Glycosylation of flavonoids with a glycosyltransferase from Bacillus cereus |
| |
Authors: | Hyung Ko Jae Gyu Kim Bong Joong-Hoon Ahn |
| |
Institution: | Division of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University, Seoul, Korea. |
| |
Abstract: | 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. |
| |
Keywords: | Bacillus cereus flavonoids glycosylation glycosyltransferases |
本文献已被 PubMed 等数据库收录! |
|