{"title":"黑曲霉C3486木聚糖酶的表达及生物信息学分析","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":"{\"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}","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
摘要
木聚糖酶(E.C 3.2.1.8)是一类广泛存在的酶,可以催化木聚糖中1,4- β - d -木糖苷键的内水解。木聚糖在工业生产中有着广泛的应用。本研究分离了黑曲霉C3486的总RNA,采用RT-PCR方法获得了成熟的木聚糖酶基因。为实现隐匿表达,以pET32a(+)为表达载体,克隆基因在大肠杆菌BL21 (DE3)中表达。经IPTG诱导后,产生大量具有活性的木聚糖酶。生物信息学分析表明,该木聚糖酶含有前导肽。此外,它还具有典型的木聚糖酶保守结构域。根据网上网站的预测,木聚糖酶是一种球蛋白,其上层结构含有许多β层。
Expression of Xylanase from A.niger C3486 and Analysis by Bioinformatics
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.