光谱法研究黑米花色苷与酪蛋白的相互作用  

Studies on the interaction between casein and black rice anthocyanin by spectroscopic methodology

作　　者：赵焕焦 吕晓玲[1] 王梦姝[1] 王璐瑶[1] 

机构地区：[1]天津科技大学食品工程与生物技术学院,天津300457

出　　处：《中国食品添加剂》2017年第1期121-127,共7页China Food Additives

基　　金：国家科技支撑计划项目:食用色素制备关键技术研究及产业化;课题编号:2011BAD23B02

摘　　要：从荧光光谱、同步荧光光谱、紫外可见光谱、抗氧化能力等方面,研究黑米花色苷与酪蛋白在模拟生理条件下的相互作用。研究结果显示黑米花色苷对酪蛋白具有较强的荧光猝灭,猝灭方式为静态猝灭,形成BRA-BSA复合物,并计算得到反应的结合位点数和结合常数,热力学参数表明氢键为其主要的作用力;根据Fster非辐射能量转移理论,计算出结合距离r为3.00nm,进一步确定了反应过程中静态猝灭机理的存在。同步荧光光谱结果显示,黑米花色苷与酪蛋白的相互作用影响蛋白质的构象,结合位点更接近于色氨酸。In this paper,we have studied the interaction between black rice anthocyanm（BRA） and casein（Cs）,using fluorescence,synchronous fluorescence spectroscopy,ultraviolet spectroscopy and the antioxidant capacity under simulated physiological conditions.The results showed that black rice anthocyanin had a strong ability to quench the casein fluorescence in a static mode,forming BRA- BSA compound and the binding constants（Ka）and site numbers（n） are obtained at different temperatures.Based on the thermodynamic parameters,the main interaction force was hydrogen bonding in the interaction between BRA and casein.According to Frster＇ s non- radiative energy transfer theory,the proximity of the acceptor to the donor in BRA- Cs complex was calculated as 3.00 nm,which further confirmed the existence of static quenching mechanism.The synchronous fluorescence spectra revealed that the interaction between BRA and Cs influenced the conformation of protein,and the binding site was more close to tryptophan.

关 键 词：黑米花色苷 酪蛋白 荧光光谱 紫外吸收光谱 抗氧化 

分 类 号：TS202.3[轻工技术与工程—食品科学] TS264.4[轻工技术与工程—食品科学与工程]