Article ID Journal Published Year Pages File Type
161141 Chemical Engineering Science 2005 14 Pages PDF
Abstract

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.

Related Topics
Physical Sciences and Engineering Chemical Engineering Chemical Engineering (General)
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