Catalytic membrane preparation for enzymatic hydrolysis reactions carried out in the membrane phase contactor

Two concepts of the localisation of hydrolytic enzymes with the use of a membrane phase contactor are presented in the paper. Because of the participation of water molecules in the process, the enzyme should be immobilized so that it could be in contact with the aqueous phase. Thus, enzyme immobilisation on the hydrophobic membrane surface and in the hydrophilic membrane pores was considered. The lipase from Candida antarctica and from pancreatic porcine were selected for experiments. Both enzymes were adsorbed on the polypropylene membrane surface, packed in the pores of nitrocellulose and cellulose membranes and bound within the pores of the polyamide membrane after its activation with glutaraldehyde. On the basis of the amount of immobilized protein, enzyme activity and stability, the most appropriate preparation of each immobilized lipase was chosen having on mind its further application in the biphase organic solvent–water system.

The authors present the characteristics of preparations that contain lipase from Candida antarctica and from pancreatic porcine immobilized on membranes. These lipases differ greatly from each other in their structure and properties, but both of them hydrolyse fats and esters, such as glycidyl butyrate. Taking into account water as a substrate and further application of these preparations in biphase systems, immobilisation of the enzymes was performed on the surface of the hydrophobic membrane and inside the pores of the hydrophilic membrane so that biocatalysts were in a direct contact with the aqueous phase.