Kinetics of lipase-catalyzed hydrolysis of palm oil in lecithin/izooctane reversed micelles |
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Authors: | Z D Knezevic S S Siler-Marinkovic L V Mojovic |
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Institution: | (1) Department of Biochemical Engineering and Biotechnology, Faculty of Technology and Metallurgy Belgrade, University of Belgrade, Karnegijeva 4, P.O. Box 494, Yu-11001 Belgrade, Yugoslavia Tel.: 381 11 3221 051/ext. 600 Fax: 381 11 3370387 e-mail: bajic@elab.tmf.bg.ac.yu, YU |
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Abstract: | Candida rugosa lipase has been used to investigate the hydrolysis of palm oil in a lecithin/isooctane reversed micellar system. The reaction
obeys Michaelis-Menten kinetics for the initial conditions. Kinetic parameters such as maximum rate and Michaelis constant
(K
m) were determined for lipase-catalyzed hydrolysis in n-hexane and isooctane. According to the K
m values, the enzyme affinity towards the substrate was increased in isooctane. The maximum degree of hydrolysis was generally
decreased as the initial substrate concentration was increased. This may suggest that the hydrolysis in lecithin reversed
micelles should be regarded as a one-substrate first-order reversible reaction. It is shown in this study that the proposed
one-substrate first-order kinetic model can serve for the precise prediction of the degree of hydrolysis for a known reaction
time or vice versa, when the initial substrate concentration is less than 0.325 mol/dm3. A disagreement with this model was found when the initial substrate concentration was higher than approximately 0.3 mol/dm3. This may be due to the effects of the products on lipase activity or even to the conversion of the reversed micellar system
to other systems.
Received: 16 May 1997 / Received revision: 22 October 1997 / Accepted: 24 October 1997 |
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Keywords: | |
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