Abstract

Laccases from different sources have been used, for the first time, for the selective oxidation of the stilbenic phytoalexin trans-resveratrol (3,5,4′-trihydroxystilbene, 1a ) on a preparative scale. Specifically, the enzymes from Myceliophtora thermophyla and from Trametes pubescens gave the dehydrodimer 2a in 31 and 18% isolated yields, respectively. These results compare favorably with the reported data for the chemically catalyzed dimerization of 1a (18% yields). The antioxidant properties of 2a have also been investigated.

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