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当前位置: 首页 > 文章 > 乌鳢和草鱼鱼皮胶原蛋白的提取与理化性能分析 食品科学 2013,34 (17) 23-27
Position: Home > Articles > Isolation and Characterization of Collagens from Skin of Grass Carp (Ctenopharyngodon idellus ) and Snakehead (Channa argus ) FOOD SCIENCE 2013,34 (17) 23-27

乌鳢和草鱼鱼皮胶原蛋白的提取与理化性能分析

作  者：
王忠稳;汪海波;梁艳萍;李云雁;王敏;汪海婴
单  位：
华中科技大学同济医学院;武汉轻工大学食品科学与工程学院
关键词：
草鱼;乌鳢;胶原蛋白;提取;理化性能
摘  要：
以草鱼鱼皮和乌鳢鱼皮为原料,提取并分离纯化酸溶性胶原蛋白和酶溶性胶原蛋白,在此基础上通过胶原蛋白的结构鉴定、热稳定性分析和体外酶降解性能分析系统比较两种胶原蛋白在分子结构和理化性能上的异同点并与哺乳动物来源的猪皮胶原蛋白相比较。结果表明:提取所得的5种胶原蛋白均为典型的Ⅰ型胶原;不同提取来源的胶原蛋白具有相似的二级结构,但其在氨基酸组成、蛋白质一级结构等方面仍存在显著的差异性;差示扫描量热仪(DSC)分析结果表明:5种胶原蛋白的热变性温度分别为:猪皮酶溶性胶原蛋白(PSC)41.58℃、草鱼酸溶性胶原蛋白(ASC)35.62℃、草鱼鱼皮PSC 35.81℃、乌鳢鱼皮ASC 33.85℃和乌鳢鱼皮PSC 34.06℃;体外酶降解性能的分析结果表明:几种胶原蛋白样品的酶降解率依次为乌鳢鱼皮PSC>草鱼鱼皮PSC>乌鳢鱼皮ASC>草鱼鱼皮ASC>猪皮PSC。与草鱼鱼皮和乌鳢鱼皮胶原蛋白相比,猪皮胶原蛋白具有更好的热稳定性和耐酶降解性能。在两种淡水鱼来源的胶原蛋白之间,草鱼鱼皮胶原具有比乌鳢鱼皮胶原更好的热稳定性和酶解稳定性。同时,酸法提取的胶原蛋白比酶法提取的胶原蛋白具有更好的酶解稳定性能。
译  名：
Isolation and Characterization of Collagens from Skin of Grass Carp (Ctenopharyngodon idellus ) and Snakehead (Channa argus )
作  者：
WANG Zhong-wen;WANG Hai-bo;LIANG Yan-ping;LI Yun-yan;WANG Min;WANG Hai-ying;College of Food Science and Engineering, Wuhan Polytechnic University;Tongji Medical College, Huazhong University of Science and Technology;
关键词：
collagen;;grass carp;;snakehead;;isolation;;physico-chemical properties
摘  要：
In this study, the molecular structure and physico-chemical properties of collagens from herbivorous fish(grass carp) and carnivorous fish(snakehead) were compared. Acid-soluble collagen(ASC) and pepsin-soluble collagen(PSC) extracted from grass carp and snakehead skins were characterized comparatively for their compositional, structural and physiochemical properties and thermal stability and the results obtained were compared with those of pig skin collagen. Results indicated that all five extracted collagens were classified as type Ⅰ collagen which comprised two different α chains( α 1 and α 2). Collagens from different sources had considerably varying amino acid composition and protein patterns as well as their primary structure. The denaturation temperatures of different collagens were: PSC from pig skin(41.58 ℃), ASC from grass carp skin(35.62 ℃), PSC from grass carp skin(35.81 ℃), ASC from snakehead skin(33.85 ℃) and PSC from snakehead skin(34.06 ℃). The enzymatic hydrolyzability of different collagens decreased in the order of snakehead skin PSC, grass carp skin PSC, snakehead skin ASC, grass carp skin PSC and pig skin PSC. Collagens extracted from grass carp and snakehead had lower denaturation temperatures and higher enzymatic hydrolyzability than those from pig skin. Grass carp skin collagens were more resistive to collagenase and showed higher denaturation temperature compared with snakehead skin collagens. In addition, ASC was more resistive to collagenase compared to PSC.

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