{"title":"Expression of Xylanase from A.niger C3486 and Analysis by Bioinformatics","authors":"Ling Lin, Lihua Liu, H. Lian, Kai Su, Shihua Wang","doi":"10.1109/WCSE.2009.177","DOIUrl":null,"url":null,"abstract":"Xylanase (E.C 3.2.1.8) is a widespread group of enzyme which can catalyze the endohydrolysis of 1,4-beta-D-xylosidic linkages in xylan. Xylanse has a wide application in industrial processes. In this study, the total RNA was isolated, the mature xylanase gene was obtained from Aspergillus niger C3486 by RT-PCR. To achieve secretive expression, pET32a (+) was used as expression vector, and the cloned gene was expressed in E. coli BL21 (DE3). After induction by IPTG, a large quantity of xylanase was produced with xylanase activity. With the analysis of bioinformatics, this xylanase contains a preceding peptide. Moreover, it has a typical conserve domain of xylanase. Perdicted by web site on line, the xylanase is globulin, and its super structure contains many beta sheets.","PeriodicalId":331155,"journal":{"name":"2009 WRI World Congress on Software Engineering","volume":"1 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2009-05-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"2009 WRI World Congress on Software Engineering","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1109/WCSE.2009.177","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 1
Abstract
Xylanase (E.C 3.2.1.8) is a widespread group of enzyme which can catalyze the endohydrolysis of 1,4-beta-D-xylosidic linkages in xylan. Xylanse has a wide application in industrial processes. In this study, the total RNA was isolated, the mature xylanase gene was obtained from Aspergillus niger C3486 by RT-PCR. To achieve secretive expression, pET32a (+) was used as expression vector, and the cloned gene was expressed in E. coli BL21 (DE3). After induction by IPTG, a large quantity of xylanase was produced with xylanase activity. With the analysis of bioinformatics, this xylanase contains a preceding peptide. Moreover, it has a typical conserve domain of xylanase. Perdicted by web site on line, the xylanase is globulin, and its super structure contains many beta sheets.
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