Formation of flavone di-O-glucosides using a glycosyltransferase from Bacillus cereus.
J Microbiol Biotechnol
; 19(4): 387-90, 2009 Apr.
Article
en En
| MEDLINE
| ID: mdl-19420995
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Bacillus cereus
/
Proteínas Bacterianas
/
Glicosiltransferasas
/
Flavonoles
/
Glucósidos
Idioma:
En
Revista:
J Microbiol Biotechnol
Año:
2009
Tipo del documento:
Article