Abstract
A new esterase-producing strain (Bacillus cereus WZZ001) which exhibiting high hydrolytic activity and excellent enantioselectivity on rac-α-ethyl-2-oxo-pyrrolidineacetic acid methyl ester (R, S-1) has been isolated from soil sample by our laboratory. In this study, the stereoselective hydrolysis of (R, S-1) was performed using the recombinant Bacillus cereus esterase which expressed in Escherichia coli BL21 (DE3). Under the optimized conditions of pH 8.0, 35°C, and concentration of substrate 400mM, a successful enzymatic resolution was achieved with an e.e. s of 99.5% and conversion of 49%. Immobilization considerably increased the reusability of the recombinant esterase; the immobilized enzyme showed excellent reusability during 6cycles of repeated 2h reactions at 35°C. Thereby, it makes the recombinant B. cereus esterase a usable biocatalyst for industrial application.
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