Enzymatic kinetic resolution of sylibin diastereoisomers
| Autor: | Monti D., Gazak R., Marhol P., Biedermann D., Purchartova K., Fedrigo M., Riva S., Kren V. |
|---|---|
| Rok vydání: | 2010 |
| Zdroj: | Journal of natural products 73 (2010): 613–619. info:cnr-pdr/source/autori:Monti D., Gazak R., Marhol P., Biedermann D., Purchartova K., Fedrigo M., Riva S., Kren V./titolo:Enzymatic kinetic resolution of sylibin diastereoisomers/doi:/rivista:Journal of natural products (Print)/anno:2010/pagina_da:613/pagina_a:619/intervallo_pagine:613–619/volume:73 |
| Popis: | In nature, the flavonolignan silybin (1) occurs as a mixture of two diastereomers, silybin A and silybin B, which in a number of biological assays exhibit different activities. A library of hydrolases (lipases, esterases, and proteases) was tested for separating the silybin A and B diastereomers by selective transesterification or by stereoselective alcoholysis of 23-O-acetylsilybin (2). Novozym 435 proved to be the most suitable enzyme for the preparative production of both optically pure silybins A and B by enzymatic discrimination. Gram amounts of the optically pure substances can be produced within one week, and the new method is robust and readily scalable to tens of grams. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|