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2000
Volume 16, Issue 4
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

The xylanase (Xyn11A) gene (883 bp) was amplified using C. thermophilum DNA as template and cloned into pET-32a (+) and expressed in E. coli BL21 under T7 promoter. The recombinant xylanase on SDS-PAGE had a molecular mass of 30 kDa. Productivity profiles of xylanase in E. coli recombinant are more than 4-fold of that produced from T. reesei RUTC-30, 5-fold of that produced by the donor and significantly higher than the values reported on other E. coli, and Saccharomyces cerevisiae recombinants. Temperature stability, pH stability, and other kinetic parameters confirmed that the gene product was thermo-stable in alkaline buffer favoring its suitability to bio-bleaching of kraft pulp.

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/content/journals/ppl/10.2174/092986609787848126
2009-04-01
2025-10-20
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/content/journals/ppl/10.2174/092986609787848126
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  • Article Type:
    Research Article
Keyword(s): Amplification; characterization; E. coli; expression; fungal xylanase; gene cloning; kinetics
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