Enzymatic synthesis of short-chain diacylated alkylglycerols: A kinetic study

Abstract

Lipase-catalyzed transesterification of 1- O-octadecyl glycerol (batyl alcohol) with ethyl butyrate has been studied. The effect of vacuum on the rate of both transesterification and distillation of ethyl butyrate has also been investigated and at different reaction conditions, more than 85% of 1- O-octadecyl glycerol was consumed in only 5 min giving rise to the monoester. Then the monoester is again acylated to produce the diesterified product. In addition, the transesterification reactions were effected in solvent free reaction medium and it has been scaled-up to produce up to ca. 500 g of 2,3-dibutyroil-1- O-alkylglycerols in three consecutive cycles reutilizing the same batch of lipase. An efficient evaporation of ethanol was necessary to significantly reduce the reaction times of the transesterification reaction. Finally, a kinetics model describing both the rate of transesterification and the rate of inactivation of the immobilized lipase has been developed. The results indicate that the operational stability of the immobilized lipase confined into the mesh baskets (according to the value of k d attained), was very high and that provides a half-life of the lipase higher than 1500 h. The present procedure is intended to be used for the synthesis of homogeneous alkylglycerols with biological activities and/or precursors of structured alkylglycerols.