Enantioseparation of (R,S)-ketoprofen using Candida antarctica lipase B in an enzymatic membrane reactor.
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.
Ong
Ai Lien
AL
School of Chemical Engineering, Engineering Campus, Universiti Sains Malaysia, Penang, Malaysia.
Kamaruddin
Azlina Harun
AH
Bhatia
Subhash
S
Aboul-Enein
Hassan Y
HY
D020001:1-Butanol; D000894:Anti-Inflammatory Agents, Non-Steroidal / Q000737:chemistry / Q000302:isolation & purification; D002175:Candida / Q000201:enzymology; D002616:Chemical Engineering; D002623:Chemistry Techniques, Analytical / Q000379:methods*; D004800:Enzymes, Immobilized; D004951:Esterification; D005656:Fungal Proteins; D006863:Hydrogen-Ion Concentration; D007660:Ketoprofen / Q000737:chemistry / Q000302:isolation & purification*; D008049:Lipase; D013237:Stereoisomerism; D013696:Temperature
D000894:Anti-Inflammatory Agents, Non-Steroidal; D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D020001:1-Butanol; D007660:Ketoprofen; D008049:Lipase; C431349:lipase B, Candida antarctica