Lipase-catalyzed transesterification between tributyrylglycerol (tributyrin) (1) and 2-octanol (2) has been studied in neat at 30°C. The kinetic resolution data fit the reported theoretical equations for the equilibrium reaction. The competitive reactions of the enantiomers in (2) with theacyl-enzyme intermediate which was formed the reaction of the free enzyme and (1) was experimentally proved by an accordance of the enantiomeric excess against the extent of conversion plots for racemic and optically active (2). A reversibility of the transesterification was also shownby a decrease in enantiomeric excess of the product and the unreacted starting material duringthe reaction.
