Onakunle, O.A., Knowles, Christopher J., 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. (doi:10.1016/S0141-0229(96)00267-0) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:18219)
The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. | |
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 |
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DOI/Identification number: | 10.1016/S0141-0229(96)00267-0 |
Uncontrolled keywords: | chiral resolution; bacterial lactonases; delta-lactones |
Subjects: |
Q Science Q Science > QR Microbiology |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | M.A. Ziai |
Date Deposited: | 17 Apr 2009 15:24 UTC |
Last Modified: | 16 Nov 2021 09:56 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/18219 (The current URI for this page, for reference purposes) |
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