Optimized Expression of a Thermostable Xylanase 11 A Gene from Chaetomium thermophilum NIBGE 1 in Escherichia coli

作者：Ghaffar Abdul; Khan Sher Afzal; Mukhtar Zahid; Latif Farooq; Rajoka Muhammad Ibrahim^*

来源：Protein and Peptide Letters, 2009, 16(4): 356-362.

DOI：10.2174/092986609787848126

• Amplification
• expression
• E. coli
• fungal xylanase
• gene cloning
• kinetics
• characterization

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 T-7 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.

• 出版日期2009-4