Directed evolution of an enantioselective lipase with broad substrate scope for hydrolysis of α-substituted esters
2010 (English)In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 132, no 20, 7038-7042 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2010. Vol. 132, no 20, 7038-7042 p.
IdentifiersURN: urn:nbn:se:su:diva-45970DOI: 10.1021/ja100593jOAI: oai:DiVA.org:su-45970DiVA: diva2:370584
FunderSwedish Research CouncilKnut and Alice Wallenberg Foundation