Enzyme and Microbial Technology, Vol.22, No.7, 641-646, 1998
Characterization and enantioselectivity of a recombinant esterase from Pseudomonas fluorescens
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 degrees C, bur rather unstable at temperatures >50 degrees 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 alpha-phenyl ethanol (E > 100) and its acetate (E = 58) while the closely related alpha-phenyl propanol was converted at very low rate and enantioselectivity.