草鱼鱼鳞胶原蛋白的提取及其部分生物学性能

Isolation and partial biological properties of scale collagens from grass carp(Ctenopharyngodon idellus)

以草鱼鱼鳞为原料,分别提取鱼鳞中的酸溶性胶原蛋白(ASC)和酶溶性胶原蛋白(PSC),着重开展了其包括热稳定性、体外酶降解性以及胶原海绵材料特性在内的相关研究,并与哺乳动物来源的猪皮胶原(PC)相比较。实验结果表明,制备所得的3种胶原蛋白均为典型的Ⅰ型胶原并具有完整的三螺旋结构;PC的热变性温度(41.6℃)明显高于ASC(34.8℃)和PSC(35.2℃);3种胶原蛋白的体外酶降解性能受水解酶的种类、胶原蛋白提取方法、胶原蛋白来源、胶原蛋白受热历史以及蛋白的自组装程度影响。胶原蛋白酶、胰蛋白酶和木瓜蛋白酶对淡水鱼胶原均具有不同程度的降解能力,但胶原蛋白酶的降解能力最强;相同条件下,3种胶原蛋白体外酶降解率依次为ASC>PSC>PC;经热变性处理后胶原蛋白的体外酶降解率明显提高而经体外自组装处理后其体外酶降解率均出现不同程度的降低;3种胶原样品冻干后得到的胶原海绵材料具有不同的机械性能和组织结构,ASC和PSC海绵是一种多孔但拉伸承受力较弱的海绵材料,而PC则与之相反。

In this study,the acid-soluble collagen（ASC） and pepsin-soluble collagen（PSC） were extracted from scale of grass carp by the methods of acid and acid-pepsin.The partial biological properties of these collagens were researched and compared with pig skin collagen（PC）.Experiment results indicate that the ASC,PSC and PC were type Ⅰcollagen and the triple helical structure in the three collagen samples.The thermal transition temperature of PC（41.6 ℃） was obviously higher than that of ASC（34.8 ℃） and PSC（35.2 ℃）.The in vitro enzyme degradation properties of collagens were influenced by many factors,such as the enzyme variety,the isolation methods of collagen,the collagen sources,the thermal treatment and self-assembly degree of collagens.PSC can be degraded by collagenase,trypsin and papain,but the degradability of collagenase is the most notable.In the same conditions,the order of in vitro enzyme deg-radation ratio of these collagens were ASCPSCPC.The enzyme degradation ratio of these collagens could be increased after thermal treatment and could be decreased after self-assembly processing.The collagen sponges of ASC,PSC and PC have different structural and mechanical characterization.Sponges of ASC and PSC were porous and had low mechanical strength but the sponge of PC was the other way round.