文献类型：期刊文献

英文题名：Insight into the interaction mechanism between mulberry polyphenols and β-lactoglobulin

作者：Yuan, Qi[1,2];He, Lin[1,2];Wang, Xuping[1];Yang, Huaigu[1];Zhu, Fan[3];Peng, Xiaoxia[4];Cheng, Jingrong[1];Lin, Yaosheng[1];Tang, Daobang[1];Liu, Xueming[1,2,5]

机构：[1]Minist Agr & Rural Affairs, Sericultural & Agri Food Res Inst Guangdong Acad A, Key Lab Funct Foods, Guangdong Key Lab Agr Prod Proc, Guangzhou 510610, Peoples R China;[2]Guangdong Ocean Univ, Coll Food Sci & Technol, Zhanjiang 524088, Peoples R China;[3]Univ Auckland, Sch Chem Sci, Private Bag 92019, Auckland 1142, New Zealand;[4]Guangdong Yantang Dairy Co Ltd, Guangzhou 510700, Peoples R China;[5]133 Yihenglu, Guangzhou 510610, Peoples R China

年份：2024

卷号：149

外文期刊名：FOOD HYDROCOLLOIDS

收录：SCI-EXPANDED(收录号：WOS:001128174200001)、、EI(收录号：20234815107173)、Scopus(收录号：2-s2.0-85177618350)、WOS

基金：This work was supported by the financial support of Special Project for Research and Development in Key areas of Guangdong Province [grant number 2022B0202030002] , Guangzhou Science and Technol- ogy Program key projects [grant number 201907010029] , Guangzhou Basic and Applied Basic Project [grant number 202201010671] . Authors also acknowledge Dr. David Hopkins for the assistance on manuscript modification.

语种：英文

外文关键词：Mulberry polyphenol; beta-Lactoglobulin; Interaction force; Structure modification; Molecular docking

外文摘要：The interaction mechanism of components in complex food systems is one of the hot topics in food science. Both protein and polyphenols co-exists in many foods, but their interaction mechanism is very difficult to elucidate. In this paper, the interaction between mulberry polyphenols (MP) and beta-lactoglobulin (beta-LG) was investigated based on individual phenolic ratios in MP to explore impact of MP on beta-LG. The results showed that the effects of MP on beta-LG could be reproduced by simulated MP (sMP) which was composed of the main individual phenolics in MP. MP, sMP and individual phenolics interacted with beta-LG through static quenching, in which MP, sMP, cyanindin-3-rutinoside (C3R) and epicatechin (EC) bound to beta-LG via hydrogen bonds and van der Waals force; cyanindin-3-glucose (C3G) and p-coumaric acid (PCA) bound to beta-LG via hydrogen bonds and hydrophobic interactions; but quercetin (Q), rutin (R), protocatechuic acid (PA) and pelargonidin-3-glucosid (Pg3G) bound to beta-LG mainly through hydrophobic interaction. Addition of MP, sMP or most individual phenolics of MP significantly increased the particle size of beta-LG. C3G, C3R, PCA, Q and R, with varying degrees of influence, markedly changed secondary structure of beta-LG by affecting the microenvironment of amino acids residues. Furthermore, R, PCA, EC and Pg3G induced the transition from beta-fold to alpha-helix of beta-LG, making the protein more stable. The contribution of each individual phenolic to the interaction between MP and beta-LG was mainly dose-dependent and also influenced by their chemical structures.