POLYMERIC SUPPORTS FOR ENZYMES IMMOBILIZATION IN SYNTHESIS OF BIOLOGICALLY ACTIVE COMPOUNDS

Abstract

The report presents the synthesis of biocatalysts based on horseradish peroxidase immobilized on commercially available polymeric supports: hyper cross-linked polystyrene MN-100 and Sepabeads EC-HA. The immobilization was carried out by covalent crosslinking of the enzyme with the support using glutaraldehyde. The optimal amount of glutaraldehyde for covalent binding of HRP was found to be 0.2 g/l. The peroxidase/MN-100 and peroxidase/Sepabeads EC-HA biocatalysts presented in the work showed good activity in the oxidation of 2-methylnaphthol to 2 methyl-1,4-naphthohydroquinone (vitamin K4). The biocatalyst based on MN-100 showed higher activity compared to the biocatalyst based on Sepabeads EC-HA, which is likely due to the different surface structure of the original polymer supports. The samples retained their activity in ten consecutive reuses. The high reusability of peroxidase/MN-100 and peroxidase/Sepabeads EC-HA is explained by the high sorption ability of commercial polymer supports MN-100 and Sepabeads EC-HA and the formation of strong covalent bonds between the enzyme and the support. The optimal conditions for the oxidation of 2-methylnaphthol to 2-methyl-1,4-naphthohydroquinone using synthesized biocatalytic systems were also selected. The temperature of 40 °C and pH 7.2 were found to be optimal for the oxidation of the proposed substrate. The presented results will undoubtedly make a positive contribution to the development of the chemical and pharmaceutical industry.