Stability of immobilized Rhizomucor miehei lipase for the synthesis of pentyl octanoate in a continuous packed bed bioreactor

Abstract

The enzymatic synthesis of organic compounds in continuous bioreactors is an efficient way to obtain industrially important chemicals. However, few works have focused on the study of the operational conditions and the bioprocess performance. In this work, the aliphatic ester pentyl octanoate was obtained by direct esterification using a continuous packed bed bioreactor containing the immobilized enzyme Lipozyme® RM IM as catalyst. Enzymatic deactivation was evaluated under different conditions for the operational parameters substrate/enzyme ratio (5.00, 1.67, 0.83 and 0.55 mmolsubstrate·min-1·g-1enzyme) and temperature (30, 40, 50 and 60°C). The optimal condition was observed at 30°C, which gave the minimum enzymatic deactivation rate and the maximum conversion to the desired product, yielding approximately 60 mmols of ester for an enzyme loading of 0.5 g into the bioreactor. A first-order deactivation model showed good agreement with the experimental data.