通过乳清蛋白组成蛋白的协同相互作用稳定和降解白藜芦醇的机制。

The mechanism of resveratrol stabilization and degradation by synergistic interactions between constituent proteins of whey protein.

机构信息

State Key Lab of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, China; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu, China; Particle and Interfacial Technology Group, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, B-9000 Gent, Belgium.

Key Laboratory of Dairy Biotechnology and Engineering, Ministry of Education, Inner Mongolia Agricultural University, Hohhot, Inner Mongolia, China.

出版信息

Food Res Int. 2024 Jul;188:114485. doi: 10.1016/j.foodres.2024.114485. Epub 2024 May 9.

DOI:10.1016/j.foodres.2024.114485

PMID:38823871

Abstract

Whey protein isolate (WPI) is mainly composed of β-lactoglobulin (β-LG), α-lactalbumin (α-LA) and bovine serum albumin (BSA). The aim of this study was to compare and analyze the influence of WPI and its three main constituent proteins, as well as proportionally reconstituted WPI (R-WPI) on resveratrol. It was found that the storage stability of resveratrol was protected by WPI, not affected by R-WPI, but reduced by individual whey proteins at 45°C for 30 days. The rank of accelerated degradation of resveratrol by individual whey proteins was BSA > α-LA > β-LG. The antioxidant activity, localization of resveratrol and oxidation of carrier proteins were determined by ABTS, HO assay, synchronous fluorescence, carbonyl and circular dichroism. The non-covalent interactions and disulfide bonds between constituent proteins improved the antioxidant activity of the R-WPI-resveratrol complex, the oxidation stability of the carrier and the solvent shielding effect on resveratrol, which synergistically inhibited the degradation of resveratrol in R-WPI system. The results gave insight into elucidating the interaction mechanism of resveratrol with protein carriers.

摘要

乳清蛋白分离物（WPI）主要由β-乳球蛋白（β-LG）、α-乳白蛋白（α-LA）和牛血清白蛋白（BSA）组成。本研究旨在比较和分析 WPI 及其三种主要组成蛋白以及按比例重构的 WPI（R-WPI）对白藜芦醇的影响。结果表明，WPI 保护白藜芦醇的储存稳定性，不受 R-WPI 影响，但在 45°C 下 30 天会降低个别乳清蛋白的稳定性。个别乳清蛋白对白藜芦醇加速降解的影响程度为 BSA＞α-LA＞β-LG。通过 ABTS、HO 测定法、同步荧光、羰基和圆二色性测定法，确定了白藜芦醇的抗氧化活性、定位和载体蛋白的氧化情况。组成蛋白之间的非共价相互作用和二硫键提高了 R-WPI-白藜芦醇复合物的抗氧化活性、载体的氧化稳定性以及对白藜芦醇的溶剂屏蔽效应，从而协同抑制了 R-WPI 体系中白藜芦醇的降解。结果深入阐明了白藜芦醇与蛋白质载体的相互作用机制。