Abstract:
:A Candida rugosa lipase immobilized on polypropylene powder was employed as the biocatalyst for the enantioselective hydrolysis of (R, S)-suprofen 2,2,2-trifluorothioester in cyclohexane, in which trioctylamine was added as the catalyst to perform in situ racemization of the remaining (R)-thioester. A hollow-fiber membrane was also integrated with the dynamic kinetic resolution process in order to continuously extract the desired (S)-suprofen into an aqueous solution containing NaOH. A kinetic model for the whole process (operating in batch and feed-batch modes) was developed, in which enzymatic hydrolysis and deactivation, lipase activation, racemization and non-enantioselective hydrolysis of the substrate by trioctylamine, and reactive extraction of (R)- and (S)-suprofen into the aqueous phase in the membrane were considered. Theoretical predictions from the model for the time-course variations of substrate and product concentrations in each phase were compared with experimental data.
journal_name
Bioprocess Biosyst Engjournal_title
Bioprocess and biosystems engineeringauthors
Wang LW,Cheng YC,Tsai SWdoi
10.1007/s00449-004-0379-8subject
Has Abstractpub_date
2004-12-01 00:00:00pages
39-49issue
1eissn
1615-7591issn
1615-7605journal_volume
27pub_type
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