Document Detail


Kinetic resolution of ibuprofen catalyzed by Candida rugosa lipase in ionic liquids.
MedLine Citation:
PMID:  15515047     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Candida rugosa lipase-catalyzed esterification of ibuprofen with 1-propanol was conducted in seven ionic liquids and the results were compared with those in isooctane. Although the enzyme showed comparable or higher activity in some ionic liquids compared to that in isooctane, only in the case of [BMIM]PF6 was the enantioselectivity (E = 24.1) almost twice that (E = 13.0) of isooctane. In another six ionic liquids the enzyme enantioselectivity was much poorer (E = 1.1-6.4). At the same conversion of 30%, E of [BMIM]PF6 is more than triple that of isooctane. The lipase stability in [BMIM]PF6 was improved by 25% of that in isooctane. It was concluded that [BMIM]PF6 could be applied to substitute the conventional organic solvent (isooctane) in the esterification of ibuprofen.
Authors:
Yu Hongwei; Wu Jinchuan; Ching Chi Bun
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Chirality     Volume:  17     ISSN:  0899-0042     ISO Abbreviation:  Chirality     Publication Date:  2005 Jan 
Date Detail:
Created Date:  2004-11-23     Completed Date:  2005-08-30     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8914261     Medline TA:  Chirality     Country:  United States    
Other Details:
Languages:  eng     Pagination:  16-21     Citation Subset:  IM    
Copyright Information:
Copyright 2004 Wiley-Liss, Inc.
Affiliation:
Chemical and Process Engineering Centre, National University of Singapore, Singapore. cpeyuhw@nus.edu.sg
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MeSH Terms
Descriptor/Qualifier:
Candida / enzymology*
Catalysis
Enzyme Stability
Ibuprofen / chemistry*
Kinetics
Lipase / metabolism*
Stereoisomerism
Temperature
Chemical
Reg. No./Substance:
15687-27-1/Ibuprofen; EC 3.1.1.3/Lipase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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