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Lipase from Candida rugosa was covalently immobilized on the surface of an ultrafiltration hollow fiber membrane fabricated from poly(acrylonitrile-co-maleic acid)(PANCMA) in which the carboxyl groups were activated with 1-ethyl- 3-(dimethylaminopropyl) carbodiimide hydrochloride(EDC) and dicyclohexyl carbodiimide(DCC)/ N-hydroxyl succinimide(NHS), respectively. The properties of the immobilized lipase were assayed and compared with those of the free enzyme. The maximum activities were observed in a relatively broader pH value range at high temperatures for the immobilized lipase compared to the free one. It was also found that the thermal and pH stabilities of lipase were improved upon immobilization and at 50 ℃ the thermal inactivation rate constant values are 2.1×10 -2 for the free lipase, 3.2×10 -3 for the immobilized lipase on the EDC-activated PANCMA membrane and 3.5×10 -3 for the immobilized lipase on the DCC/NHS-activated PANCMA membrane, respectively.
Lipase from Candida rugosa was covalently immobilized on the surface of an ultrafiltration hollow fiber membrane fabricated from poly (acrylonitrile-co-maleic acid) (PANCMA) in which the carboxyl groups were activated with 1-ethyl- 3- (dimethylaminopropyl) carbodiimide hydrochloride EDC) and dicyclohexyl carbodiimide (DCC) / N-hydroxyl succinimide (NHS), respectively. The maximum of the activities of observed immobilized lipase were assayed and compared with those of the free enzyme. temperatures for the immobilized lipase compared to the free one. It was also found that the thermal and pH stabilities of lipase were improved upon immobilization and at 50 ° C the thermal inactivation rate constant was 2.1 × 10 -2 for the free lipase, 3.2 × 10 -3 for the immobilized lipase on the EDC-activated PANCMA membrane and 3.5 × 10 -3 for the immobilized lipase on the DCC / NHS-activated PANCMA membrane, respectively.