热处理对羊骨胶原蛋白结构的影响  

The Effect of Heat Treatment on Collagen Structure from Sheep

作　　者：高玲玲[1] 王振宇[1] 李铮[1] 饶伟丽[1] 张德权[1] Gao Lingling;Wang Zhenyu;Li Zheng;Rao Weili;Zhang Dequan(Key Laboratory of Agro-Products Processing, Ministry of Agriculture , Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences , Beijing 100193)

机构地区：[1]中国农业科学院农产品加工研究所农业部农产品加工重点实验室,北京100193

出　　处：《中国食品学报》2019年第3期67-74,共8页Journal of Chinese Institute Of Food Science and Technology

基　　金：国家现代肉羊产业技术体系项目(CARS-39);内蒙古自治区科技重大专项(巴彦淖尔优质羊肉加工关键技术集成与研究应用);国家农业科技创新工程

摘　　要：为明确热处理对胶原蛋白三螺旋结构域的影响,采用红外光谱分析了胶原蛋白在脱水和水溶液两种加热环境下的结构变化规律。结果表明,脱水和水溶液两种加热环境下,胶原蛋白二级结构含量变化规律相同,溶液状态下胶原蛋白对温度更加敏感;随温度的升高,其主要吸收峰发生迁移,三螺旋结构解旋,α-螺旋含量降低,无规则卷曲含量增加,分子结构逐渐舒展,无序性增大。二维红外相关光谱结果表明,脱水和水溶液两种加热环境下,胶原蛋白基团对温度的响应顺序不同,脱水加热时,脯氨酸CH3基团摇摆振动先作出响应,而水溶液加热时,N-H弯曲振动先作出响应。The aim is to study the response of collagen to temperature in the dehydration and aqueous by FTIR.The results of peak fitting of infrared spectrum showed the rules of structure changes of collagen are almost similar during the dehydration and aqueous heating, however, collagen was more sensitive to temperature in water aqueous. With the increase of temperature, the shift of the main absorption bands and the unwinding of triple helix occurred. The content of α-helix gradually reduce, and the content of random coil increased, showing the molecular structure gradually stretch and disorder. Two-dimensional infrared scorrelation spectroscopy indicated the response order of collagen molecules to temperature was different during the dehydration and aqueous heating.

关 键 词：羊骨 胶原蛋白 加热 分峰拟合 二维红外相关光谱 

分 类 号：TS251.94[轻工技术与工程—农产品加工及贮藏工程]