Mol. Cells 2009; 28(4): 397-401
Published online September 30, 2009
https://doi.org/10.1007/s10059-009-0135-7
© The Korean Society for Molecular and Cellular Biology
Flavonoids are a group of polyphenolic compounds that have been recognized as important due to their physiological and pharmacological roles and their health benefits. Glycosylation of flavonoids has a wide range of effects on flavonoid solubility, stability, and bioavailability. We previously generated the E. coli BL21 (DE3) Δpgi host by deleting the glucose-phosphate isomerase (Pgi) gene in E. coli BL21 (DE3). This host was further engineered for whole-cell biotransformation by integration of galU from E. coli K12, and expression of calS8 (UDP-glucose dehydrogenase) and calS9 (UDP-glucuronic acid decarboxylase) from Micromonospora echinospora spp. calichensis and arGt-4 (7-O-glycosyltransferase) from Arabidopsis thaliana to form E. coli (US89Gt-4), which is expected to produce glycosylated flavonoids. To test the designed system, the engineered host was fed with naringenin as a substrate, and naringenin 7-O-xyloside, a glycosylated naringenin product, was detected. Product was verified by HPLC-LC/MS and ESI-MS/MS analyses. The recon-structed host can be applied for the production of various classes of glycosylated flavonoids.
Keywords 7-O-xylosyl naringenin, glycosylation, metabolic engineering, naringenin, UDP-D-xylose
Mol. Cells 2009; 28(4): 397-401
Published online October 31, 2009 https://doi.org/10.1007/s10059-009-0135-7
Copyright © The Korean Society for Molecular and Cellular Biology.
Dinesh Simkhada, EuiMin Kim, Hei Chan Lee, and Jae Kyung Sohng
Flavonoids are a group of polyphenolic compounds that have been recognized as important due to their physiological and pharmacological roles and their health benefits. Glycosylation of flavonoids has a wide range of effects on flavonoid solubility, stability, and bioavailability. We previously generated the E. coli BL21 (DE3) Δpgi host by deleting the glucose-phosphate isomerase (Pgi) gene in E. coli BL21 (DE3). This host was further engineered for whole-cell biotransformation by integration of galU from E. coli K12, and expression of calS8 (UDP-glucose dehydrogenase) and calS9 (UDP-glucuronic acid decarboxylase) from Micromonospora echinospora spp. calichensis and arGt-4 (7-O-glycosyltransferase) from Arabidopsis thaliana to form E. coli (US89Gt-4), which is expected to produce glycosylated flavonoids. To test the designed system, the engineered host was fed with naringenin as a substrate, and naringenin 7-O-xyloside, a glycosylated naringenin product, was detected. Product was verified by HPLC-LC/MS and ESI-MS/MS analyses. The recon-structed host can be applied for the production of various classes of glycosylated flavonoids.
Keywords: 7-O-xylosyl naringenin, glycosylation, metabolic engineering, naringenin, UDP-D-xylose
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