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• W2037900140 startingPage "7038" @default.
• W2037900140 abstract "A variant of Candida antarctica lipase A (CalA) was developed for the hydrolysis of α-substituted p-nitrophenyl esters by directed evolution. The E values of this variant for 7 different esters was 45−276, which is a large improvement compared to 2−20 for the wild type. The broad substrate scope of this enzyme variant is of synthetic use, and hydrolysis of the tested substrates proceeded with an enantiomeric excess between 95−99%. A 30-fold increase in activity was also observed for most substrates. The developed enzyme variant shows (R)-selectivity, which is reversed compared to the wild type that is (S)-selective for most substrates." @default.
• W2037900140 created "2016-06-24" @default.
• W2037900140 creator A5014896436 @default.
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• W2037900140 creator A5076473366 @default.
• W2037900140 date "2010-05-07" @default.
• W2037900140 modified "2023-10-07" @default.
• W2037900140 title "Directed Evolution of an Enantioselective Lipase with Broad Substrate Scope for Hydrolysis of α-Substituted Esters" @default.
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• W2037900140 doi "https://doi.org/10.1021/ja100593j" @default.
• W2037900140 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20450151" @default.
• W2037900140 hasPublicationYear "2010" @default.
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