罗非鱼皮胶原蛋白肽亚铁螯合修饰及螯合物性质的研究  

Preparation,characterization and antioxidant activity of tilapia skin collagen polypeptides chelated iron

作　　者：段秀[1] 杨成涛[1] 孙云[1] 孙丽平[1] 庄永亮[1] 

机构地区：[1]昆明理工大学化学工程学院食品科学研究中心,云南昆明650500

出　　处：《食品工业科技》2014年第18期157-160,166,共5页Science and Technology of Food Industry

基　　金：国家自然科学基金项目(31101392)

摘　　要：以罗非鱼皮为原料制备胶原蛋白肽(TSGP),胶原蛋白肽与亚铁盐进行螯合反应,对TSGP亚铁螯合物的理化性质及功能特性进行研究。实验优化得出最佳螯合反应条件是m多肽∶mFeCl2·4H2O=500∶1,pH为6.0,反应时间50min,温度35℃。通过荧光光谱、紫外光谱和红外光谱测定发现Fe2+与TSGP的羧基与氨基均可发生配位反应。抗氧化活性测定实验表明,螯合物具有较强的清除DPPH自由基和ABTS+自由基的能力。Tilapia skin collagen polypeptides（TSGP） was prepared and chelated by iron. The physical,chemical and functional properties of the chelate were characterized. The optimum parameters of chelating as follows：mpolypeptides：mFeCl2·4H2O=500：1, pH6.0, reaction time 50min,temperature 35℃. The formation of iron-TSGP chelate was confirmed by the Ultraviolet spectrum and Infrared spectroscopy,and found that the carboxyl and amino group of TSGP bounded with iron. In addition,chelate had a strong radical scavenging activities of DPPH· and ABTS^＋.

关 键 词：罗非鱼皮 胶原蛋白肽 亚铁螯合物 结构 抗氧化 

分 类 号：TS201.1[轻工技术与工程—食品科学]