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Updated: Apr 10, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Creating a Water-Soluble Resveratrol-Based Antioxidant by Site-Selective Enzymatic Glucosylation
Alexander Lepak1, Alexander Gutmann1, Sandra T Kulmer1
1Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, Petersgasse 12, 8010 Graz (Austria).
Abstract:
The phytochemical resveratrol (trans-3,5,4'-trihydroxystilbene) has drawn great interest as health-promoting food ingredient and potential therapeutic agent. However, resveratrol shows vanishingly low water solubility; this limits its uptake and complicates the development of effective therapeutic forms. Glycosylation should be useful to enhance resveratrol solubility, with the caveat that unselective attachment of sugars could destroy the molecule's antioxidant activity. UGT71A15 (a uridine 5'-diphosphate α-D-glucose-dependent glucosyltransferase from apple) was used to synthesize resveratrol 3,5-β-D-diglucoside; this was about 1700-fold more water-soluble than the unglucosylated molecule (∼0.18 mM), yet retained most of the antioxidant activity. Resveratrol 3-β-D-glucoside, which is the naturally abundant form of resveratrol, was a practical substrate for perfect site-selective conversion into the target diglucoside in quantitative yield (g L-1 concentration).
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