Laccase-Catalyzed Dimerization of Piceid, a Resveratrol Glucoside, and its Further Enzymatic Elaboration

The laccase‐catalyzed oxidation of piceid, the 3‐β‐D‐glucopyranosyl derivative of the stilbenic phytoalexin resveratrol, allowed isolation of the corresponding β‐5 like trans‐dehydrodimer in good yield (45%) avoiding chromatography. This compound was then submitted to the action of a small library o...

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Bibliographic Details
Published in:Advanced synthesis & catalysis 2015-05, Vol.357 (8), p.1831-1839
Main Authors: Gavezzotti, Paolo, Bertacchi, Federica, Fronza, Giovanni, Křen, Vladimír, Monti, Daniela, Riva, Sergio
Format: Article
Language:English
Subjects:
Antioxidants
Cellulase
Dimerization
Dimers
Enantiomers
Fungi
Glucosidase
glycosidase
Laccase
Oxidation
piceid
resveratrol
viniferin
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Summary:The laccase‐catalyzed oxidation of piceid, the 3‐β‐D‐glucopyranosyl derivative of the stilbenic phytoalexin resveratrol, allowed isolation of the corresponding β‐5 like trans‐dehydrodimer in good yield (45%) avoiding chromatography. This compound was then submitted to the action of a small library of commercially available hydrolases. While the cellulase from Trichoderma viride was able to fully hydrolyze the diglycosylated dimer to give the corresponding β‐5 like trans‐dehydrodimer of resveratrol, the β‐glucosidase from almonds allowed the isolation of a monoglycosylated intermediate in reasonable yield. The diastereoisomers and the enantiomers of the isolated dimeric products were separated using a semi‐preparative chiral column. The basic antioxidant properties of these new dimers have been determined.
ISSN:1615-4150
1615-4169
DOI:10.1002/adsc.201500185