Lipase esterification in the Centrifugal Partition Reactor: Modelling and determination of the specific interfacial area

Abstract

Recently the Centrifugal Partition Chromatography (CPC) device, called Centrifugal Partition Reactor (CPR), was proposed to operate biocatalytic reactions in two phase systems in continuous mode. However, information about hydrodynamic behavior in this device for operation of enzymatic reactions is still missing. In this study, in order to propose a modelling of this type of reactor, we firstly determined in a batch reactor the kinetics constants of a model reaction, the esterification of oleic acid with n-butanol, catalyzed by Rhizomucor miehei lipase. This reaction was described by a Ping Pong bi-bi mechanism with alcohol inhibition and specific experiments were done to determine the kinetic constants. Specific interfacial area in the batch reactor has to be known and its determination was done by measuring droplets size of organic phase by using a microscope. Experimental conversion values of oleic acid obtained in the continuous operation of the CPR, enabled the modelling to give an estimation of the value of the specific interfacial area in the CPR, which was found around 15,000 m2. m−3. The value of the specific interfacial area was shown here to be independent of the mobile phase flow rate, an important feature to characterize such an intensified enzymatic reactor.