The influence of substrate systems on the enantioselective and lipolytic activity of immobilized Amano PS from Burkholderia cepacia lipase (APS-BCL)

Abstract

In this study, Amano lipase PS from Burkholderia cepacia (APS-BCL) was immobilized onto polyacrylic support IB-150A, which allowed to improve immobilized lipase activity in nonaqueous media compared with the free (native) form. The enantioselectivity of the immobilized APS-BCL (8 mg/mL) in the kinetic resolution of (R,S)−1-phenylethanol was evaluated. High values of catalytic parameters with isopropenyl acetate (E =775.4, C =49 % ± 0.4) and vinyl acetate (E =206.6, C = 50 % ± 0.3) as acyl donors were achieved after a reaction time of 12 h. The effects of 7 different non-aqueous solvents on catalyst enantioselectivity in the kinetic resolution of (R,S)−1−phenylethanol were also assessed. Diisopropyl ether and n-hexane were selected as the optimal reaction media. A novel lipolytic activity study of immobilized APS-BCL (7.9–9.3 mg/mL) with the application of the developed multicomponent unsaturated fatty acids (MC-UFAs) method using 13 vegetable oils in an aqueous medium has been proposed (pH =7, T =37 °C). The effect of the ratio of polyunsaturated fatty acids (PUFAs) to monounsaturated fatty acids (MUFAs) on lipase activity was demonstrated and a cut-off limit (ω6/ω9 =2.3) was determined. Hyperactivation of immobilized APS-BCL in peanut oil (Arec=104.85 %, Aret=110.19 %) as the substrate was observed.