Heat treatment effect on whey protein-epigallocatechin gallate interaction: A fluorescence spectroscopic analysis
文献类型： 外文期刊
作者： Song, Yu-qi 1 ; Zhao, Ying 3 ; Yao, Guanglong 2 ; Dong, Rong-shu 1 ; Chen, Jian 2 ;
作者机构： 1.Chinese Acad Trop Agr Sci, Inst Trop Crop Genet Resources, Dept Grass Res, Haikou 571101, Peoples R China
2.Hainan Univ, Key Lab Food Nutr & Funct Food Hainan Prov, Engn Res Ctr Utilizat Trop Polysaccharide Resource, Minist Educ,One Hlth Inst,Coll Food Sci & Technol, Haikou 570228, Peoples R China
3.Hainan Univ, Forestry Inst, Hainan Key Lab Biol Trop Flowers & Trees Resources, Haikou 570228, Peoples R China
关键词： Epigallocatechin gallate; Whey protein; Interaction; Quenching mechanism
期刊名称：FOOD CHEMISTRY-X （ 影响因子：6.1； 五年影响因子：6.4 ）
ISSN： 2590-1575
年卷期： 2023 年 20 卷
页码：
收录情况： SCI
摘要： This study aimed to examine the interaction mechanism of polyphenol protein in a heat-treated aqueous solution system using epigallocatechin gallate (EGCG) and whey protein (WP) as raw materials. Further, we hypothesized the binding characteristics of these two compounds. The results were as follows: The quenching mechanism between WP and EGCG was characterized as static quenching. As the temperature increased, the binding constant and the binding force between EGCG and WP both increased. The number of binding sites (denoted as n) between WP and EGCG was approximately 1. Hence, WP provided a single site to bind to EGCG to form a complex. The main binding modes between WP and EGCG were hydrophobic and electrostatic interactions, and they were spontaneously combined into complexes (Delta G < 0). This study provided a basis for the interaction between WP and EGCG under different heating conditions and their combination mode.
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