Enantioselectivity of a recombinant esterase from Pseudomonas fluorescens towards alcohols and carboxylic acids.
A recombinant esterase from Pseudomonas fluorescens (PFE) was produced from E. coli cultures and the enantioselectivity towards a series of racemic substrates was investigated. PFE exhibited high rate and enantioselectivity in the acylation of alpha-phenyl ethanol with vinyl acetate in toluene (E > 100) and the hydrolysis of the corresponding acetate in phosphate buffer (E = 58). In sharp contrast, extremely low enantioselectivity (E from 1.1 to 7) was found for the acylation of a series of 1,2-O-protected glycerol derivatives and the hydrolysis of 3-phenylbutyric acid methylester. Almost no reaction occurred with alpha-phenyl propanol and its acetate and 2-phenylbutyric acid ethylester.
Krebsfänger
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Universität Stuttgart, Institut für Technische Biochemie, Germany.
Schierholz
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Bornscheuer
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UT
D000433:1-Propanol / Q000737:chemistry / Q000378:metabolism; D000085:Acetates / Q000378:metabolism; D000215:Acylation; D000438:Alcohols / Q000378:metabolism*; D002087:Butyrates / Q000737:chemistry / Q000378:metabolism; D020148:Butyric Acid; D002264:Carboxylic Acids / Q000378:metabolism*; D004926:Escherichia coli; D004950:Esterases / Q000235:genetics / Q000378:metabolism*; D000431:Ethanol / Q000737:chemistry / Q000378:metabolism; D005990:Glycerol / Q000737:chemistry / Q000378:metabolism; D006868:Hydrolysis; D010957:Plasmids / Q000235:genetics; D011551:Pseudomonas fluorescens / Q000201:enzymology*; D011994:Recombinant Proteins / Q000378:metabolism; D015183:Restriction Mapping; D013237:Stereoisomerism; D013379:Substrate Specificity; D014753:Vinyl Compounds / Q000737:chemistry
D000085:Acetates; D000438:Alcohols; D002087:Butyrates; D002264:Carboxylic Acids; D011994:Recombinant Proteins; D014753:Vinyl Compounds; D020148:Butyric Acid; D000431:Ethanol; D000433:1-Propanol; D004950:Esterases; C011566:vinyl acetate; D005990:Glycerol