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°C, but rather unst...

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Bibliographic Details
Published in:Enzyme and microbial technology 1998-05, Vol.22 (7), p.641-646
Main Authors: Krebsfänger, N., Zocher, F., Altenbuchner, J., Bornscheuer, U.T.
Format: Article
Language:English
Subjects:
Aromatic compounds
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
Catalyst activity
Cell culture
Coliform bacteria
Enantioselectivity
Escherichia coli
esterase
Esters
Ethanol
Fundamental and applied biological sciences. Psychology
Hydrolysis
Miscellaneous
Mission oriented research
pH effects
Pseudomonas fluorescens
Purification
Thermal effects
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Description
Summary: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.
ISSN:0141-0229
1879-0909
DOI:10.1016/S0141-0229(98)00004-0