R‐stereopreference analysis of lipase Novozym®435 in kinetic resolution of flurbiprofen
Abstract Immobilized lipase from Candida antarctica (Novozym®435) was employed in the kinetic resolution of racemic flurbiprofen by enantioselective esterification with methanol. It was found that the lipase has the R‐stereopreference and the reaction matches Bi Bi Ping Pong mechanism with dead‐end...
| Published in: | Chirality |
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| Main Authors: | , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Wiley
2006
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.1002/chir.20347 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fchir.20347 https://onlinelibrary.wiley.com/doi/pdf/10.1002/chir.20347 |
| Summary: | Abstract Immobilized lipase from Candida antarctica (Novozym®435) was employed in the kinetic resolution of racemic flurbiprofen by enantioselective esterification with methanol. It was found that the lipase has the R‐stereopreference and the reaction matches Bi Bi Ping Pong mechanism with dead‐end inhibition of methanol. Furthermore, the R‐stereopreference was analyzed in details from the aspects of enzymatic kinetic mechanism and reaction activation energy of both enantiomers. The R‐enantiomer shows lower activation energy and higher maximum reaction rate than the S‐enantiomer, which implies the R‐stereopreference of the lipase and makes the kinetic resolution of flurbiprofen via enzymatic reaction feasible. Chirality 2006. © 2006 Wiley‐Liss, Inc. |
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