Preliminary study on the correlation between enzyme activity assays and substrate preferences of microbial transglutaminase

IF 3.3 3区农林科学 Q2 FOOD SCIENCE & TECHNOLOGY

International Journal of Food Science & Technology Pub Date : 2025-01-01 DOI:10.1093/ijfood/vvae100

Xinyue Zheng, Wenjie Luo, Mingfeng Wang, Xing Chen, Jing Liu, Lei Wang, Wei Zhang, Weiyao Hu, Gaofeng Dong, Hongyang Pan, Zhaojun Wang, Qiuming Chen

{"title":"Preliminary study on the correlation between enzyme activity assays and substrate preferences of microbial transglutaminase","authors":"Xinyue Zheng, Wenjie Luo, Mingfeng Wang, Xing Chen, Jing Liu, Lei Wang, Wei Zhang, Weiyao Hu, Gaofeng Dong, Hongyang Pan, Zhaojun Wang, Qiuming Chen","doi":"10.1093/ijfood/vvae100","DOIUrl":null,"url":null,"abstract":"Abstract Transglutaminase (TGase) derived from microorganisms, known for its exceptional protein cross-linking properties, holds significant application potential across various fields. In order to meet market demands such as temperature preferences, catalytic capabilities, selectivity, and the exploration of novel TGases, challenges have arisen for the development of TGases. In this study, we conducted enzymatic activity assays on TGases from Shouchella clausii (strain KSM-K16) (Alkalihalobacillus clausii) and Couchioplanes caeruleus, randomly selected from the TrEMBL database in UniProt. We also simulated the reaction process of these assays and provided interpretations of the results. Subsequently, we examined their cross-linking abilities with protein substrates bovine serum albumin (BSA) and soy protein isolate. By validating with commercial TGase, we identified the correlation between the two commonly used enzymatic activity assay methods for TGase and the substrate preference of TGase. This correlation will aid in the specific modification of TGase.","PeriodicalId":181,"journal":{"name":"International Journal of Food Science & Technology","volume":"60 1","pages":""},"PeriodicalIF":3.3000,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://academic.oup.com/ijfst/advance-article-pdf/doi/10.1093/ijfood/vvae100/61353927/vvae100.pdf","citationCount":"1","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Journal of Food Science & Technology","FirstCategoryId":"0","ListUrlMain":"https://doi.org/10.1093/ijfood/vvae100","RegionNum":3,"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: 1

Abstract

Abstract Transglutaminase (TGase) derived from microorganisms, known for its exceptional protein cross-linking properties, holds significant application potential across various fields. In order to meet market demands such as temperature preferences, catalytic capabilities, selectivity, and the exploration of novel TGases, challenges have arisen for the development of TGases. In this study, we conducted enzymatic activity assays on TGases from Shouchella clausii (strain KSM-K16) (Alkalihalobacillus clausii) and Couchioplanes caeruleus, randomly selected from the TrEMBL database in UniProt. We also simulated the reaction process of these assays and provided interpretations of the results. Subsequently, we examined their cross-linking abilities with protein substrates bovine serum albumin (BSA) and soy protein isolate. By validating with commercial TGase, we identified the correlation between the two commonly used enzymatic activity assay methods for TGase and the substrate preference of TGase. This correlation will aid in the specific modification of TGase.

查看原文本刊更多论文

微生物转谷氨酰胺酶活性测定与底物偏好相关性的初步研究

谷氨酰胺转胺酶（TGase）源于微生物，以其独特的蛋白质交联特性而闻名，在各个领域具有重要的应用潜力。为了满足市场对温度偏好、催化能力、选择性和新型tgase的探索等方面的需求，对tgase的开发提出了挑战。在这项研究中，我们从UniProt的TrEMBL数据库中随机选择克劳绥碱性杆菌（KSM-K16）和克劳绥碱性杆菌（Couchioplanes caeruleus）的tgase进行酶活性测定。我们还模拟了这些实验的反应过程，并对结果进行了解释。随后，我们检测了它们与蛋白质底物牛血清白蛋白（BSA）和大豆分离蛋白的交联能力。通过商用TGase验证，我们确定了两种常用的TGase酶活性测定方法与TGase底物偏好之间的相关性。这种相关性将有助于TGase的特异性修饰。

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

International Journal of Food Science & Technology 工程技术-食品科技

CiteScore

5.80

自引率

9.10%

发文量

655

审稿时长

2.9 months

期刊介绍： The International Journal of Food Science & Technology (IJFST) is published for the Institute of Food Science and Technology, the IFST. This authoritative and well-established journal publishes in a wide range of subjects, ranging from pure research in the various sciences associated with food to practical experiments designed to improve technical processes. Subjects covered range from raw material composition to consumer acceptance, from physical properties to food engineering practices, and from quality assurance and safety to storage, distribution, marketing and use. While the main aim of the Journal is to provide a forum for papers describing the results of original research, review articles are also welcomed.