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• W2055615058 abstract "A highly enantioselective l-menthyl acetate esterase was purified to homogeneity from Burkholderia cepacia ATCC 25416, with a recovery of 4.8% and a fold purification of 22.7. The molecular weight of the esterase was found to be 37 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The N-terminal amino acid sequence was “MGARTDA”, and there was no homology in contrast to other Burkholderia sp. esterases. This enzyme preferentially hydrolyzed short-chain fatty acid esters of menthol with high stereospecificity and high hydrolytic activity, while long-chain l-menthyl esters were poor substrates. Considered its substrate specificity and N-terminal sequence, this esterase was concluded as a new enzyme belonging to the carboxylesterase group (EC 3.1.1.1) of esterase family. The optimum temperature and pH for enzyme activity using racemic menthyl acetate as substrate were 30 °C and 7.0, respectively. The esterase was more stable in the pH range of 7.0–9.0 and temperature range of 30–40 °C. Hydrolytic activity was enhanced by Ca2+, K+ and Mg2+, but completely inhibited by Hg2+, Cu2+, ionic detergents and phenylmethylsulfonyl fluoride (PMSF) at 0.01 M concentration." @default.
• W2055615058 created "2016-06-24" @default.
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• W2055615058 date "2009-05-01" @default.
• W2055615058 modified "2023-09-24" @default.
• W2055615058 title "Purification and properties of a highly enantioselective l-menthyl acetate hydrolase from Burkholderia cepacia" @default.
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• W2055615058 doi "https://doi.org/10.1016/j.molcatb.2008.06.011" @default.
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