The formation and substrate specificity of bacterial lactonases capable of enantioselective resolution of racemic lactones

Onakunle, O.A. and Knowles, Christopher J. and Bunch, Alan William (1997) The formation and substrate specificity of bacterial lactonases capable of enantioselective resolution of racemic lactones. Enzyme and Microbial Technology, 21 (4). pp. 245-251. ISSN 0141-0229. (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1016/S0141-0229(96)00267-0

Abstract

The substrate specificities of epsilon-caprolactone hydrolase from Acinetobacter NCIMB 9871 and delta-valerolactone hydrolase from Pseudomonas NCIMB 9872 were investigated. Both lactonases showed activity toward six- and seven-membered ring lactones. delta-Valerolactone hydrolase exhibited enantioselectivity in its activity. It showed a preference for the R enantiomer of delta-decanolactone and delta-nonalactone whereas epsilon-caprolactone hydrolase showed little enantioselectivity toward the lactone substrates tested The delta-valerolactone hydrolase front Pseudomonas NCIMB 9872 may be useful for the resolution of racemic lactones, and hence may serve as an alternative route to chiral lactone synthesis.

Item Type: Article
Uncontrolled keywords: chiral resolution; bacterial lactonases; delta-lactones
Subjects: Q Science
Q Science > QR Microbiology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: M.A. Ziai
Date Deposited: 17 Apr 2009 15:24
Last Modified: 28 May 2014 10:36
Resource URI: http://kar.kent.ac.uk/id/eprint/18219 (The current URI for this page, for reference purposes)
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