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Comparison of kinetic resolution between two racemic ibuprofen esters in an enzymic membrane reactor

Paper ID Volume ID Publish Year Pages File Format Full-Text
36545 45136 2005 9 PDF Available
Title
Comparison of kinetic resolution between two racemic ibuprofen esters in an enzymic membrane reactor
Abstract

The enantioselective hydrolysis of racemic esters and simultaneous separation of the corresponding optically pure (S)-acid as pure isomer is of considerable interest to the pharmaceutical industry as a route to non-steroidal anti-inflammatory drugs. In the present study, an enzymic membrane reactor (EMR) was employed for the optical resolution of racemic ibuprofen ester. EMR consisted of a lipase immobilized polymeric membrane, an organic phase dissolving ester and an aqueous phase to recover the reaction products. The catalytic behaviour of lipase immobilized in a polymeric hollow fibre membrane was investigated using 1-heptyl-ibuprofen ester and 2-ethoxyethyl-ibuprofen ester. The two ester substrates differ in the nature of the alkyl group of the alcohol moiety. The performance of the immobilized enzyme was studied as a function of temperature, pH of phosphate buffer solution and substrate flow rate. The operational conditions that favoured the enzyme selectivity for the (S)-ibuprofen esters, in order to obtain the corresponding (S)-ibuprofen acid as an optically pure single enantiomer, were identified. Lipase from Candida rugosa was used in the hydrolysis of racemic ibuprofen ester. (R)-Ibuprofen ester was found to be less reactive in the reaction. Highest enantioselectivity of enzyme was obtained with phosphate buffer solution of pH 8.0 at temperature of 40 °C and at lower substrate flow rate for both racemic 1-heptyl-ibuprofen and 2-ethoxyethyl-ibuprofen esters. The hydrolysis of racemic 1-heptyl-ibuprofen ester gave 4% eeS, 90% eeP and E value of 1–4, while the hydrolysis of 2-ethoxyethyl-ibuprofen ester resulted in 31% eeS, 85% eeP and E value of 9.5–13 by running the experiment under optimum operating condition in an enzymatic membrane reactor.

Keywords
Membrane reactor; Ibuprofen; Candida rugosa; Hydrolysis; Enantioselectivity; 1-Heptyl-ibuprofen ester; 2-Ethoxyethyl-ibuprofen ester
First Page Preview
Comparison of kinetic resolution between two racemic ibuprofen esters in an enzymic membrane reactor
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 40, Issue 7, June 2005, Pages 2417–2425
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering