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J. Microbiol. Biotechnol. 2009; 19(4): 387-390

Published online April 28, 2009 https://doi.org/10.4014/jmb.0802.116

Copyright © The Korean Society for Microbiology and Biotechnology.

Formation of Flavone Di-O-Glucosides Using a Glycosyltransferase from Bacillus cereus

Byoung Chan Ahn , Bong Gyu Kim , Young Min Jeon , Eun Jeong Lee , Yoongho Lim and Joong-Hoon Ahn *

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

Abstract

Microbial UDP-glycosyltransferases can convert many
small lipophilic compounds into glycons using uridinediphosphate-
activated sugars. The glycosylation of flavonoids
affects solubility, stability, and bioavailability. The gene
encoding the UDP-glycosyltransferase from Bacillus cereus,
BcGT-3, was cloned by PCR and sequenced. BcGT-3 was
expressed in Escherichia coli BL21 (DE3) with a glutathione
S-transferase tag and purified using a glutathione Stransferase
affinity column. BcGT-3 was tested for activity
on several substrates including genistein, kaempferol,
luteolin, naringenin, and quercetin. Flavonols were the
best substrates for BcGT-3. The enzyme dominantly
glycosylated the 3-hydroxyl group, but the 7-hydroxyl
group was glycosylated when the 3-hydroxyl group was
not available. The kaempferol reaction products were
identified as kaempferol-3-O-glucoside and kaempferol-
3,7-O-diglucoside. Kaempferol was the most effective
substrate tested. Based on HPLC, LC/MS, and NMR analyses
of the reaction products, we conclude that BcGT-3 can be
used for the synthesis of kaempferol 3,7-O-diglucose.

Keywords: Glycosylation, UDP-glycosyltransferases, kaempferol 3,7-O-diglucoside