The enantiocatalytic performance of immobilised lipase in an emulsion membrane reactor using stable emulsion prepared by membrane emulsification technology has been studied. The production of optical pure (S)-naproxen from racemic naproxen methyl ester has been used as model reaction system. The O/W emulsion, containing the substrate in the organic phase, was fed to the enzyme membrane reactor from shell-to-lumen. The enzyme was immobilised in the sponge layer (shell side) of capillary polyamide membrane with 50 kDa cut-off. The results evidenced that lipase maintained stable activity during all the operation time (more than 250 hours), showing an enantiomeric excess (96 ±2%) comparable to the free enzyme (98 ± 1%) and much higher compared to similar lipase-loaded membrane reactors used in two-separate phase systems (90%). The results demonstrate that immobilised enzymes can achieve high stability as well as high catalytic activity and enantioselectivity.
Use of Stable Emulsion to Improve Stability, Activity, and Enantioselectivity of Lipasi Immobilized in a Membrane Reactor
Giorno L;
2003
Abstract
The enantiocatalytic performance of immobilised lipase in an emulsion membrane reactor using stable emulsion prepared by membrane emulsification technology has been studied. The production of optical pure (S)-naproxen from racemic naproxen methyl ester has been used as model reaction system. The O/W emulsion, containing the substrate in the organic phase, was fed to the enzyme membrane reactor from shell-to-lumen. The enzyme was immobilised in the sponge layer (shell side) of capillary polyamide membrane with 50 kDa cut-off. The results evidenced that lipase maintained stable activity during all the operation time (more than 250 hours), showing an enantiomeric excess (96 ±2%) comparable to the free enzyme (98 ± 1%) and much higher compared to similar lipase-loaded membrane reactors used in two-separate phase systems (90%). The results demonstrate that immobilised enzymes can achieve high stability as well as high catalytic activity and enantioselectivity.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
