Preparation of enantiomerically pure (S)-flurbiprofen by an esterase from Pseudomonas sp. KCTC 10122BP

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Title
Preparation of enantiomerically pure (S)-flurbiprofen by an esterase from Pseudomonas sp. KCTC 10122BP
Author(s)
Eun Gyo Lee; Hye Soon Won; Hyeon Su Ro; Y W Ryu; Bong Hyun Chung
Bibliographic Citation
Journal of Molecular Catalysis B: Enzymatic, vol. 26, no. 3, pp. 149-156
Publication Year
2003
Abstract
Esterase PF1-K from Pseudomonas sp. KTCC 10122BP was overproduced by the fed-batch culture of Escherichia coli. The soluble expression of esterase PF1-K was achieved by shifting the culture temperature from 37 to 25°C at the time of IPTG induction. The enzyme was partially purified to about 75% purity by a single-step hydrophobic interaction column chromatography. The purified enzyme exhibited a fairly high enantioselectivity towards the hydrolysis of rac-flurbiprofen ethyl ester. The enzymatic chiral resolution was further improved by optimizing the reaction conditions in terms of reaction rate and enantioselectivity. The optimal reaction conditions were found to be 40°C, pH 10.5 and 600mM of initial rac-flurbiprofen ethyl ester. After 90min of batch reaction under the optimal conditions, 50% of the initial rac-flurbiprofen was hydrolyzed with an enantiomeric excess of 99%.
Keyword
enantioselective hydrolysisflurbiprofenpseudomonasrecombinant esterase
ISSN
1381-1177
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.molcatb.2003.05.004
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > BioProcess Engineering Center > 1. Journal Articles
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