Modification of Mung Bean Protein Isolate Structure and Functionality by Freeze-Thaw Process

IF 2.8 4区农林科学 Q2 FOOD SCIENCE & TECHNOLOGY Food Biophysics Pub Date : 2024-11-05 DOI:10.1007/s11483-024-09897-9

Wattinee Katekhong, Uraiwun Phuangjit

{"title":"Modification of Mung Bean Protein Isolate Structure and Functionality by Freeze-Thaw Process","authors":"Wattinee Katekhong, Uraiwun Phuangjit","doi":"10.1007/s11483-024-09897-9","DOIUrl":null,"url":null,"abstract":"<div><p>This study investigated changes of the structural and functional properties of mung bean protein isolate (MPI) during multiple freeze-thaw cycles. Results showed that freeze-thaw treatment did not affect protein electrophoresis patterns but induced a more disordered secondary protein structure of MPI. The exposed sulfhydryl content and surface hydrophobicity of MPI increased first and then decreased, while, protein denaturation enthalpy decreased first and then increased, indicating the unfolding and rearrangement of protein conformation during multiple freeze-thaw cycles. The particle size diameter of MPI trended to increase as a result of freeze-thaw treatment. The foaming capacity, foaming stability, emulsifying activity index, and emulsifying stability index of MPI significantly improved by the freeze-thaw process. MPI treated with 1 freeze-thaw cycle had comparable foaming properties to soy protein isolate. However, freeze-thawing up to 5 cycles led to a negative effect on protein functionality, especially the foaming stability. Results suggested that the freeze-thaw process modified protein structure resulting in the improvement of the functional properties of MPI.</p></div>","PeriodicalId":564,"journal":{"name":"Food Biophysics","volume":null,"pages":null},"PeriodicalIF":2.8000,"publicationDate":"2024-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Biophysics","FirstCategoryId":"97","ListUrlMain":"https://link.springer.com/article/10.1007/s11483-024-09897-9","RegionNum":4,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}

引用次数: 0

Abstract

This study investigated changes of the structural and functional properties of mung bean protein isolate (MPI) during multiple freeze-thaw cycles. Results showed that freeze-thaw treatment did not affect protein electrophoresis patterns but induced a more disordered secondary protein structure of MPI. The exposed sulfhydryl content and surface hydrophobicity of MPI increased first and then decreased, while, protein denaturation enthalpy decreased first and then increased, indicating the unfolding and rearrangement of protein conformation during multiple freeze-thaw cycles. The particle size diameter of MPI trended to increase as a result of freeze-thaw treatment. The foaming capacity, foaming stability, emulsifying activity index, and emulsifying stability index of MPI significantly improved by the freeze-thaw process. MPI treated with 1 freeze-thaw cycle had comparable foaming properties to soy protein isolate. However, freeze-thawing up to 5 cycles led to a negative effect on protein functionality, especially the foaming stability. Results suggested that the freeze-thaw process modified protein structure resulting in the improvement of the functional properties of MPI.

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

用冻融工艺改变绿豆蛋白分离物的结构和功能

本研究调查了绿豆分离蛋白（MPI）在多次冻融过程中结构和功能特性的变化。结果表明，冻融处理不会影响蛋白质电泳图谱，但会导致 MPI 的二级蛋白质结构更加紊乱。MPI的外露巯基含量和表面疏水性先增大后减小，蛋白质变性焓先减小后增大，表明在多次冻融过程中蛋白质构象发生了解折和重排。冻融处理后，MPI 的粒径呈增大趋势。冻融过程显著提高了 MPI 的发泡能力、发泡稳定性、乳化活性指数和乳化稳定性指数。经过一个冻融周期处理的 MPI 具有与大豆分离蛋白相当的发泡性能。然而，冻融 5 次以上会对蛋白质的功能，尤其是发泡稳定性产生负面影响。结果表明，冻融过程改变了蛋白质结构，从而改善了 MPI 的功能特性。

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 Biophysics 工程技术-食品科技

CiteScore

5.80

自引率

3.30%

发文量

审稿时长

1 months

期刊介绍： Biophysical studies of foods and agricultural products involve research at the interface of chemistry, biology, and engineering, as well as the new interdisciplinary areas of materials science and nanotechnology. Such studies include but are certainly not limited to research in the following areas: the structure of food molecules, biopolymers, and biomaterials on the molecular, microscopic, and mesoscopic scales; the molecular basis of structure generation and maintenance in specific foods, feeds, food processing operations, and agricultural products; the mechanisms of microbial growth, death and antimicrobial action; structure/function relationships in food and agricultural biopolymers; novel biophysical techniques (spectroscopic, microscopic, thermal, rheological, etc.) for structural and dynamical characterization of food and agricultural materials and products; the properties of amorphous biomaterials and their influence on chemical reaction rate, microbial growth, or sensory properties; and molecular mechanisms of taste and smell. A hallmark of such research is a dependence on various methods of instrumental analysis that provide information on the molecular level, on various physical and chemical theories used to understand the interrelations among biological molecules, and an attempt to relate macroscopic chemical and physical properties and biological functions to the molecular structure and microscopic organization of the biological material.