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

被引：3
作者：
Ghaffar, Abdul [1 ,2 ]
Khan, Sher Afzal [1 ]
Mukhtar, Zahid [1 ]
Latif, Farooq [1 ]
Rajoka, Muhammad Ibrahim [1 ]
机构：
[1] NIBGE, Faisalabad, Pakistan
[2] Univ Agr Faisalabad, Dept Chem Biochem, Faisalabad, Pakistan
来源：
PROTEIN AND PEPTIDE LETTERS | 2009年 / 16卷 / 04期
关键词：
Amplification; expression; E; coli; fungal xylanase; gene cloning; kinetics; characterization; TRICHODERMA-REESEI; SACCHAROMYCES-CEREVISIAE; FUNGAL HOSTS; CLONING; MICROORGANISMS; PROTEINS; ENZYMES; BINDING; XYN2;
D O I：
10.2174/092986609787848126
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：356 / 362
页数：7
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