酸法和酶法提取草鱼鱼鳞胶原蛋白的特性分析  

Comparative Analysis of Collagen Extracted from Grass Carp Fish Scale Using Acid and Enzyme Methods

作　　者：杨平[1] 刘影[1] 公丽艳 许青[1] YANG Ping;LIU Ying;GONG Liyan;XU Qing(Shenyang Normal University（Shenyang 110034)

机构地区：[1]沈阳师范大学,沈阳110034

出　　处：《食品工业》2018年第7期129-132,共4页The Food Industry

基　　金：辽宁省自然科学基金(20170540815);国家重点研发计划课题(2016YFD0400404)

摘　　要：以草鱼鱼鳞为原料,分别采用酸法和酶法提取胶原蛋白并进行理化性质分析。通过氨基酸组成、紫外光谱、傅里叶红外光谱、聚丙烯酰胺凝胶电泳(SDS-PAGE)、变性温度,对胶原蛋白进行比较。结果表明,2种方法的提取物均为典型的胶原蛋白,在波长230 nm左右出现最大紫外吸收峰;红外光谱及SDS-PAGE凝胶电泳显示提取的ASC和PSC主体结构一致,属于Ⅰ型胶原蛋白,胃蛋白酶不会破坏胶蛋白三螺旋构象,酸溶胶原蛋白和酶溶胶原蛋白的热变性分别为30.16℃和30.63℃。综合来看2种方法所提胶原蛋白在理化特性上并无太大差别,可以利用胃蛋白酶处理有效提高胶原蛋白的提取率。Taking the grass carp fish scale as raw material, acid method and acidolysis enzyme were used to extract collagen and the physical and chemical properties were compared. The amino acid composition of obtained collagens was analyzed and their structures were determined by using UV spectrum, fourier transform infrared spectroscopy, SDS-PAGE, and thermal denaturation temperature. The extracts were characterized as collagens with the maximum UV absorption peak showing at 230 nm. FT-IR and SDS-PAGE analysis demonstrated that the main structure of ASC and PSC is consistent, which belongs to type Ⅰ collagen, and pepsin does not cause damage to the three-strand spiral structure. The thermal denaturation temperature of Acid-soluble collagen（ASC） and pepsin-soluble collagen（PSC） was 30.16 ℃ and 30.63 ℃. There was no significant difference in the physiochemical properties of collagens obtained using the two methods. The extraction rate of collagen can be improved by pepsin treatment.

关 键 词：草鱼鱼鳞 胶原蛋白 酸法 酶法 

分 类 号：TS254.9[轻工技术与工程—水产品加工及贮藏工程]