A Novel Highly Thermostable Multifunctional Beta-Glycosidase from Crenarchaeon Acidilobus saccharovorans

IF 2.3 4区生物学 Q3 MICROBIOLOGY

Archaea-An International Microbiological Journal Pub Date : 2015-10-11 DOI:10.1155/2015/978632

V. Gumerov, A. Rakitin, A. Mardanov, N. Ravin

{"title":"A Novel Highly Thermostable Multifunctional Beta-Glycosidase from Crenarchaeon Acidilobus saccharovorans","authors":"V. Gumerov, A. Rakitin, A. Mardanov, N. Ravin","doi":"10.1155/2015/978632","DOIUrl":null,"url":null,"abstract":"We expressed a putative β-galactosidase Asac_1390 from hyperthermophilic crenarchaeon Acidilobus saccharovorans in Escherichia coli and purified the recombinant enzyme. Asac_1390 is composed of 490 amino acid residues and showed high sequence similarity to family 1 glycoside hydrolases from various thermophilic Crenarchaeota. The maximum activity was observed at pH 6.0 and 93°C. The half-life of the enzyme at 90°C was about 7 hours. Asac_1390 displayed high tolerance to glucose and exhibits hydrolytic activity towards cellobiose and various aryl glucosides. The hydrolytic activity with p-nitrophenyl (pNP) substrates followed the order pNP-β-D-galactopyranoside (328 U mg−1), pNP-β-D-glucopyranoside (246 U mg−1), pNP-β-D-xylopyranoside (72 U mg−1), and pNP-β-D-mannopyranoside (28 U mg−1). Thus the enzyme was actually a multifunctional β-glycosidase. Therefore, the utilization of Asac_1390 may contribute to facilitating the efficient degradation of lignocellulosic biomass and help enhance bioconversion processes.","PeriodicalId":49105,"journal":{"name":"Archaea-An International Microbiological Journal","volume":"2015 1","pages":""},"PeriodicalIF":2.3000,"publicationDate":"2015-10-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2015/978632","citationCount":"15","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Archaea-An International Microbiological Journal","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1155/2015/978632","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"MICROBIOLOGY","Score":null,"Total":0}

引用次数: 15

Abstract

We expressed a putative β-galactosidase Asac_1390 from hyperthermophilic crenarchaeon Acidilobus saccharovorans in Escherichia coli and purified the recombinant enzyme. Asac_1390 is composed of 490 amino acid residues and showed high sequence similarity to family 1 glycoside hydrolases from various thermophilic Crenarchaeota. The maximum activity was observed at pH 6.0 and 93°C. The half-life of the enzyme at 90°C was about 7 hours. Asac_1390 displayed high tolerance to glucose and exhibits hydrolytic activity towards cellobiose and various aryl glucosides. The hydrolytic activity with p-nitrophenyl (pNP) substrates followed the order pNP-β-D-galactopyranoside (328 U mg−1), pNP-β-D-glucopyranoside (246 U mg−1), pNP-β-D-xylopyranoside (72 U mg−1), and pNP-β-D-mannopyranoside (28 U mg−1). Thus the enzyme was actually a multifunctional β-glycosidase. Therefore, the utilization of Asac_1390 may contribute to facilitating the efficient degradation of lignocellulosic biomass and help enhance bioconversion processes.

查看原文本刊更多论文

一种新型高耐热性多功能β -糖苷酶

我们在大肠杆菌中表达了一种推测的β-半乳糖苷酶Asac_1390，并纯化了重组酶。Asac_1390由490个氨基酸残基组成，与各种嗜热绿藻的1家族糖苷水解酶具有高度的序列相似性。在pH 6.0和93°C条件下活性最高。酶在90℃下的半衰期约为7小时。Asac_1390对葡萄糖具有较高的耐受性，对纤维素二糖和各种芳基糖苷具有水解活性。对硝基苯基(pNP)底物的水解活性依次为:pNP-β- d -半乳糖苷(328 U mg−1)、pNP-β- d -葡萄糖吡喃苷(246 U mg−1)、pNP-β- d -木吡喃苷(72 U mg−1)和pNP-β- d -甘露吡喃苷(28 U mg−1)。因此，该酶实际上是一种多功能β-糖苷酶。因此，利用Asac_1390可能有助于促进木质纤维素生物质的有效降解，并有助于提高生物转化过程。

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

Archaea-An International Microbiological Journal MICROBIOLOGY-

CiteScore

7.50

自引率

0.00%

发文量

审稿时长

>12 weeks

期刊介绍： Archaea is a peer-reviewed, Open Access journal that publishes original research articles as well as review articles dealing with all aspects of archaea, including environmental adaptation, enzymology, genetics and genomics, metabolism, molecular biology, molecular ecology, phylogeny, and ultrastructure. Bioinformatics studies and biotechnological implications of archaea will be considered. Published since 2002, Archaea provides a unique venue for exchanging information about these extraordinary prokaryotes.