tgase诱导的桑叶蛋白颗粒作为高内相皮克林乳状液稳定剂的交联:表征和稳定性。

IF 3.3 2区 农林科学 Q1 AGRICULTURE, MULTIDISCIPLINARY
Mingze Zhi, Yingshan Xie, Hongyan Li, Zeyuan Deng, Han Peng, Yanfang Yu, Bing Zhang
{"title":"tgase诱导的桑叶蛋白颗粒作为高内相皮克林乳状液稳定剂的交联:表征和稳定性。","authors":"Mingze Zhi,&nbsp;Yingshan Xie,&nbsp;Hongyan Li,&nbsp;Zeyuan Deng,&nbsp;Han Peng,&nbsp;Yanfang Yu,&nbsp;Bing Zhang","doi":"10.1002/jsfa.14196","DOIUrl":null,"url":null,"abstract":"<div>\n \n \n <section>\n \n <h3> BACKGROUND</h3>\n \n <p>Mulberry leaf protein (MLP) is a high-quality protein with significant nutritional value and functional properties. Enzymatic modification of proteins can enhance their functional properties by using proteases to covalently crosslink or hydrolyze proteins. This study investigates the potential of transglutaminase (TGase)-induced crosslinked MLP as an emulsifier in the formation of high-internal-phase Pickering emulsions.</p>\n </section>\n \n <section>\n \n <h3> RESULTS</h3>\n \n <p>Crosslinked MLP samples were prepared with TGase concentrations ranging from 0 to 25 U g<sup>−1</sup>. High-internal-phase Pickering emulsions (80% v/v) were formed at pH 8, with a crosslinking temperature of 50 °C, a TGase concentration of 20 U g<sup>−1</sup> and an optimal crosslinking time of 60 min. As the enzyme concentration increased, the content of exposed sulfhydryl groups progressively increased, while the total free sulfhydryl content remained relatively stable. After varying crosslinking durations, both total free and exposed sulfhydryl group contents initially increased before declining. Additionally, the content of free amino groups in MLP gradually decreased with higher enzyme dosages and longer crosslinking times. The surface hydrophobicity of crosslinked MLP increased initially, followed by a decrease, reflecting changes in the spatial structure of MLP. SDS-PAGE analysis confirmed the formation of polymer masses after TGase-catalyzed crosslinking. Under optimal crosslinking conditions, the high-internal-phase Pickering emulsion prepared with TGase-induced crosslinked MLP exhibited a relatively uniform droplet distribution.</p>\n </section>\n \n <section>\n \n <h3> CONCLUSION</h3>\n \n <p>TGase-induced crosslinking enhances both the emulsifying activity and stability of MLP emulsions. © 2025 Society of Chemical Industry.</p>\n </section>\n </div>","PeriodicalId":17725,"journal":{"name":"Journal of the Science of Food and Agriculture","volume":"105 8","pages":"4388-4399"},"PeriodicalIF":3.3000,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"TGase-induced crosslinking of mulberry leaf protein particles as stabilizer of high-internal-phase Pickering emulsions: characterization and stability\",\"authors\":\"Mingze Zhi,&nbsp;Yingshan Xie,&nbsp;Hongyan Li,&nbsp;Zeyuan Deng,&nbsp;Han Peng,&nbsp;Yanfang Yu,&nbsp;Bing Zhang\",\"doi\":\"10.1002/jsfa.14196\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div>\\n \\n \\n <section>\\n \\n <h3> BACKGROUND</h3>\\n \\n <p>Mulberry leaf protein (MLP) is a high-quality protein with significant nutritional value and functional properties. Enzymatic modification of proteins can enhance their functional properties by using proteases to covalently crosslink or hydrolyze proteins. This study investigates the potential of transglutaminase (TGase)-induced crosslinked MLP as an emulsifier in the formation of high-internal-phase Pickering emulsions.</p>\\n </section>\\n \\n <section>\\n \\n <h3> RESULTS</h3>\\n \\n <p>Crosslinked MLP samples were prepared with TGase concentrations ranging from 0 to 25 U g<sup>−1</sup>. High-internal-phase Pickering emulsions (80% v/v) were formed at pH 8, with a crosslinking temperature of 50 °C, a TGase concentration of 20 U g<sup>−1</sup> and an optimal crosslinking time of 60 min. As the enzyme concentration increased, the content of exposed sulfhydryl groups progressively increased, while the total free sulfhydryl content remained relatively stable. After varying crosslinking durations, both total free and exposed sulfhydryl group contents initially increased before declining. Additionally, the content of free amino groups in MLP gradually decreased with higher enzyme dosages and longer crosslinking times. The surface hydrophobicity of crosslinked MLP increased initially, followed by a decrease, reflecting changes in the spatial structure of MLP. SDS-PAGE analysis confirmed the formation of polymer masses after TGase-catalyzed crosslinking. Under optimal crosslinking conditions, the high-internal-phase Pickering emulsion prepared with TGase-induced crosslinked MLP exhibited a relatively uniform droplet distribution.</p>\\n </section>\\n \\n <section>\\n \\n <h3> CONCLUSION</h3>\\n \\n <p>TGase-induced crosslinking enhances both the emulsifying activity and stability of MLP emulsions. © 2025 Society of Chemical Industry.</p>\\n </section>\\n </div>\",\"PeriodicalId\":17725,\"journal\":{\"name\":\"Journal of the Science of Food and Agriculture\",\"volume\":\"105 8\",\"pages\":\"4388-4399\"},\"PeriodicalIF\":3.3000,\"publicationDate\":\"2025-03-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of the Science of Food and Agriculture\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://onlinelibrary.wiley.com/doi/10.1002/jsfa.14196\",\"RegionNum\":2,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"AGRICULTURE, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of the Science of Food and Agriculture","FirstCategoryId":"97","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/jsfa.14196","RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"AGRICULTURE, MULTIDISCIPLINARY","Score":null,"Total":0}
引用次数: 0

