On-off dewatering control for lipase-catalyzed synthesis of n-butyl oleate in n-hexane by tubular type pervaporation system

Abstract

Lipase-catalyzed esterification of n-butyl oleate was carried out in n-hexane as a model reaction. The optimal activity of Candida rugosa lipase was shown in a water activity (a(w)) range of 0.52 to 0.65 at 30 degrees C. The water produced from the esterification was removed by a tubular type pervaporation system. The rate of ester formed from the enzymatic esterification was allowed to be the same as the rate of water removal by maintaining an optimal a(w) of the reaction system using an on-off dewatering control device. The reaction rate and yield with a(w) control were increased two folds higher than the respective values for the uncontrolled reaction.