Abstract
An approach is presented for the stable covalent immobilization of Upase from Candida rugosa on Eupergit? with a high retention of hydrolytic activity. It comprises covalent bonding via lipase carbohydrate moiety previously modified by periodate oxidation, allowing a reduction in the involvement of the enzyme functional groups that are probably important in the catalytic mechanism. The hydrolytic activities of the lipase immobilized on Eupergif1 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 applied in this study with respect to both, yield of immobilization and hydrolytic activity of the immobilized enzyme.
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