Maqbool, Qurrat-ul-Ain and Johri, Sarojini and Rasool, Shafaq and Riyaz-ul-Hassan, Syed and Verma, Vijeshwar and Nargotra, Amit and Koul, Surrinder and Qazi, Ghulam N. (2006) Molecular cloning of carboxylesterase gene and biochemical characterization of encoded protein from Bacillus subtilis (RRL BB1). Journal of Biotechnology, 125 (1). pp. 1-10. ISSN 01681656

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An isolated strain of Bacillus subtilis identified by 16S rDNA sequence analysis produces an enantioselective ester hydrolase.Whole cells of B. subtilis (RRL BB1) and enzyme derived from it was capable of enantioselective hydrolysis of several racemates including drug intermediates with moderate to high enantioselectivity as already reported by us. In this communication, we describe cloning of the gene encoding the enantioselective esterase designated as estBB1. The primary structure of the enzyme determined from the nucleotide sequence indicated that esterase estBB1 has Mw ∼52 kDa and pI ∼5.2 and belongs to the family of type B carboxylesterases with 50–60% similarity at amino acid level. Alignment studies of sequences of the estBB1 and Pnb esterase 56C8 from B. subtilis showed that estBB1 has an �/� hydrolase fold with catalytic triad formed by Ser190, Glu305 and His394 at active site and Ser190 is located in the conserved motif –G–X–S–X–G–.

Item Type: Article
Subjects: Biological Sciences
Depositing User: Mr. Amit Nargotra
Date Deposited: 02 Jan 2012 10:51
Last Modified: 02 Jan 2012 10:51

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