Optimized expression of a thermostable xylanase 11 A gene from Chaetomium thermophilum NIBGE 1 in Escherichia coli.
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.
National Institute for Biotechnology and Genetic Engineering, (NIBGE), Jhang Road, Faisalabad, Pakistan.
Abdul
A
Ghaffar
Sher Afzal
SA
Khan
Zahid
Z
Mukhtar
Farooq
F
Latif
Muhammad Ibrahim
MI
Rajoka
D002597:Chaetomium / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D043364:Endo-1,4-beta Xylanases / Q000096:biosynthesis* / Q000378:metabolism; D004765:Enteropeptidase / Q000378:metabolism; D004795:Enzyme Stability; D004926:Escherichia coli / Q000201:enzymology; D006358:Hot Temperature; D007700:Kinetics; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D013816:Thermodynamics
D011994:Recombinant Proteins; D043364:Endo-1,4-beta Xylanases; D004765:Enteropeptidase