Mildly preheating induced conformational changes of soy protein isolates contributed to the binding interaction with blueberry anthocyanins for stabilization

IF 11 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Hydrocolloids Pub Date : 2024-05-16 DOI:10.1016/j.foodhyd.2024.110209

Siyi Tang , Xu Si , Zhihuan Zang , Hailong Gui , Xu Xie , Liang Wang , Ying He , Baoru Yang , Bin Li

{"title":"Mildly preheating induced conformational changes of soy protein isolates contributed to the binding interaction with blueberry anthocyanins for stabilization","authors":"Siyi Tang , Xu Si , Zhihuan Zang , Hailong Gui , Xu Xie , Liang Wang , Ying He , Baoru Yang , Bin Li","doi":"10.1016/j.foodhyd.2024.110209","DOIUrl":null,"url":null,"abstract":"<div>Preheated proteins have been proven to stabilize anthocyanins better than natural proteins, but the binding mechanism remains to be further studied. This study investigated the interacting mechanism between soy protein isolate (SPI) that has been slightly heated and blueberry anthocyanins (ANs) using multi-spectroscopy and molecular dynamics approaches. It was found that preheated SPI (pre-SPI) increased the stability of the ANs and provided better protection than natural SPI. In particular, SPI preheated at 45 °C provided the most effective protection against anthocyanin instability. Multi-spectroscopy demonstrates that SPI exhibits a robust affinity for and causes static quenching of malvidin-3-O-galactoside (M3G). The binding of SPI causes a considerable modification in its secondary structure, leading to a decrease in the β-sheet format and an increase in the α-helix, β-turn, and random coil structures. When heated to 45 °C, the combination effect of SPI and M3G was the most significant, thus improving blueberry ANs' stability. The interaction between SPI and M3G predominantly occurs via hydrophobic interactions. Furthermore, molecular dynamics simulations utilized the AMBER 18 protein force field and demonstrated that hydrogen bonds played a role as a source of force. Notably, pre-SPI exhibited superior anthocyanin wrapping capabilities to natural SPI, mitigating external environmental damage resulting from pocket tightening. These findings offer a deeper understanding of how proteins and ANs interact.</div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":null,"pages":null},"PeriodicalIF":11.0000,"publicationDate":"2024-05-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Hydrocolloids","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0268005X24004831","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}

引用次数: 0

Abstract

Preheated proteins have been proven to stabilize anthocyanins better than natural proteins, but the binding mechanism remains to be further studied. This study investigated the interacting mechanism between soy protein isolate (SPI) that has been slightly heated and blueberry anthocyanins (ANs) using multi-spectroscopy and molecular dynamics approaches. It was found that preheated SPI (pre-SPI) increased the stability of the ANs and provided better protection than natural SPI. In particular, SPI preheated at 45 °C provided the most effective protection against anthocyanin instability. Multi-spectroscopy demonstrates that SPI exhibits a robust affinity for and causes static quenching of malvidin-3-O-galactoside (M3G). The binding of SPI causes a considerable modification in its secondary structure, leading to a decrease in the β-sheet format and an increase in the α-helix, β-turn, and random coil structures. When heated to 45 °C, the combination effect of SPI and M3G was the most significant, thus improving blueberry ANs' stability. The interaction between SPI and M3G predominantly occurs via hydrophobic interactions. Furthermore, molecular dynamics simulations utilized the AMBER 18 protein force field and demonstrated that hydrogen bonds played a role as a source of force. Notably, pre-SPI exhibited superior anthocyanin wrapping capabilities to natural SPI, mitigating external environmental damage resulting from pocket tightening. These findings offer a deeper understanding of how proteins and ANs interact.

Abstract Image

查看原文本刊更多论文

轻度预热引起的大豆分离蛋白构象变化有助于与蓝莓花青素的结合作用，从而达到稳定效果

事实证明，预热蛋白质比天然蛋白质更能稳定花青素，但其结合机制仍有待进一步研究。本研究采用多光谱和分子动力学方法研究了经过轻微加热的大豆分离蛋白（SPI）与蓝莓花青素（ANs）之间的相互作用机制。研究发现，与天然 SPI 相比，预热 SPI（pre-SPI）可提高 ANs 的稳定性，并提供更好的保护。尤其是在 45 °C 下预热的 SPI 能最有效地防止花青素的不稳定性。多光谱分析表明，SPI 对麦饭石苷-3-半乳糖苷（M3G）具有很强的亲和力，并能使其静态淬灭。与 SPI 结合后，M3G 的二级结构发生了相当大的改变，-片状结构减少，-螺旋、-匝和无规线圈结构增加。当加热至 45 °C时，SPI 和 M3G 的组合效应最为显著，从而提高了蓝莓 ANs 的稳定性。SPI 和 M3G 之间的相互作用主要是通过疏水作用进行的。此外，分子动力学模拟使用了 AMBER 18 蛋白质力场，结果表明氢键是作用力的来源之一。值得注意的是，与天然 SPI 相比，pre-SPI 具有更强的花青素包裹能力，可减轻口袋收紧造成的外部环境破坏。这些发现加深了人们对蛋白质与花青素相互作用的理解。

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分钟内获得全文求助全文

来源期刊

Food Hydrocolloids 工程技术-食品科技

CiteScore

19.90

自引率

14.00%

发文量

871

审稿时长

37 days

期刊介绍： Food Hydrocolloids publishes original and innovative research focused on the characterization, functional properties, and applications of hydrocolloid materials used in food products. These hydrocolloids, defined as polysaccharides and proteins of commercial importance, are added to control aspects such as texture, stability, rheology, and sensory properties. The research's primary emphasis should be on the hydrocolloids themselves, with thorough descriptions of their source, nature, and physicochemical characteristics. Manuscripts are expected to clearly outline specific aims and objectives, include a fundamental discussion of research findings at the molecular level, and address the significance of the results. Studies on hydrocolloids in complex formulations should concentrate on their overall properties and mechanisms of action, while simple formulation development studies may not be considered for publication. The main areas of interest are: -Chemical and physicochemical characterisation Thermal properties including glass transitions and conformational changes- Rheological properties including viscosity, viscoelastic properties and gelation behaviour- The influence on organoleptic properties- Interfacial properties including stabilisation of dispersions, emulsions and foams- Film forming properties with application to edible films and active packaging- Encapsulation and controlled release of active compounds- The influence on health including their role as dietary fibre- Manipulation of hydrocolloid structure and functionality through chemical, biochemical and physical processes- New hydrocolloids and hydrocolloid sources of commercial potential. The Journal also publishes Review articles that provide an overview of the latest developments in topics of specific interest to researchers in this field of activity.