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

Paper ID Volume ID Publish Year Pages File Format Full-Text
35400 45088 2011 7 PDF Available
Title
Covalent immobilization of lipase onto amine functionalized polypropylene membrane and its application in green apple flavor (ethyl valerate) synthesis
Abstract

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 Km values for the free and immobilized lipase were 2.9 and 8.4 mM, respectively. The Vmax values of free and immobilized enzymes were calculated as 926 and 741 U/mg enzyme, respectively. Optimal temperature was 5 °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.

Keywords
Polypropylene membrane; Immobilized enzyme; Enzyme stability; Enzyme kinetics; Lipase; Ethyl valerate
First Page Preview
Covalent immobilization of lipase onto amine functionalized polypropylene membrane and its application in green apple flavor (ethyl valerate) synthesis
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 46, Issue 1, January 2011, Pages 372–378
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering