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Enzymatic Kinetic Resolution of Silybin Diastereoisomers
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SYSNO ASEP 0350993 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Enzymatic Kinetic Resolution of Silybin Diastereoisomers Author(s) Monti, D. (IT)
Gažák, Radek (MBU-M) RID, ORCID
Marhol, Petr (MBU-M) RID
Biedermann, David (MBU-M) RID, ORCID
Purchartová, Kateřina (MBU-M) RID
Fedrigo, M. (IT)
Riva, S. (IT)
Křen, Vladimír (MBU-M) RID, ORCIDSource Title Journal of Natural Products. - : American Chemical Society - ISSN 0163-3864
Roč. 73, č. 4 (2010), s. 613-619Number of pages 7 s. Language eng - English Country US - United States Keywords MARIANUM MILK THISTLE ; PROSTATE-CANCER ; SILYMARIN Subject RIV CC - Organic Chemistry R&D Projects GAP207/10/0288 GA ČR - Czech Science Foundation (CSF) LC06010 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) OC08049 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z50200510 - MBU-M (2005-2011) UT WOS 000276950000019 DOI 10.1021/np900758d Annotation 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 transcsterification 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 Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2011
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