KINETICS OF LIPASE-CATALYZED RESOLUTION OF RACEMIC ALCOHOLS BY REVERSIBLE INTERESTERIFICATION

In this paper a predictive model for the lipase-catalyzed resolution of 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 reaction mechanism was determined as ping-pong with inhibition by n-butanol. The model is based on reaction constants which can be calculated from 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.