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通过非共价相互作用形成的多糖-乳清分离蛋白(WPI)复合物的分子特性

Molecular Properties of Polysaccharide-Whey Protein Isolate (WPI) Complexes via Noncovalent Interactions.

作者信息

Shang Jiaqi, Liao Minhe, Jin Ritian, Teng Xiangyu, Li Hao, Xu Yan, Zhang Ligang, Liu Ning

机构信息

Key Laboratory of Dairy Science, Ministry of Education, Harbin 150030, China.

College of Food Science, Northeast Agricultural University, Harbin 150030, China.

出版信息

Foods. 2020 Dec 22;10(1):1. doi: 10.3390/foods10010001.

DOI:10.3390/foods10010001
PMID:33374899
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7821936/
Abstract

Whey protein isolate (WPI) has a variety of nutritional benefits. The stability of WPI beverages has attracted a large amount of attention. In this study, polysaccharides (FVPs) interacted with WPI to improve the stability via noncovalent interactions. Multiple light scattering studies showed that FVPs can improve the stability of WPI solutions, with results of radical scavenging activity assays demonstrating that the solutions of the complex had antioxidant activity. The addition of FVPs significantly altered the secondary structures of WPI, including its α-helix and random coil. The results of bio-layer interferometry (BLI) analysis indicated that FVPs interacted with the WPI, and the equilibrium dissociation constant () was calculated as 1.736 × 10 M in this study. The in vitro digestibility studies showed that the FVPs protected WPI from pepsin digestion, increasing the satiety. Therefore, FVPs effectively interact with WPI through noncovalent interactions and improve the stability of WPI, with this method expected to be used in protein-enriched and functional beverages.

摘要

乳清分离蛋白(WPI)具有多种营养益处。WPI饮料的稳定性已引起大量关注。在本研究中,多糖(FVPs)与WPI相互作用,通过非共价相互作用提高稳定性。多重光散射研究表明,FVPs可提高WPI溶液的稳定性,自由基清除活性测定结果表明复合物溶液具有抗氧化活性。FVPs的添加显著改变了WPI的二级结构,包括其α-螺旋和无规卷曲。生物层干涉术(BLI)分析结果表明,FVPs与WPI相互作用,本研究中计算出的平衡解离常数()为1.736×10 M。体外消化率研究表明,FVPs可保护WPI不被胃蛋白酶消化,增加饱腹感。因此,FVPs通过非共价相互作用与WPI有效相互作用并提高WPI的稳定性,预计该方法可用于富含蛋白质的功能性饮料。

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