Onakunle, O.A. and Knowles, C.J. and Bunch, A.W. (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.
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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.
|Uncontrolled keywords:||chiral resolution; bacterial lactonases; delta-lactones|
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:||17 Apr 2009 15:24|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/18219 (The current URI for this page, for reference purposes)|
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