Enzymatic synthesis of piceid glycosides by cyclodextrin glucanotransferase

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Abstract

Novel glycosides of piceid (3,4'-5-trihydroxy stilbene 3-O-beta-D-glucoside) were produced by the transglycosylation reactions of cyclodextrin glucanotransferase (CGTase) from Bacillus macerans, with piceid (PicG(1)) and maltodextrin as the acceptor and donor substrates, respectively. The reactions were performed at 40 degrees C with 2.56 mM piceid (0.1% w/v) and maltodextrin (5% w/v) in 0.02 M citrate phosphate buffer, pH 6.0 containing 5% (v/v) methanol for 6h. Glucose, maltose, sucrose, maltotriose and alpha-cyclodextrin (alpha-CD) were also used to analyze their ability to function as donor substrates, for the glycosylation of piceid. Among the different donor substrates used, the maximum transfer efficiency (TE) of glycosylation of piceid was observed for a-cyclodextrin (78.9%) followed by maltodextrin (72.1%). The partially purified piceid glycoside products (PicG(2) and PicG(3)) were identified by mass spectrometry. (C) 2011 Elsevier Ltd. All rights reserved.

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Subject classification (UKÄ) – MANDATORY

  • Industrial Biotechnology

Keywords

  • Piceid, Cyclodextrin glucanotransferase, Transglycosylation, Resveratrol, Glucoside
Original languageEnglish
Pages (from-to)528-532
JournalProcess Biochemistry
Volume47
Issue number3
Publication statusPublished - 2012
Publication categoryResearch
Peer-reviewedYes