Immobilization of lipase from Candida cylindracea on inorganic supports

Abstract

Lipase from Candida cylindracea has been covalently immobilized on trichlorotriazine activated supports (alumina, silica and two types of controlled pore glass). The optimum conditions of the activation process have been determined (pretreatment, solvent, gram of activating agent/gram of support ratio and reaction time). The influence of the enzyme concentration and of the temperature on the immobilization process has been evaluated. The immobilized derivatives on silica and alumina exhibited greater residual activity and were more resistant to inactivation by temperature (50°C) than their immobilized counterpart on controlled pore glasses. The derivatives obtained on alumina and silica have been used in the hydrolysis of (R,S) ethyl 2-phenylpropionate only yielding the S(+) acid. The influence of Na^I and Ca^II on the lipase activity is discussed. The immobilized derivative on silica, stored at 50°C, was 37 times more stable than the native enzyme and displayed 80% residual activity after 336 h of operating time