CLONING AND EXPRESSION OF CHAETOMIUM THERMOPHILUM XYLANASE 11-A GENE IN PROKARYOTE

Authors

  • S. Wajid National Institute for Biotechnology and Genetic Engineering (NIBGE), P.O. Box 577, Faisalabad, Pakistan
  • F. Latif National Institute for Biotechnology and Genetic Engineering (NIBGE), P.O. Box 577, Faisalabad, Pakistan
  • S. Afzal National Institute for Biotechnology and Genetic Engineering (NIBGE), P.O. Box 577, Faisalabad, Pakistan
  • Z. Mukhtar National Institute for Biotechnology and Genetic Engineering (NIBGE), P.O. Box 577, Faisalabad, Pakistan
  • A. Ghaffar National Institute for Biotechnology and Genetic Engineering (NIBGE), P.O. Box 577, Faisalabad, Pakistan
  • S. Mansoor National Institute for Biotechnology and Genetic Engineering (NIBGE), P.O. Box 577, Faisalabad, Pakistan
  • I. Rajoka National Institute for Biotechnology and Genetic Engineering (NIBGE), P.O. Box 577, Faisalabad, Pakistan

Abstract

The xylanase gene was cloned into pET32a(+) and expressed in E. coli BL21 under T7 promotor alongwith fusion protein. The SDS-PAGE and western blot analysis showed a protein of ~42 kDa. The best expression of xylanase enzyme was found by using xylose as carbon source and lactose as an inducer. The maximum activity of xylanase expressed in E. coli was 6.02 U/mL in the presence of 2 % xylose in DS medium. The activity of recombinant xylanase was observed on 1 % xylan LB agar plates, showed halos of xylan clearance when lactose was used as an inducer.

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Published

01-07-2020

How to Cite

[1]
S. Wajid, “CLONING AND EXPRESSION OF CHAETOMIUM THERMOPHILUM XYLANASE 11-A GENE IN PROKARYOTE”, The Nucleus, vol. 45, no. 3-4, pp. 149–156, Jul. 2020.

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