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J. Microbiol. Biotechnol. 2007; 17(3): 539-542

Published online March 28, 2007

Copyright © The Korean Society for Microbiology and Biotechnology.

Glycosylation of Flavonoids with E. coli Expressing Glycosyltransferase from Xanthomonas campestris

Kim, Jeong Ho , Bong Gyu Kim , Jae Ah Kim , Younghee Park , Yoon Jeong Lee , Yoongho Lim and Joong-Hoon Ahn *

Bio/Molecular Informatics Center, Department of Molecular Biotechnology, Konkuk University, Seoul 143-701, Korea

Abstract

Glycosyltransferase family 1 (UOT) uses small chemicals including phenolics, antibiotics, and alkaloids as substrates to have an influence in biological activities. A glycosyltransferase (XcGT-2) from Xanthomonas campestris was cloned and consisted of a 1,257 bp open reading frame encoding a 45.5 kDa protein. In order to use this for the modification of phenolic compounds, XcGT-2 was expressed in Escherichia coli as a glutathione S-transferase fusion protein. With the E. coli transformant expressing XcGT-2, biotransformation of flavonoids was carried out. Flavonoids having a double bond between carbons 2 and 3, and hydroxyl groups at both C-3' and C-4', were glycosylated and the glycosylation position was determined to be at the hydroxyl group of C-3', using nuclear magnetic resonance spectroscopy. These results showed that XcGT-2 regiospecifically transferred a glucose molecule to the 3'-hydroxyl group of flavonoids containing both 3' and 4'-hydroxyl groups.

Keywords: Biotransformation, flavonoids, glycosyltransferase