Mf. Maximo et Jp. Vanderlugt, KINETICS OF LIPASE-CATALYZED RESOLUTION OF RACEMIC ALCOHOLS BY REVERSIBLE INTERESTERIFICATION, Biocatalysis, 8(4), 1994, pp. 321-335
In this paper a predictive model for the lipase-catalyzed resolution o
f racemic alcohols by reversible interesterification is presented. The
approach takes into account the acyl transference from the acyl donor
to the enzyme and from the acyl-enzyme complex to the acyl acceptor.
Resolution of (R,S)-2-phenyl-1-propanol by interesterification using n
-butyl-butyrate as acyl donor has been experimentally studied. The rea
ction mechanism was determined as ping-pong with inhibition by n-butan
ol. The model is based on reaction constants which can be calculated f
rom a few long term experiments. The reaction constants calculated in
this way were able to reproduce the results made in other experimental
conditions. The extension of this technique to other reaction systems
is straight forward.