摘要
利用荧光猝灭法研究在pH值为6.5时,不同温度(25℃、35℃和45℃)下β-酪蛋白与表没食子儿茶素没食子酸酯(EGCG)之间的相互作用机制.实验结果表明,EGCG可与β-酪蛋白相互作用形成复合物从而引起后者发生内源性的静态荧光猝灭.不同温度(25℃、35℃和45℃)下,其双分子猝灭速率常数(K_q)分别为0.664×10^(13) L/(mol·s)、0.629×10^(13) L/(mol·s)和0.945×10^(13) L/(mol·s),结合位点(n)数约为1.热力学参数值分析结果显示EGCG与β-酪蛋白的结合过程为吉普斯自由能降低的自发过程,二者之间的作用类型以疏水作用力为主.
The interactions between epigallocatechin gallate(EGCG)andβ-casein at different temperatures(25℃,35℃and 45℃,in phosphate-buffered saline of pH 6.5)were investigated using fluorescence quenching.The experimental results indicated that EGCG can interact withβ-casein to form a complex,which caused the latter to undergo endogenous static fluorescence quenching.The fluorescence quenching rate constants(K q)were 0.664×10^13 L/(mol·s)、0.629×10^13 L/(mol·s)and 0.945×10^13 L/(mol·s)at different temperatures(25℃,35℃and 45℃),respectively,and the number of binding sites(n)was about 1.Thermodynamic parameters analysis showed that the binding process of EGCG withβ-casein was a spontaneous process of Gibbs free energy reduction,and the interaction between EGCG andβ-casein was mainly a hydrophobic force.
作者
曹云刚
陈星怡
齐梦恬
李颖
赵倩倩
CAO Yun-gang;CHEN Xing-yi;QI Meng-tian;LI Ying;ZHAO Qian-qian(School of Food and Biological Engineering,Shaanxi University of Science & Technology,Xi′an 710021,China)
出处
《陕西科技大学学报》
CAS
2019年第3期59-63,共5页
Journal of Shaanxi University of Science & Technology
基金
国家自然科学基金项目(31801480)
陕西省科技厅自然科学基础研究计划项目(2019JQ-397)
陕西科技大学大学生创新创业训练计划项目(2018019)
陕西科技大学自然科学预研基金项目(2016QNBJ-16
2016BJ-53)
