Esterification of fatty acids by Penicillium crustosum lipase in a membrane reactor

This study investigated the performance of a membrane reactor system for esterification of oleic acid and butyric acid with ethanol by Penicillium crustosum lipase using polyethersulfone membranes with molecular weight cut-offs of 30, 60 and 100 kDa at pressures up to 200 kPa.

The confinement of lipase with 60 and 100 kDa membranes showed the best results. The esterification of butyric acid in the membrane reactor and with free lipase showed higher conversions than those obtained with oleic acid, since the system operated with oleic acid was more subject to fouling and thus could not be run for repeated cycles.

The confinement of lipase from P. crustosum in a membrane reactor was possible, resulting in the satisfactory conversion of butyric acid to ethyl butyrate with the possibility of reuse of the immobilized enzyme.