title: Investigation of the impact of water on the enantioselectivity displayed by CALB in the kinetic resolution of δ-functionalized alkan-2-ol derivatives.
abstract: It is shown that the low enantioselectivity of Candida antarctica lipase B (CALB)-catalyzed transesterification of a δ-functionalized alkan-2-ol to its acetate does not correlate at all with the high enantioselectivity of the CALB-catalyzed hydrolysis of the corresponding acetate in water. This lack of correlation is unusual and for unfunctionalized alkan-2-ol derivatives there is a very good correlation between the enantioselectivity of transesterification of the alcohol and hydrolysis of the corresponding acetate (E>200 in both cases). The results confirm previous predictions from molecular modeling. The water effect was mimicked by CALB variant Ala281Ser, which showed an enhanced enantioselectivity in transesterification of δ-functionalized alkan-2-ols compared to wild-type CALB.
authors.affiliation: Department of Organic Chemistry, Arrhenius Laboratory Stockholm University, 106 91 Stockholm (Sweden).
authors.forename: Bin
authors.initials: B
authors.lastname: Yang
authors.forename: Richard
authors.initials: R
authors.lastname: Lihammar
authors.forename: Jan-E
authors.initials: JE
authors.lastname: Bäckvall
mesh_terms: D000085:Acetates / Q000378:metabolism; D002175:Candida / Q000201:enzymology* / Q000378:metabolism; D005233:Fatty Alcohols / Q000378:metabolism; D005656:Fungal Proteins / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D013237:Stereoisomerism; D013379:Substrate Specificity; D014867:Water / Q000378:metabolism*
chemical_list: D000085:Acetates; D005233:Fatty Alcohols; D005656:Fungal Proteins; D014867:Water; D008049:Lipase; C431349:lipase B, Candida antarctica
keywords: CALB; enantioselectivity; hydrolysis; lipase; transesterification