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Laccase‐Catalyzed Dimerization of Piceid, a Resveratrol Glucoside, and its Further Enzymatic Elaboration
Author(s) -
Gavezzotti Paolo,
Bertacchi Federica,
Fronza Giovanni,
Křen Vladimír,
Monti Daniela,
Riva Sergio
Publication year - 2015
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.201500185
Subject(s) - chemistry , glucoside , cellulase , resveratrol , yield (engineering) , enantiomer , phytoalexin , organic chemistry , dimer , hydrolysis , laccase , enantiomeric excess , enzyme , catalysis , stereochemistry , chromatography , enantioselective synthesis , biochemistry , medicine , materials science , alternative medicine , pathology , metallurgy
Abstract 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.