Covalent Immobilization of Lipase on Poly(acrylonitrile-co-maleic acid) Ultrafiltration Hollow Fiber Membrane  

作　　者：YE Peng XU Zhi-kang WU Jian DENG Hong-tao SETA Patrick 

机构地区：[1]Institute of Polymer Science, Zhejiang University, Hangzhou 310027, P. R. China [2]Department of Chemistry, Zhejiang University, Hangzhou 310027, P. R. China [3]Institute of Europee des Membranes, UMR CNRS No. 5635, 34293 Montpellier Cedex 05, France

出　　处：《Chemical Research in Chinese Universities》2005年第6期723-727,共5页高等学校化学研究（英文版）

基　　金：SupportedbytheNationalNaturalScienceFoundationofChina(No.50273032)andProgrammeSino-FrancaisdeRecherchesAvances(No.PRAE03-04).

摘　　要：Lipase from Candida rugosa was covalently immobilized on the surface of an uhrafihration 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 uhrafihration 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.

关 键 词：Poly（acrylonitrile-co-maleic acid） Uhrafihration hollow fiber membrane LIPASE Enzyme immobilization Covalent bonding 

分 类 号：TQ46[化学工程—制药化工]