Food utility potential of protease obtained from insect-commensal Bacillus subtilis AU-2.

IF 3.3 2区 农林科学 Q1 AGRICULTURE, MULTIDISCIPLINARY
Santosh D Raut, Vipul A Bharuka, Aniketa R Patel, Ulhas K Patil
{"title":"Food utility potential of protease obtained from insect-commensal Bacillus subtilis AU-2.","authors":"Santosh D Raut, Vipul A Bharuka, Aniketa R Patel, Ulhas K Patil","doi":"10.1002/jsfa.14089","DOIUrl":null,"url":null,"abstract":"<p><strong>Background: </strong>Bacillus subtilis AU-2, isolated from the gut of Tribolium castaneum, was used for protease production. The purified protease was evaluated for its potential in food-related applications including meat tenderization, milk coagulation, and the preparation of enzymatic soybean hydrolysates. Enzymatic hydrolysis of soy protein is an effective method for producing protein hydrolysates with optimal techno-functional properties.</p><p><strong>Results: </strong>This study confirmed that B. subtilis AU-2 is a commensal with T. castaneum, within the insect gut flora. The purified protease obtained from B. subtilis AU-2 exhibited meat tenderization activity and an ability to promote milk coagulation within a 20 min timeframe. Soybean hydrolysate prepared using the protease exhibited a relatively higher degree of hydrolysis (20.1%) than pepsin, trypsin, and papain. The sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) peptide fragmentation pattern of the enzymatically prepared soy protein hydrolysate revealed the disappearance of ~35 kDa protein bands after 4 h protease treatment. The prepared soy protein hydrolysate showed improved emulsifying capacity (EC) (705 mL g<sup>-1</sup>) and exhibited significant 2,2-diphenyl-1-picrylhydrazyl (DPPH) antioxidant activity (77.89%) and hydroxyl (OH) radical scavenging activity (97.23%).</p><p><strong>Conclusions: </strong>The protease obtained from the newly isolated B. subtilis AU-2 strain exhibited potential for food-related applications, including meat tenderization, milk clotting, and soybean hydrolysate preparation. Its accessibility opens avenues for utilization in the food processing industry. © 2024 Society of Chemical Industry.</p>","PeriodicalId":17725,"journal":{"name":"Journal of the Science of Food and Agriculture","volume":" ","pages":""},"PeriodicalIF":3.3000,"publicationDate":"2024-12-23","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://doi.org/10.1002/jsfa.14089","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

Abstract

Background: Bacillus subtilis AU-2, isolated from the gut of Tribolium castaneum, was used for protease production. The purified protease was evaluated for its potential in food-related applications including meat tenderization, milk coagulation, and the preparation of enzymatic soybean hydrolysates. Enzymatic hydrolysis of soy protein is an effective method for producing protein hydrolysates with optimal techno-functional properties.

Results: This study confirmed that B. subtilis AU-2 is a commensal with T. castaneum, within the insect gut flora. The purified protease obtained from B. subtilis AU-2 exhibited meat tenderization activity and an ability to promote milk coagulation within a 20 min timeframe. Soybean hydrolysate prepared using the protease exhibited a relatively higher degree of hydrolysis (20.1%) than pepsin, trypsin, and papain. The sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) peptide fragmentation pattern of the enzymatically prepared soy protein hydrolysate revealed the disappearance of ~35 kDa protein bands after 4 h protease treatment. The prepared soy protein hydrolysate showed improved emulsifying capacity (EC) (705 mL g-1) and exhibited significant 2,2-diphenyl-1-picrylhydrazyl (DPPH) antioxidant activity (77.89%) and hydroxyl (OH) radical scavenging activity (97.23%).

Conclusions: The protease obtained from the newly isolated B. subtilis AU-2 strain exhibited potential for food-related applications, including meat tenderization, milk clotting, and soybean hydrolysate preparation. Its accessibility opens avenues for utilization in the food processing industry. © 2024 Society of Chemical Industry.

求助全文
约1分钟内获得全文 求助全文
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