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 30-7 0 degrees C, bur rather unstable at temperatures >50 degrees C. PFE hy drolyzes a wide range of aliphatic and aromatic esters, but no long ch ain fatty acid esters. The enzyme showed high rate and enantioselectiv ity in the resolution of alpha-phenyl ethanol (E > 100) and its acetat e (E = 58) while the closely related alpha-phenyl propanol was convert ed at very low rate and enantioselectivity. (C) 1998 Elsevier Science Inc.