Sono-processing treatments enhanced the stability and digestive properties of soy-myofibrillar dual-protein systems

IF 9.7 1区 化学 Q1 ACOUSTICS
Songmin Cao , Fanwei Xi , Ziye Wang , Hui He , Di Zhao , Miao Zhang
{"title":"Sono-processing treatments enhanced the stability and digestive properties of soy-myofibrillar dual-protein systems","authors":"Songmin Cao ,&nbsp;Fanwei Xi ,&nbsp;Ziye Wang ,&nbsp;Hui He ,&nbsp;Di Zhao ,&nbsp;Miao Zhang","doi":"10.1016/j.ultsonch.2025.107613","DOIUrl":null,"url":null,"abstract":"<div><div>This study systematically investigated the effects of sono-processing treatment on the stability and digestive characteristics of soy protein isolate (SPI) and myofibrillar protein (MPN) mixed systems. The sono-processing intensity in the SPI-MPN4 group reached 37.58%, which was approximately 4.12 times higher than that of the SPI-MPN2 system (9.12%), indicating significantly greater efficiency in structural modification. Consequently, the SPI-MPN4 system exhibited the most pronounced structural transformation, leading to reduced disordered aggregation and improved system stability. To be specific, the system stability of the SPI-MPN4 system was enhanced by 28.94% when compared with that of the SPI-MPN2 group. Additionally, structural analyses revealed that ultrasound effectively disrupted hydrogen bonds, reduced α-helix content, and promoted the assembly of structurally ordered SPI–MPN complexes. Notably, the random coil contents in SPI-MPN4 increased by approximately 22.70%, facilitating trypsin accessibility. These findings highlighted that sono-processing intensity changes were critical factors governing the structural alteration of the dual-protein system. This insight was pivotal for designing targeted and energy-efficient processing strategies in the future.</div></div>","PeriodicalId":442,"journal":{"name":"Ultrasonics Sonochemistry","volume":"122 ","pages":"Article 107613"},"PeriodicalIF":9.7000,"publicationDate":"2025-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Ultrasonics Sonochemistry","FirstCategoryId":"92","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S135041772500392X","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"ACOUSTICS","Score":null,"Total":0}
引用次数: 0

Abstract

This study systematically investigated the effects of sono-processing treatment on the stability and digestive characteristics of soy protein isolate (SPI) and myofibrillar protein (MPN) mixed systems. The sono-processing intensity in the SPI-MPN4 group reached 37.58%, which was approximately 4.12 times higher than that of the SPI-MPN2 system (9.12%), indicating significantly greater efficiency in structural modification. Consequently, the SPI-MPN4 system exhibited the most pronounced structural transformation, leading to reduced disordered aggregation and improved system stability. To be specific, the system stability of the SPI-MPN4 system was enhanced by 28.94% when compared with that of the SPI-MPN2 group. Additionally, structural analyses revealed that ultrasound effectively disrupted hydrogen bonds, reduced α-helix content, and promoted the assembly of structurally ordered SPI–MPN complexes. Notably, the random coil contents in SPI-MPN4 increased by approximately 22.70%, facilitating trypsin accessibility. These findings highlighted that sono-processing intensity changes were critical factors governing the structural alteration of the dual-protein system. This insight was pivotal for designing targeted and energy-efficient processing strategies in the future.
超声处理提高了大豆-肌原纤维双蛋白系统的稳定性和消化性能。
本研究系统地研究了超声处理对大豆分离蛋白(SPI)和肌原纤维蛋白(MPN)混合体系的稳定性和消化特性的影响。SPI-MPN4体系的声处理强度达到37.58%,是SPI-MPN2体系(9.12%)的约4.12倍,表明SPI-MPN4体系的结构修饰效率显著提高。因此,SPI-MPN4体系表现出最明显的结构转变,导致无序聚集减少,提高了体系的稳定性。其中,SPI-MPN4系统的稳定性较SPI-MPN2组提高了28.94%。此外,结构分析表明,超声有效地破坏了氢键,降低了α-螺旋含量,促进了结构有序的SPI-MPN配合物的组装。值得注意的是,SPI-MPN4的随机线圈含量增加了约22.70%,促进了胰蛋白酶的可及性。这些发现强调了声加工强度的变化是控制双蛋白系统结构改变的关键因素。这一见解对于未来设计有针对性和节能的处理策略至关重要。
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
Ultrasonics Sonochemistry
Ultrasonics Sonochemistry 化学-化学综合
CiteScore
15.80
自引率
11.90%
发文量
361
审稿时长
59 days
期刊介绍: Ultrasonics Sonochemistry stands as a premier international journal dedicated to the publication of high-quality research articles primarily focusing on chemical reactions and reactors induced by ultrasonic waves, known as sonochemistry. Beyond chemical reactions, the journal also welcomes contributions related to cavitation-induced events and processing, including sonoluminescence, and the transformation of materials on chemical, physical, and biological levels. Since its inception in 1994, Ultrasonics Sonochemistry has consistently maintained a top ranking in the "Acoustics" category, reflecting its esteemed reputation in the field. The journal publishes exceptional papers covering various areas of ultrasonics and sonochemistry. Its contributions are highly regarded by both academia and industry stakeholders, demonstrating its relevance and impact in advancing research and innovation.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信