• DocumentCode
    2306514
  • Title

    Expression of Xylanase from A.niger C3486 and Analysis by Bioinformatics

  • Author

    Lin, Ling ; Liu, Lihua ; Lian, Huixiang ; Su, Kai ; Wang, Shihua

  • Author_Institution
    Key Lab. of Biopeticide & Chem. Biol., Fujian Agric. & Forestry Univ., Fuzhou, China
  • Volume
    2
  • fYear
    2009
  • fDate
    19-21 May 2009
  • Firstpage
    313
  • Lastpage
    317
  • 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. Xylanase 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. Predicted by Web site online, the xylanase is globulin, and its super structure contains many beta-sheets.
  • Keywords
    Web sites; bioinformatics; macromolecules; organic compounds; A.niger C3486; Aspergillus niger C3486; E. coli BL21; RNA; Web site; bioinformatics; endohydrolysis; pET32a; xylanase gene; Biochemical analysis; Biochemistry; Bioinformatics; Bleaching; Capacitive sensors; Cloning; Couplings; DNA; RNA; Software engineering; Aspergillus niger C3486; bioinformatics; clone; expression; xylanases;
  • fLanguage
    English
  • Publisher
    ieee
  • Conference_Titel
    Software Engineering, 2009. WCSE '09. WRI World Congress on
  • Conference_Location
    Xiamen
  • Print_ISBN
    978-0-7695-3570-8
  • Type

    conf

  • DOI
    10.1109/WCSE.2009.177
  • Filename
    5319658