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Lipases in the native or immobilized form have commonly been used as catalysts
in the chemical and pharmaceutical industry. One of the widely available enzyme
catalysts on the market is lipase from Burkholderia cepacia (BCLs), previously called
Pseudomonas cepacia (PCLs). This enzyme is applied, among others, in the stereoselective
acylation of molecules to achieve chiral pure enantiomers of drugs or their building
blocks. In this study, Amano lipase PS (APS-BCL), which is a commercial lipase from
Burkholderia cepacia (BC) was tested. The lipolytic activity of APS-BCL by hydrolysis
of vegetable oils and enantioselective activity of APS-BCL by the kinetic resolution of
(R,S)-1-phenylethanol with using isopropenyl acetate as an acyl donor were evaluated. An
effect of reaction media with different logP values (t-butyl methyl ether, dichloromethane,
diisopropyl ether, toluene, cyclohexane, n-hexane, isooctane and n-heptane) on the enantioselective activity of
lipase was also studied. The high value of the enantiomeric ratio (E =308.5) with the utilization of isopropenyl
acetate was achieved. Whereas, the best reaction medium turned out to be diisopropyl ether, C =47.9%, eep
=98%, ees =90%, after 24 h of incubation. Moreover, the influence of ω6/ω9 polyunsaturated fatty acids (PUFAs)
ratio in commercial (peanut, camelina, rape, pumpkin seed, walnut, sesame, avocado, rice, corn, black
cumin, hemp, safflower, grape seed) oils was investigated for the lipase activity. For the first time, the cut-off
limit of ω6/ω9 ratio was proposed. The ratio equal to or higher than 2.3 allows achieving higher lipolytic activity.
Kinetic Resolution of Enantiomers in Racemic and Enantiomerically Enriched 2-Alkanols by Pseudomonas cepacia Lipase Catalyzed Transesterification with Isopropenyl Acetate in Organic Solvent
