Effect of Lactobacillus pentosus fermentation on molecular structure and gel quality of peanut protein

IF 5.2 Q1 FOOD SCIENCE & TECHNOLOGY Journal of Future Foods Pub Date : 2024-09-24 DOI:10.1016/j.jfutfo.2024.07.005
{"title":"Effect of Lactobacillus pentosus fermentation on molecular structure and gel quality of peanut protein","authors":"","doi":"10.1016/j.jfutfo.2024.07.005","DOIUrl":null,"url":null,"abstract":"<div><div>Peanut protein was fermented by <em>Lactobacillus pentosus</em>, to study the effects of different protein composition of peanut protein isolate, arachin and concomitant arachin on their molecular structure and thermal properties during fermentation, the composite gel was prepared by compounding peanut protein with myofibril protein, the rheological properties of the composite emulsion and the texture properties of the composite gel were studied to reveal the molecular mechanism of the effect of <em>L. pentosus</em> on the gel properties of peanut protein. The results showed that the free sulfhydryl content, surface hydrophobicity and denaturation temperature of arachin were increased, <em>β</em>-sheet content and denaturation enthalpy were decreased by <em>L. pentosus</em> fermentation. It can reduce the content of free sulfhydryl group, surface hydrophobicity and denaturation enthalpy of peanut protein isolate and concomitant arachin, the denaturation temperature and <em>α</em>-helix content of peanut protein isolate and arachin were significantly increased. After fermentation, the structure of arachin developed to the maximum and the thermal stability of arachin was higher, which proved that <em>L. pentosus</em> could promote the gel modification of peanut protein. The complex gel formed by fermentation with arachin is easier to form porous structure and has better macro-elasticity than the complex gel prepared by modification of arachin and isolate protein.</div></div>","PeriodicalId":100784,"journal":{"name":"Journal of Future Foods","volume":null,"pages":null},"PeriodicalIF":5.2000,"publicationDate":"2024-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2772566924000399/pdfft?md5=558e1e599f080c461f252cf92ca056a6&pid=1-s2.0-S2772566924000399-main.pdf","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Future Foods","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2772566924000399","RegionNum":0,"RegionCategory":null,"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

Peanut protein was fermented by Lactobacillus pentosus, to study the effects of different protein composition of peanut protein isolate, arachin and concomitant arachin on their molecular structure and thermal properties during fermentation, the composite gel was prepared by compounding peanut protein with myofibril protein, the rheological properties of the composite emulsion and the texture properties of the composite gel were studied to reveal the molecular mechanism of the effect of L. pentosus on the gel properties of peanut protein. The results showed that the free sulfhydryl content, surface hydrophobicity and denaturation temperature of arachin were increased, β-sheet content and denaturation enthalpy were decreased by L. pentosus fermentation. It can reduce the content of free sulfhydryl group, surface hydrophobicity and denaturation enthalpy of peanut protein isolate and concomitant arachin, the denaturation temperature and α-helix content of peanut protein isolate and arachin were significantly increased. After fermentation, the structure of arachin developed to the maximum and the thermal stability of arachin was higher, which proved that L. pentosus could promote the gel modification of peanut protein. The complex gel formed by fermentation with arachin is easier to form porous structure and has better macro-elasticity than the complex gel prepared by modification of arachin and isolate protein.
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
五味子乳杆菌发酵对花生蛋白分子结构和凝胶质量的影响
以五味子乳杆菌发酵花生蛋白,研究发酵过程中不同蛋白组成的花生蛋白分离物、花生素和伴生花生素对其分子结构和热学性质的影响,将花生蛋白与肌纤蛋白复配制备复合凝胶,研究复合乳液的流变学性质和复合凝胶的质构性质,揭示五味子乳杆菌对花生蛋白凝胶性质影响的分子机理。结果表明,五味子发酵增加了花生蛋白的游离巯基含量、表面疏水性和变性温度,降低了β片含量和变性焓。发酵能降低花生蛋白分离物和伴生花生蛋白的游离巯基含量、表面疏水性和变性焓,显著提高花生蛋白分离物和伴生花生蛋白的变性温度和α-螺旋含量。发酵后,花生蛋白分离物和花生素的α-螺旋含量明显增加,花生素的结构发展到最大程度,花生素的热稳定性更高,这证明五味子球菌能促进花生蛋白的凝胶改性。与花生蛋白和分离蛋白改性制备的复合凝胶相比,花生蛋白发酵形成的复合凝胶更容易形成多孔结构,宏观弹性更好。
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
CiteScore
5.80
自引率
0.00%
发文量
0
期刊最新文献
Plant proteins, insects, edible mushrooms and algae: more sustainable alternatives to conventional animal protein Effect of Lactobacillus pentosus fermentation on molecular structure and gel quality of peanut protein Characterization of a novel date energy bar fortified with Moringa oleifera leaves powder The volatile compounds changes of Malus asiatica Nakai under different drying methods Potential of umami molecules against SARS-CoV-2 (Omicron) S-RBD/hACE2 interaction: an in-silico study
×
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
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 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 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1