Kaiser, Peerzada and Raina, Chand and Parshad, Rajinder and Johri, Sarojini and Verma, Vijeshwer and Andrabi, Khurshid I. and Qazi, Ghulam N. (2006) A novel esterase from Bacillus subtilis (RRL 1789): Purification and characterization of the enzyme. Protein Expression and Purification, 45 (2). pp. 262-268. ISSN 10465928

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An esterase (EC produced by an isolated strain of Bacillus subtilis RRL 1789 exhibited moderate to high enantioselectivity in the kinetic resolution of several substrates like aryl carbinols, hydroxy esters, and halo esters. The enzyme named as B. subtilis esterase(BSE), was purified to >95% purity with a specific activity of 944 U/mg protein and 12% overall yield. The purified enzyme is �52 kDa monomer, maximally activity at 37 �C and pH 8.0 and fairly stable up to 55 �C. The enzyme does not exhibit the phenomenon of interfacial activation with tributyrin and p-nitrophenyl butyrate beyond the saturation concentration. The enzyme showed preference for triacyglycerols and esters of p-nitrophenol with short chain fatty acid. Presence of Ca2+ ions increases the activity of enzyme by �20% but its presence does not have any influence on the thermostability of the enzyme. The enzyme is not a metalloprotein and belongs to the family of serine proteases. The N-terminal amino acid sequence of BSE determined, as Met-Thr-Pro-Glu-Iso-Val-Thr-Thr-Glu-Tyr-Glyrevealed similarity with the N-terminal amino acid sequence of p-nitrobenzylesterase of B. subtilis.

Item Type: Article
Subjects: Biological Sciences
Depositing User: Mr. Amit Nargotra
Date Deposited: 19 Dec 2011 07:40
Last Modified: 19 Dec 2011 07:40
URI: http://iiim.csircentral.net/id/eprint/189

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