non-helix peptide which is very important to the thermal-stability of three-helix collagen. The hydrolysis of non-helix peptide reduced the thermal stability of collagen greatly.
出处
《食品科技》
CAS
北大核心
2008年第10期173-177,共5页
Food Science and Technology
基金
江苏省海洋生物重点建设实验室基金项目(2006HS016)
关键词
鲤鱼鱼鳞
胶原蛋白
ASC
PSC
fish skin
Cyprinus carpio
decalcification
collagen
