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LIPASES : BIOTRANSFORMATIONS, ACTIVE SITE MODELS AND KINETICS
Kloosterman, M. Kierkels, J. G. T. Guit, R. P. M. Vleugels, L. F. W. Gelade, E. T. F. van den Tweel, W. J. J. Elferink, V. H. M. Hulshof, L. A. Kamphuis, J.
Kloosterman, M.
Kierkels, J. G. T.
Guit, R. P. M.
Vleugels, L. F. W.
Gelade, E. T. F.
van den Tweel, W. J. J.
Elferink, V. H. M.
Hulshof, L. A.
Kamphuis, J.
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Issue Date
1991
Submitted date
2024-03-20
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Abstract
Lipases can be used to obtain various (chiral) intermediates. To select a suitable hydrolytic enzyme from the increasing number of commercially available lipases application of active-site models may be very useful. Since the hydrolysis takes place at the interface, the kinetics of lipase catalyzed reactions are strongly dependend upon the quantity and quality of the interface. A newly developed dynamic method, based on measuring the droplet-size distribution by light scattering (Fraunhofer diffraction), has proven to be very useful to measure the total interfacial area of a non-stabilized emulsion. In an alternative approach lipase kinetics could be determined by using a hollow fiber membrane reactor. Both approaches indicate that there is a linear relationship between the rate of lipolysis and the interfacial area. The effect of the quality of the interface on the enzymic hydrolysis reaction is currently being studied to optimize both the rate as well as the (stereo)selectivity of the hydrolysis.
Citation
Lipases : structure, mechanism and genetic engineering, 187 - 200
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Book chapter
conference paper
conference paper
Language
en
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Series/Report no.
GBF monographs ; Volume 16
ISSN
0930-4320
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ISBN
156081165X
3527283323
3527283323
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Attribution-NonCommercial-ShareAlike 4.0 International