The main focus of this work was to investigate the residual esterification activity and the product conversion after 10 successive cycles of utilization of a commercial lipase in three systems: esterification of 2-ethyl hexanol and palmitic acid in a solvent-free system; esterification of ascorbic acid and palmitic acid in tert-butanol; and transesterification of glycerol and methyl benzoate in 2-propanol. These systems were chosen based on previous results by our research group in terms of product conversion. Before scale-up, there is a need for evaluating several cycles of utilization of the biocatalyst. The esterification of 2-ethyl hexanol showed that after 10 cycles the enzyme retained 90% of its activity. The system consisting of ascorbic acid, palmitic acid, Novozym 435 and tert-butanol showed that a reduction in enzyme activity was accompanied by a reduction in reaction conversion; the same behavior was not observed for the third system.
Lipase; Transesterification; Reuse
