Stilbene biotransformation activity demonstrated in partially purified protein fractions from C. polonica. Stilbene biotransformation activity demonstrated.

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Stilbene biotransformation activity demonstrated in partially purified protein fractions from C. polonica. Stilbene biotransformation activity demonstrated in partially purified protein fractions from C. polonica. A two-step chromatography scheme (affinity separation on concanavalin A-Sepharose followed by anion exchange) separated the three astringin conversion activities indicated by the in vivo experiments: oxidation of astringin to the ring-opened lactone 1 (A); deglucosylation of astringin to form (E)- and (Z)-piceatannol (2a and 2b; B); and oxidation of astringin to form a mixture of dimeric products 3a and 3b (C). Assays for the activities in A and C were performed in 50 mm MOPSO, pH 6.8, and 10% (v/v) glycerol with 1.2 mm astringin and analyzed by LC-ESI-MS and UV-diode array detector. Assays for the activity in B were performed in 50 mm Tris, pH 7.5, and 10% (v/v) glycerol. mAU, Milliabsorbance unit. Almuth Hammerbacher et al. Plant Physiol. 2013;162:1324-1336 ©2013 by American Society of Plant Biologists