鲟鱼鱼皮胶原蛋白的提取及其理化性能分析  

Isolation and Characterization of Collagens from the Skin of Sturgeon

作　　者：杨玲[1] 赵燕[2] 鲁亮[2] 王忠稳[2] 宋保垒 王占方 汪海波[1] 

机构地区：[1]武汉轻工大学化学与环境工程学院,湖北武汉430023 [2]武汉轻工大学食品科学与工程学院,湖北武汉430023 [3]河北省粮食产业集团有限公司,河北石家庄050800

出　　处：《食品科学》2013年第23期41-46,共6页Food Science

基　　金：国家自然科学基金面上项目(21076166);武汉市科技局科技攻关计划项目(200920137006);武汉市农副资源循环利用与新产品开发工程技术中心资助项目(201120637175);湖北省自然科学基金重点项目(2009CDA117);武汉市科技局应用基础研究项目(2013020501010177);湖北省高校优秀中青年创新团队项目(T201208)

摘　　要：从鲟鱼鱼皮中分别提取、纯化酸溶性胶原蛋白(ASC)和酶溶性胶原蛋白(PSC),并对鲟鱼鱼皮胶原蛋白分子结构组成及理化性能进行测定和分析,并与哺乳动物来源的牛跟腱胶原进行比较研究。结果表明:提取所得的鲟鱼鱼皮胶原和牛跟腱胶原均为典型的Ⅰ型胶原;鲟鱼鱼皮胶原ASC和PSC的氨基酸组成和蛋白二级结构基本一致,但与牛跟腱胶原有较明显的差异性;胶原蛋白的理化性能分析结果表明:鲟鱼鱼皮胶原蛋白ASC和PSC的热变性温度(28.04、28.13℃)明显低于牛跟腱胶原蛋白的变性温度(42.81℃);在溶液状态下,牛跟腱胶原蛋白更容易形成分子间的聚集体且展现出比鲟鱼鱼皮胶原蛋白更好的耐酶降解能力。In this study, acid-soluble collagen （ASC） and pepsin-soluble collagen （PSC） were extracted from sturgeon skin by the methods of acid and acid-pepsin. The molecular structures and physicochemical properties of ASC and PSC were determined and compared with those of bovine Achilles tendon collagen. The results indicated that the ASC and PSC were similar in their amino acid composition and secondary structures, but they were different from those of bovine Achilles tendon collagen. The denaturation temperatures for these collagens were determined to be 42.81℃ for bovine Achilles tendon collagen, 28.04 ℃ for sturgeon skin ASC and 28.13 ℃ for sturgeon skin PSC, suggesting an obvious difference in thermostability between sturgeon skin collagen and bovine Achilles tendon collagen. In the solution state, bovine Achilles tendon collagen could more easily form collagen polymers and was more resistant to enzymatic hydrolysis than sturgeon skin collagen.

关 键 词：鲟鱼皮 牛跟腱 胶原蛋白 提取 理化性能 

分 类 号：TQ93[化学工程]