Chemical Research in Chinese Universities ›› 2005, Vol. 21 ›› Issue (6): 723-727.

• Articles • Previous Articles     Next Articles

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

YE Peng1, XU Zhi-kang1, WU Jian2, DENG Hong-tao1, SETA Patrick3   

  1. 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 Europée des Membranes, UMR CNRS No. 5635, 34293 Montpellier Cedex 05, France
  • Received:2005-01-19 Online:2005-11-23 Published:2011-08-06
  • Supported by:

    Supported by the National Natural Science Foundation of China(No.50273032) and Programme Sino-Francais de Recherches Avancées(No.PRA E03-04)

Abstract: 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.

Key words: Poly(acrylonitrile-co-maleic acid), Ultrafiltration hollow fiber membrane, Lipase, Enzyme immobilization, Covalent bonding