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Lipase Immobilization in a Hollow Fibre Membrane Reactor: Kinetics Characterization and Application for Palm Oil Hydrolysis

Z. Knezevicz and B. Obradovic

Department of Biochemical Engineering, Faculty of Technology and Metallurgy, University of Belgrade, YU-11000 Belgrade

 

E-mail: zknez@elab.tmf.bg.ac.yu

Received: 1 April 2004

Abstract: Feasibility of lipase immobilization in a hydrophilic hollow fibre membrane reactor for oil hydrolysis has been demonstrated. A simple immobilization technique was applied resulting in about 155 mg m−2 of immobilized lipase at approximately 40 mass % yield. The immobilized lipase in the membrane reactor had favourable kinetic properties. The reaction in the membrane reactor was well approximated by one-substrate first-order reversible kinetics, previously established for a microemulsion reactor, implying the same reaction mechanism in both systems. Estimation of kinetic parameters revealed that the immobilized lipase retained activity equivalent to approximately 44 % of that of the free lipase but the final conversions were higher with the immobilized lipase. At the enzyme load employed in this study, the loss of activity due to enzyme desorption had only a small effect on the reactor stability and oil hydrolysis. The membrane reactor operated for up to 137 h with no significant loss in productivity. These results imply that the proposed immobilization technique and hollow fibre reactor system with immobilized lipase provide a promising solution for applications of lipase for oil hydrolysis at industrial scale.

Full paper in Portable Document Format: 586a418.pdf

 

Chemical Papers 58 (6) 418–423 (2004)

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