Covalent immobilization of lipase onto amine functionalized polypropylene membrane and its application in green apple flavor (ethyl valerate) synthesis


BAYRAMOĞLU G. , HAZER B., Altintas B., Arica M. Y.

PROCESS BIOCHEMISTRY, cilt.46, ss.372-378, 2011 (SCI İndekslerine Giren Dergi) identifier identifier

  • Cilt numarası: 46 Konu: 1
  • Basım Tarihi: 2011
  • Doi Numarası: 10.1016/j.procbio.2010.09.014
  • Dergi Adı: PROCESS BIOCHEMISTRY
  • Sayfa Sayıları: ss.372-378

Özet

In this study, a functionalized hydrophobic polypropylene chloride membrane (PPC) was prepared by the amination of chlorinated polypropylene with hexamethylene diamine (APP). The PPC and APP membranes were characterized using SEM, FTIR and contact angle studies. The aminated polypropylene (APP) membrane was used for covalent immobilization of Candida rugosa lipase via glutaraldehyde coupling. The retained activity of the immobilized lipase was 76%. Kinetic analysis shows that the dependence of lipolytic activity of both free and immobilized lipase on tributyrin substrate concentration can be described by Michaelis-Menten model. The estimated apparent K-m values for the free and immobilized lipase were 2.9 and 8.4 mM, respectively. The V-max values of free and immobilized enzymes were calculated as 926 and 741 U/mg enzyme, respectively. Optimal temperature was 5 degrees C higher for immobilized enzyme than that of the free enzyme. Thermal and storage stabilities were found to be increased upon immobilization. Finally, the immobilized lipase was used for the production of green apple flavor (i.e., ethyl valerate) in hexane medium. (C) 2010 Elsevier Ltd. All rights reserved.