BMB Reports
- Volume 34 Issue 6
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- Pages.509-516
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- 2001
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- 1976-670X(eISSN)
Purification and Characterisation of a Burkholderia pseudomallei Protease Expressed in Recombinant E. coli
- Ling, Jessmi M.L. (Centre for Gene Analysis and Technology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia) ;
- Nathan, Sheila (Centre for Gene Analysis and Technology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia) ;
- Hin, Lee Kok (Centre for Gene Analysis and Technology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia) ;
- Mohamed, Rahmah (Centre for Gene Analysis and Technology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia)
- Received : 2001.06.12
- Accepted : 2001.07.22
- Published : 2001.11.30
Abstract
A genomic DNA fragment that contains the gene, which codes for a novel extracellular serine protease in Burkholderia pseudomallei, was cloned by using pQE40 as a vector. It was maintained in Escherichia coli JM109. The expression of the gene(s) resulted in the production of a 52 kDa protease. The recombinant protease was purified from the culture filtrate via ammonium sulfate fractionation, gel filtration, and anion-exchange chromatography. The purified protease had an optimum pH and temperature of pH 8.9 and