Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 132, Issue 20, Pages 7038-7042Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja100593j
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Funding
- Swedish Research Council
- Swedish Foundation for Strategic Research
- K&A Wallenberg Foundation
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A variant of Candida antarctica lipase A (CalA) was developed for the hydrolysis of a-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.
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