COVALENT IMMOBILIZATION OF LIPASE FROM Candida rugosa ON EUPERGIT®

An approach is presented for the stable covalent immobilization of lipase from Can-dida rugosa on Eupergit ® with a high retention of hydrolytic activity. It comprises cova-lent bonding via lipase carbohydrate moiety previously modified by periodate oxidation, allowing a reduction in the involvement of the enzyme functional groups that are proba-bly important in the catalytic mechanism. The hydrolytic activities of the lipase immobi-lized on Eupergit ® by two conventional methods (via oxirane group and via glutaralde-hyde) and with periodate method were compared. Results of lipase assays suggest that periodate method is superior for lipase immobilization on Eupergit ® among methods ap-plied in this study with respect to both, yield of immobilization and hydrolytic activity of the immobilized enzyme. KEY WORDS: Eupergit®; lipase; Candida rugosa; immobilizatio