Enhancing soy protein isolate flexibility through non-covalent ferulic acid modification: Implications for interfacial characteristics and protein-based emulsion performance

IF 5.6 3区农林科学 Q1 FOOD SCIENCE & TECHNOLOGY Food Structure-Netherlands Pub Date : 2024-10-01 DOI:10.1016/j.foostr.2024.100400

Yurou Chen, Mengyue Zhang, Yuhan Lan, Xibo Wang

{"title":"Enhancing soy protein isolate flexibility through non-covalent ferulic acid modification: Implications for interfacial characteristics and protein-based emulsion performance","authors":"Yurou Chen, Mengyue Zhang, Yuhan Lan, Xibo Wang","doi":"10.1016/j.foostr.2024.100400","DOIUrl":null,"url":null,"abstract":"<div><div>This study aims to enhance the flexibility of soy protein isolate (SPI) to improve its functional properties, focusing on the investigated the effects of ferulic acid (FA) on the structure, interfacial behaviour and emulsification performance of SPI. Our study showed that FA induces SPI structures to depolymerization and unfolding primarily through hydrogen bonding and hydrophobic interactions, thereby increasing the flexible structures (random coils and β-turns) of protein. These changes enhanced the interfacial functional properties of SPI, with 150 μmol/g of FA-modified SPI exhibiting the best molecular flexibility, and its emulsification and emulsification stability were improved by 21.26 % and 39.86 %, respectively, compared to unmodified SPI. In addition, non-covalently modified FA significantly improved emulsions stability. Emulsions stabilized by SPI-FA<sub>150</sub> complexes exhibited better storage, heat, and freeze-thaw stability than SPI, with a significant reduction in oxidation products. This relationship between flexibility and function reveals the importance of structural modification in enhancing protein functionality. These discoveries shed new light on flexible protein processing technologies and the application of FA in protein functional modification.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100400"},"PeriodicalIF":5.6000,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Structure-Netherlands","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2213329124000364","RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}

引用次数: 0

Abstract

This study aims to enhance the flexibility of soy protein isolate (SPI) to improve its functional properties, focusing on the investigated the effects of ferulic acid (FA) on the structure, interfacial behaviour and emulsification performance of SPI. Our study showed that FA induces SPI structures to depolymerization and unfolding primarily through hydrogen bonding and hydrophobic interactions, thereby increasing the flexible structures (random coils and β-turns) of protein. These changes enhanced the interfacial functional properties of SPI, with 150 μmol/g of FA-modified SPI exhibiting the best molecular flexibility, and its emulsification and emulsification stability were improved by 21.26 % and 39.86 %, respectively, compared to unmodified SPI. In addition, non-covalently modified FA significantly improved emulsions stability. Emulsions stabilized by SPI-FA₁₅₀ complexes exhibited better storage, heat, and freeze-thaw stability than SPI, with a significant reduction in oxidation products. This relationship between flexibility and function reveals the importance of structural modification in enhancing protein functionality. These discoveries shed new light on flexible protein processing technologies and the application of FA in protein functional modification.

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

通过非共价阿魏酸改性提高大豆分离蛋白的柔韧性：对界面特性和蛋白质乳液性能的影响

本研究旨在提高大豆分离蛋白（SPI）的柔韧性，从而改善其功能特性，重点研究阿魏酸（FA）对 SPI 结构、界面行为和乳化性能的影响。我们的研究表明，阿魏酸主要通过氢键和疏水作用诱导 SPI 结构解聚和展开，从而增加了蛋白质的柔性结构（无规线圈和 β-匝）。这些变化增强了 SPI 的界面功能特性，其中 150 μmol/g 的 FA 改性 SPI 表现出最佳的分子柔性，与未改性 SPI 相比，其乳化性和乳化稳定性分别提高了 21.26 % 和 39.86 %。此外，非共价改性的 FA 也显著提高了乳液的稳定性。与 SPI 相比，经 SPI-FA150 复合物稳定的乳液具有更好的储存稳定性、热稳定性和冻融稳定性，氧化产物也明显减少。柔性与功能之间的这种关系揭示了结构修饰在增强蛋白质功能方面的重要性。这些发现为柔性蛋白质加工技术和 FA 在蛋白质功能修饰中的应用提供了新的思路。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文去求助

来源期刊

Food Structure-Netherlands Chemical Engineering-Bioengineering

CiteScore

7.20

自引率

0.00%

发文量

期刊介绍： Food Structure is the premier international forum devoted to the publication of high-quality original research on food structure. The focus of this journal is on food structure in the context of its relationship with molecular composition, processing and macroscopic properties (e.g., shelf stability, sensory properties, etc.). Manuscripts that only report qualitative findings and micrographs and that lack sound hypothesis-driven, quantitative structure-function research are not accepted. Significance of the research findings for the food science community and/or industry must also be highlighted.