摘要

背景:桑叶蛋白(MLP)是一种具有重要营养价值和功能特性的优质蛋白质。蛋白质的酶修饰可以通过利用蛋白酶共价交联或水解蛋白质来增强蛋白质的功能特性。本研究探讨了转谷氨酰胺酶(TGase)诱导的交联MLP作为乳化剂在形成高内相皮克林乳剂中的潜力。结果:制备了TGase浓度为0 ~ 25 U g-1的交联MLP样品。在pH为8、交联温度为50℃、TGase浓度为20 U g-1、最佳交联时间为60 min的条件下,制备高内相Pickering乳状液(80% v/v)。随着酶浓度的增加,暴露的巯基含量逐渐增加,而总游离巯基含量保持相对稳定。不同交联时间后,总游离和暴露巯基含量均呈先上升后下降趋势。随着酶用量的增加和交联时间的延长,MLP中游离氨基的含量逐渐降低。交联MLP的表面疏水性先升高后降低,反映了MLP空间结构的变化。SDS-PAGE分析证实了tgase催化交联后聚合物团块的形成。在最佳交联条件下,以tgase诱导交联MLP制备的高内相Pickering乳液的液滴分布相对均匀。结论:tgase诱导的交联增强了MLP乳剂的乳化活性和稳定性。©2025化学工业协会。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
TGase-induced crosslinking of mulberry leaf protein particles as stabilizer of high-internal-phase Pickering emulsions: characterization and stability

BACKGROUND

Mulberry leaf protein (MLP) is a high-quality protein with significant nutritional value and functional properties. Enzymatic modification of proteins can enhance their functional properties by using proteases to covalently crosslink or hydrolyze proteins. This study investigates the potential of transglutaminase (TGase)-induced crosslinked MLP as an emulsifier in the formation of high-internal-phase Pickering emulsions.

RESULTS

Crosslinked MLP samples were prepared with TGase concentrations ranging from 0 to 25 U g−1. High-internal-phase Pickering emulsions (80% v/v) were formed at pH 8, with a crosslinking temperature of 50 °C, a TGase concentration of 20 U g−1 and an optimal crosslinking time of 60 min. As the enzyme concentration increased, the content of exposed sulfhydryl groups progressively increased, while the total free sulfhydryl content remained relatively stable. After varying crosslinking durations, both total free and exposed sulfhydryl group contents initially increased before declining. Additionally, the content of free amino groups in MLP gradually decreased with higher enzyme dosages and longer crosslinking times. The surface hydrophobicity of crosslinked MLP increased initially, followed by a decrease, reflecting changes in the spatial structure of MLP. SDS-PAGE analysis confirmed the formation of polymer masses after TGase-catalyzed crosslinking. Under optimal crosslinking conditions, the high-internal-phase Pickering emulsion prepared with TGase-induced crosslinked MLP exhibited a relatively uniform droplet distribution.

CONCLUSION

TGase-induced crosslinking enhances both the emulsifying activity and stability of MLP emulsions. © 2025 Society of Chemical Industry.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
CiteScore
8.10
自引率
4.90%
发文量
634
审稿时长
3.1 months
期刊介绍: The Journal of the Science of Food and Agriculture publishes peer-reviewed original research, reviews, mini-reviews, perspectives and spotlights in these areas, with particular emphasis on interdisciplinary studies at the agriculture/ food interface. Published for SCI by John Wiley & Sons Ltd. SCI (Society of Chemical Industry) is a unique international forum where science meets business on independent, impartial ground. Anyone can join and current Members include consumers, business people, environmentalists, industrialists, farmers, and researchers. The Society offers a chance to share information between sectors as diverse as food and agriculture, pharmaceuticals, biotechnology, materials, chemicals, environmental science and safety. As well as organising educational events, SCI awards a number of prestigious honours and scholarships each year, publishes peer-reviewed journals, and provides Members with news from their sectors in the respected magazine, Chemistry & Industry . Originally established in London in 1881 and in New York in 1894, SCI is a registered charity with Members in over 70 countries.
×
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:481959085
Book学术官方微信