从粘菌及其伴生菌株的微生物群中挖掘、鉴定和表征三种木聚糖酶

IF 3.8 3区化学 Q2 CHEMISTRY, PHYSICAL

Catalysts Pub Date : 2023-12-24 DOI:10.3390/catal14010015

Yanhuan Lin, Changle Li, Chenxin Wei, Hui Lin, Liaoyuan Zhang

{"title":"从粘菌及其伴生菌株的微生物群中挖掘、鉴定和表征三种木聚糖酶","authors":"Yanhuan Lin, Changle Li, Chenxin Wei, Hui Lin, Liaoyuan Zhang","doi":"10.3390/catal14010015","DOIUrl":null,"url":null,"abstract":"Microbial xylanase has wide application in bioenergy, animal feed, environmental protection, the pulp and paper industry, and agricultural development. In this study, three xylanases from the microbiota of T. fuciformis with its companion strains were identified by metagenomics sequencing. The three enzymes were subjected to cloning and expression in E. coli or P. pastoris, purification, and characterization for their properties. The results showed that AsXyn1, from Annulohypoxylon stygium, among the three enzymes possessed high thermostability at 40 °C and broad pH tolerance in the range of 2.0–10.0, exhibiting its application potential. Furthermore, it was found that post-translational modification (such as glycosylation) of AsXyn1 enzyme modulated its activity, kinetic parameters, and thermostability. These results and findings provided a hint for enzyme modification and design in future.","PeriodicalId":9794,"journal":{"name":"Catalysts","volume":"15 1","pages":""},"PeriodicalIF":3.8000,"publicationDate":"2023-12-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Mining, Identification, and Characterization of Three Xylanases from the Microbiota of T. fuciformis with Its Companion Strains\",\"authors\":\"Yanhuan Lin, Changle Li, Chenxin Wei, Hui Lin, Liaoyuan Zhang\",\"doi\":\"10.3390/catal14010015\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Microbial xylanase has wide application in bioenergy, animal feed, environmental protection, the pulp and paper industry, and agricultural development. In this study, three xylanases from the microbiota of T. fuciformis with its companion strains were identified by metagenomics sequencing. The three enzymes were subjected to cloning and expression in E. coli or P. pastoris, purification, and characterization for their properties. The results showed that AsXyn1, from Annulohypoxylon stygium, among the three enzymes possessed high thermostability at 40 °C and broad pH tolerance in the range of 2.0–10.0, exhibiting its application potential. Furthermore, it was found that post-translational modification (such as glycosylation) of AsXyn1 enzyme modulated its activity, kinetic parameters, and thermostability. These results and findings provided a hint for enzyme modification and design in future.\",\"PeriodicalId\":9794,\"journal\":{\"name\":\"Catalysts\",\"volume\":\"15 1\",\"pages\":\"\"},\"PeriodicalIF\":3.8000,\"publicationDate\":\"2023-12-24\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Catalysts\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://doi.org/10.3390/catal14010015\",\"RegionNum\":3,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"CHEMISTRY, PHYSICAL\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Catalysts","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.3390/catal14010015","RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"CHEMISTRY, PHYSICAL","Score":null,"Total":0}

引用次数: 0

摘要

微生物木聚糖酶在生物能源、动物饲料、环境保护、纸浆和造纸工业以及农业发展方面有着广泛的应用。在本研究中，通过元基因组学测序，从粘菌及其伴生菌株的微生物群中鉴定出了三种木聚糖酶。这三种酶在大肠杆菌或棒状杆菌中进行了克隆和表达、纯化，并对其特性进行了鉴定。结果表明，三种酶中，来自苯乙烯噻吩（Annulohypoxylon stygium）的AsXyn1在40 °C下具有高热稳定性，在2.0-10.0范围内具有广泛的pH耐受性，显示了其应用潜力。此外，研究还发现 AsXyn1 酶的翻译后修饰（如糖基化）调节了其活性、动力学参数和耐热性。这些结果和发现为今后的酶修饰和设计提供了提示。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

查看原文本刊更多论文

Mining, Identification, and Characterization of Three Xylanases from the Microbiota of T. fuciformis with Its Companion Strains

Microbial xylanase has wide application in bioenergy, animal feed, environmental protection, the pulp and paper industry, and agricultural development. In this study, three xylanases from the microbiota of T. fuciformis with its companion strains were identified by metagenomics sequencing. The three enzymes were subjected to cloning and expression in E. coli or P. pastoris, purification, and characterization for their properties. The results showed that AsXyn1, from Annulohypoxylon stygium, among the three enzymes possessed high thermostability at 40 °C and broad pH tolerance in the range of 2.0–10.0, exhibiting its application potential. Furthermore, it was found that post-translational modification (such as glycosylation) of AsXyn1 enzyme modulated its activity, kinetic parameters, and thermostability. These results and findings provided a hint for enzyme modification and design in future.

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

Catalysts CHEMISTRY, PHYSICAL-

CiteScore

6.80

自引率

7.70%

发文量

1330

审稿时长

3 months

期刊介绍： Catalysts (ISSN 2073-4344) is an international open access journal of catalysts and catalyzed reactions. Catalysts publishes reviews, regular research papers (articles) and short communications. Our aim is to encourage scientists to publish their experimental and theoretical results in as much detail as possible. Therefore, there is no restriction on the length of the papers. The full experimental details must be provided so that the results can be reproduced.