Enzyme kinetics of kinetic resolution of racemic ibuprofen ester using enzymatic membrane reactor

An ultrafiltration hollow fiber enzymatic membrane reactor was employed to study the kinetics of lipase-catalyzed kinetic resolution of racemic ibuprofen ester. Lipase from Candida rugosa   was employed in the hydrolysis reaction both in free form in a batch system and in immobilized form in an enzymatic membrane reactor (EMR). The half life (t1/2t1/2) of immobilized lipase on spongy layer was 105 h at reaction temperature of 40∘C and 62 h at 45∘C. This value was 94 h for lipase immobilized on the inner lumen and 45 h for free lipase in batch system at 40∘C . Excessive substrate was found to inhibit the reaction as an uncompetitive inhibitor. The by-product 2-ethoxyethanol was found to be non-competitive inhibitor to the reaction when it was present in an excess. Michaelis constant (KmKm) and maximum reaction rate (VmaxVmax) for immobilized lipase were 36.47mmolL-1 and 3.27mmolL-1h-1, respectively; and that for free lipase were 63.43mmolL-1 and 2.83mmolL-1h-1h-1, respectively.