The study on efficient hydrolases immobilization for the kinetic resolution of the α-acetoxyamides

Using different immobilization protocols, the lipases from Pseudomonas cepacia (PCL) and porcine pancreas (PPL) were immobilised. The catalytic behaviour of the biocatalysts used in the hydrolytic resolution of the target compounds, viz., acetic acid phenyl(3,4,5-trimethoxybenzylcarbamoyl)methyl ester (3a) and acetic acid (3,4,5-trimethoxy benzylcarbamoyl)(3,4,5-trimethoxyphenyl)methyl ester (3b), in an aqueous environment, was investigated. The native lipases from P. cepacia (PCL) and porcine pancreas (PPL) showed low enantioselectivity (E = 5.1 and 3.5, respectively). Upon immobilization into a sol–gel matrix, the enantioselectivity of PCL improved significantly (from E = 5.1 up to 30.5). The covalent immobilization on Eupergit® substantially increased the enzymatic activity as well as the enantioselectivity of PCL (E = 34.0).