Cell suspension cultures of Phytolacca americana can glucosylate 6- and 7-hydroxyflavone, but not 5-hydroxyflavone. In order to identify the enzymes responsible for these transformations, glucosyltransferases (GTs) from P. americana were overexpressed in Escherichia coli and purified. The purified PaGT3 enzyme could glucosylate 6- and 7-hydroxyflavone when incubated with UDP-glucose, a glucosyl donor molecule, but PaGT2 could conjugate a glucose moiety only to 6-hydroxyflavone. E. coli cells expressing PaGT2 and 3 could also be utilized for the glucosylation of hydroxyflavones. The glucoside products which had accumulated in the medium of overnight E. coli cell cultures were isolated using hydrophobic resins. This methodology might be suitable for the glucosylation of aglycones with important health-related properties.
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