基于超细粉碎技术的鱼鱼皮胶原热稳定性研究  

Study on the thermal stability of channel catfish skin collagen based on ultrafine grinding

作　　者：王立慧 马倩[2] 张裕中 

机构地区：[1]江南大学食品装备工程研究中心,江苏无锡214122 [2]江南大学食品学院,江苏无锡214122

出　　处：《食品工业科技》2014年第1期70-73,共4页Science and Technology of Food Industry

基　　金：江苏省科技型创新资金项目(BC2010031)

摘　　要：利用醋酸及胃蛋白酶从经过超细粉碎的鮰鱼鱼皮中提取了胶原,并对其热稳定性进行了研究。通过差示量热扫描分析测定其变性温度和收缩温度,并将鱼皮胶原在变性温度和收缩温度下处理1h,在4℃下复性24h,后通过圆二色谱分析、傅立叶红外扫描分析和SDS-PAGE凝胶电泳分析其复性情况。结果表明:胶原蛋白的变性温度为36℃,收缩温度为65℃;SDS-PAGE凝胶电泳图谱表明所提取的胶原具备Ⅰ型胶原的特征;热处理后的胶原蛋白发生了一定程度的变性,且结构不能完全恢复;65℃处理比36℃处理的胶原蛋白复性效果好。本研究可为斑点鮰鱼鱼皮胶原的应用提供理论依据。Through the method of acid-pepsin, the collagen was extracted from the skin of channel catfish which was grinded, and its thermal stability was studied.The denaturation temperature and shrinkage temperature of skin collagenwere analyzed through differential scanning calorimetric measurements, and the renaturation of collagen was investigated through circular dichroic, FT- IR spectra and SDS- PAGE after it was treated in denaturation temperature and shrinkage temperature for i h and placed at 4℃ for 24h.The result indicated that the denaturation temperature and shrinkage temperature were respectively 36℃ and 65℃, and the collagen was characterized as type I by SDS-PAGE spectra.The structure of collagen treated in 36℃ and 65℃ was damaged to a certain extent compared with the untreated collagen,and it could＇t revert to the original structure.What＇s more,the collagen of 36℃ treatment had a better denaturation than that of 65℃ treatment.The research can provide theoretical basis for the use of channel catfish skin collagen（CCSC）.

关 键 词：鮰鱼鱼皮 胶原 变性温度 收缩温度 复性 

分 类 号：TS254.9[轻工技术与工程—水产品加工及贮藏工程]