Abstract
A recombinant esterase from Pseudomonas fluorescens (PFE) was produced from E. coli cultures and purified to homogeneity resulting in a specific activity of 120 U/mg ( p-nitrophenylacetate assay). PFE is stable in a wide range of pH (6–9) 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-phenylethanol ( E>100) and its acetate ( E=58), while the closely related α-phenylpropanol was converted at very low rate and enantioselectivity. 3-Phenylbutyric acid methylester was hydrolyzed at acceptable rate, but low enantioselectivity ( E=3.4–3.7), whereas 2-phenylbutyric acid ethylester was not a substrate for PFE.
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