Protein & Peptide Letters

Prof. Ben M. Dunn  
Department of Biochemistry and Molecular Biology
University of Florida
College of Medicine
P.O. Box 100245
Gainesville, FL


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

Author(s): Abdul Ghaffar, Sher Afzal Khan, Zahid Mukhtar, Farooq Latif and Muhammad Ibrahim Rajoka

Affiliation: National Institute for Biotechnology and Genetic Engineering, (NIBGE), P.O. Box 577, Jhang Road, Faisalabad, Pakistan.


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.

Keywords: Amplification, expression, E. coli, fungal xylanase, gene cloning, kinetics, characterization

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Article Details

Page: [356 - 362]
Pages: 7
DOI: 10.2174/092986609787848126