GBF Gesellschaft für Biotechnologische Forschung mbH, Braunschweig
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
