Ketoprofen resolution by enzymatic estirification and hydrolysis of the ester product
| Autor: | Ruijiang Li, Hou Ran Low, Won Jae Choi, Mmr Talukder, Yvonne Chow, Jin Chuan Wu, Yujun Leng |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
chemistry.chemical_classification
Ketoprofen Chromatography Ethanol biology Resolution (mass spectrometry) Chemistry Biomedical Engineering Bioengineering biology.organism_classification Applied Microbiology and Biotechnology humanities stomatognathic diseases Hydrolysis chemistry.chemical_compound Enzyme Enzymatic hydrolysis biology.protein medicine Candida antarctica Lipase Biotechnology medicine.drug |
| Zdroj: | Biotechnology and Bioprocess Engineering. 11:211-214 |
| ISSN: | 1976-3816 1226-8372 |
| DOI: | 10.1007/bf02932032 |
| Popis: | ImmobilizedCandida antarctica lipase was used to catalyze the separation of ketoprofen into its components by means of esterification followed by the enzymatic hydrolysis of the ester product. In this study, ketoprofen underwent esterification to ethanol in the presence of isooctane. When the reaction was complete, 58.3% of the ketoprofen had been transformed into an ester. The ketoprofen remaining in solution after the reation was complete consisted primarily of itsS-enantiomer (83.0%), while the 59.4% of the ketoprofen component of the ester consisted of itsR-enantiomer. We then subjected the ester product to enzymatic hydrolysis in the presence of the same enzyme and produced a ketoprofen product rich in theR-enantiomer; 77% of this product consisted of theR-enantiomer when 50% of the ester had been hydrolyzed, and 90% of it consisted of theR-enantiomer when 30% of the ester had been hydrolyzed. By contrast, theR-enantiomer levels only reached approximately 42 and 65%, respectively, when 50 and 30% of the racemic ester was hydrolyzed under the same conditions. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink