摘要
采用荧光光谱、紫外吸收光谱和计算机模拟分子对接研究了偶氮类食品着色剂诱惑红与蛋溶菌酶的相互作用.讨论了诱惑红对蛋溶菌酶荧光的猝灭机理,属于静态猝灭.测定了诱惑红与蛋溶菌酶反应体系的结合常数和结合位点数,根据热力学参数焓变(ΔH>0)和熵变(ΔS>0)可推断诱惑红和蛋溶菌酶的相互作用力为典型的疏水作用力.在298、304、310 K温度下,两者间的结合常数分别为17897、19865、23267.
To explore the interaction between food pigment allure red and lysozyme,fluorescence spectroscopy,ultraviolet spectroscopy and docking were used.The discussion revealed that fluorescence quenching mechanism for lysozyme was suggested as static quenching.The binding constants and binding sites of the reaction system of allure red and lysozyme were determined.According to the thermodynamic parameters of the enthalpy change(ΔH>0)and entropy(ΔS>0),it could be inferred that the interaction between allure red and lysozyme was Vander Ed Ley and hydrogen bonds.At the temperature of 298 K,304 K,310 K,the binding constants were 17897,19865,23267.
作者
胡霞
唐岚
曾珍
张静
周典
吴笛
HU Xia;TANG Lan;ZENG Zhen;ZHANG Jing;ZHOU Dian;WU Di(School of Food and Bioengineering,Chengdu University,Chengdu 610106,China)
出处
《成都大学学报(自然科学版)》
2021年第1期35-40,共6页
Journal of Chengdu University(Natural Science Edition)
基金
国家自然科学基金(21808020)资助项目。