Abstract
A recombinant esterase from Pseudomonas fluorescens (PFE) was produced from Escherichia coli cultures and purified to homogeneity resulting in a specific activity of 120 U mg −1 ( p-nitrophenyl acetate assay). PFE is stable in a wide range of pH values (5–10) and active from 30–70°C, but rather unstable at temperatures >50°C. PFE hydrolyzes a wide range of aliphatic and aromatic esters, but no long chain fatty acid esters. The enzyme showed high rate and enantioselectivity in the resolution of α-phenyl ethanol ( E > 100) and its acetate ( E = 58) while the closely related α-phenyl propanol was converted at very low rate and enantioselectivity.
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