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

0445863 - MBÚ 2016 RIV DE eng J - Journal Article
Gavezzotti, P. - Bertacchi, F. - Fronza, G. - Křen, Vladimír - Monti, D. - Riva, S.
Laccase-Catalyzed Dimerization of Piceid, a Resveratrol Glucoside, and its Further Enzymatic Elaboration.
Advanced Synthesis & Catalysis. Roč. 357, č. 8 (2015), s. 1831-1839. ISSN 1615-4150. E-ISSN 1615-4169
R&D Projects: GA MŠMT(CZ) LD13041
Institutional support: RVO:61388971
Keywords : glycosidase * laccase * piceid
Subject RIV: CC - Organic Chemistry
Impact factor: 6.453, year: 2015

The laccase-catalyzed oxidation of piceid, the 3-beta-D-glucopyranosyl derivative of the stilbenic phytoalexin resveratrol, allowed isolation of the corresponding beta-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 beta-5 like trans-dehydrodimer of resveratrol, the beta-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.
Permanent Link: http://hdl.handle.net/11104/0247898