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- W1990667458 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." @default.
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- W1990667458 date "1998-09-01" @default.
- W1990667458 modified "2023-09-27" @default.
- W1990667458 title "Enantioselectivity of a recombinant esterase from Pseudomonas fluorescens" @default.
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- W1990667458 doi "https://doi.org/10.1016/s1381-1177(98)00034-4" @default.
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