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Enantioseparation of ( R,S )‐ketoprofen using Candida antarctica lipase B in an enzymatic membrane reactor
Author(s) -
Ong Ai Lien,
Kamaruddin Azlina Harun,
Bhatia Subhash,
AboulEnein Hassan Y.
Publication year - 2008
Publication title -
journal of separation science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.72
H-Index - 102
eISSN - 1615-9314
pISSN - 1615-9306
DOI - 10.1002/jssc.200800086
Subject(s) - candida antarctica , chemistry , lipase , substrate (aquarium) , immobilized enzyme , biocatalysis , membrane reactor , chromatography , ketoprofen , triacylglycerol lipase , enzyme catalysis , batch reactor , catalysis , organic chemistry , enzyme , reaction mechanism , oceanography , geology
An enzymatic membrane reactor (EMR) for enantioseparation of ( R , S )‐ketoprofen via Candida antarctica lipase B (CALB) as biocatalyst was investigated. A comparative study of free and immobilized CALB was further conducted. The catalytic behaviour of CALB in an EMR was affected by the process parameters of enzyme load, substrate concentration, substrate molar ratio, lipase solution pH, reaction temperature, and substrate flow rate. Immobilization of CALB in the EMR was able to reduce the amount of enzyme required for the enantioseparation of ( R , S )‐ketoprofen. Immobilized CALB in the EMR assured higher reaction capacity, better thermal stability, and reusability. It was also found to be more cost effective and practical than free CALB in a batch reactor.