Open AccessGlycosylation of flavonoids with a glycosyltransferase from Bacillus cereus
Author(s) -
Hyung Ko Jae,
Gyu Kim Bong,
JoongHoon Ahn
Publication year - 2006
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2006.00226.x
Subject(s) - glycosyltransferase , glycosylation , biochemistry , naringenin , kaempferol , uridine diphosphate , chemistry , bacillus cereus , biotransformation , apigenin , enzyme , escherichia coli , flavonoid , biology , bacteria , gene , genetics , antioxidant
Microbial glycosyltransferases can convert many small lipophilic compounds such as phenolics, terpenoids, cyanohydrins and alkaloids into glycons using uridine‐diphosphate‐activated sugars. The main chemical functions of glycosylation processes are stabilization, detoxification and solubilization of the substrates. The gene encoding the UDP‐glycosyltransferase from Bacillus cereus, BcGT‐1 , was cloned by PCR and sequenced. BcGT‐1 was expressed in Escherichia coli BL21 (DE3) with a his‐tag and purified using a His‐tag affinity column. BcGT‐1 could use apigenin, genistein, kaempferol, luteolin, naringenin and quercetin as substrates and gave two reaction products. The enzyme preferentially glycosylated at the 3‐hydroxyl group, but it could transfer a glucose group onto the 7‐hydroxyl group when the 3‐hydroxyl group was not available. The reaction products made by biotransformation of flavonoids with E. coli expressing BcGT‐1 are similar to those produced with the purified recombinant enzyme. Thus, this work provides a method that might be useful for the biosynthesis of flavonoid glucosides and for the glycosylation of related compounds.