Mas, G; Heiss, A; Benaim, RI; Duleba, J; Siodmiak, T; Marszall, MP
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 stereoselec-tive 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 Tomasz Siódeffect 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 Ï6/Ï9 polyunsaturated fatty acids (PU-FAs) 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 Ï6/Ï9 ratio was proposed. The ratio equal to or higher than 2.3 allows achieving higher lipolytic activ-ity. lipase. © 2020 Bentham Science Publishers.