Abstract
Flavonoid glycosides are highly attractive targets due to their dominant roles in clinical, cosmetic production and in the food industry. In this research, an Escherichia coli strain bearing the reconstructed uridine-diphosphate glucose (UDP-glucose) pathway cassette and a putative glycosyltransferase from Arabidopsis thaliana, was developed as a host for the production of apigenin-7-O-β-d-glucoside (APG) and baicalein-7-O-β-d- glucoside (BCG) from exogenously supplied flavone aglycones (apigenin and baicalein, respectively). In order to improve the yield, genetic engineering of E. coli strains for optimization of intracellular UDP-glucose generation, as well as media optimization were carried out. The production was scaled up using a fed batch fermentation, and the maximal yield of products reached 90.88 μM (39.28 mg L-1) and 76.82 μM (33.19 mg L-1) of APG and BCG, respectively. And, the maximum bioconversion rate corresponded to 90.88% and 76.82% of apigenin and baicalein, respectively.
| Original language | English |
|---|---|
| Pages (from-to) | 1744-1748 |
| Number of pages | 5 |
| Journal | Process Biochemistry |
| Volume | 48 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - 2013 Nov 1 |
| Externally published | Yes |
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Keywords
- Escherichia coli
- Flavones
- Glucosylation
- Heterologous production
- Whole cell biotransformation
ASJC Scopus subject areas
- Bioengineering
- Biochemistry
- Applied Microbiology and Biotechnology
Cite this
Toward the production of flavone-7-O-β-d-glucopyranosides using Arabidopsis glycosyltransferase in Escherichia coli. / Thuan, Nguyen Huy; Park, Je Won; Sohng, Jae Kyung.
In: Process Biochemistry, Vol. 48, No. 11, 01.11.2013, p. 1744-1748.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Toward the production of flavone-7-O-β-d-glucopyranosides using Arabidopsis glycosyltransferase in Escherichia coli
AU - Thuan, Nguyen Huy
AU - Park, Je Won
AU - Sohng, Jae Kyung
PY - 2013/11/1
Y1 - 2013/11/1
N2 - Flavonoid glycosides are highly attractive targets due to their dominant roles in clinical, cosmetic production and in the food industry. In this research, an Escherichia coli strain bearing the reconstructed uridine-diphosphate glucose (UDP-glucose) pathway cassette and a putative glycosyltransferase from Arabidopsis thaliana, was developed as a host for the production of apigenin-7-O-β-d-glucoside (APG) and baicalein-7-O-β-d- glucoside (BCG) from exogenously supplied flavone aglycones (apigenin and baicalein, respectively). In order to improve the yield, genetic engineering of E. coli strains for optimization of intracellular UDP-glucose generation, as well as media optimization were carried out. The production was scaled up using a fed batch fermentation, and the maximal yield of products reached 90.88 μM (39.28 mg L-1) and 76.82 μM (33.19 mg L-1) of APG and BCG, respectively. And, the maximum bioconversion rate corresponded to 90.88% and 76.82% of apigenin and baicalein, respectively.
AB - Flavonoid glycosides are highly attractive targets due to their dominant roles in clinical, cosmetic production and in the food industry. In this research, an Escherichia coli strain bearing the reconstructed uridine-diphosphate glucose (UDP-glucose) pathway cassette and a putative glycosyltransferase from Arabidopsis thaliana, was developed as a host for the production of apigenin-7-O-β-d-glucoside (APG) and baicalein-7-O-β-d- glucoside (BCG) from exogenously supplied flavone aglycones (apigenin and baicalein, respectively). In order to improve the yield, genetic engineering of E. coli strains for optimization of intracellular UDP-glucose generation, as well as media optimization were carried out. The production was scaled up using a fed batch fermentation, and the maximal yield of products reached 90.88 μM (39.28 mg L-1) and 76.82 μM (33.19 mg L-1) of APG and BCG, respectively. And, the maximum bioconversion rate corresponded to 90.88% and 76.82% of apigenin and baicalein, respectively.
KW - Escherichia coli
KW - Flavones
KW - Glucosylation
KW - Heterologous production
KW - Whole cell biotransformation
UR - http://www.scopus.com/inward/record.url?scp=84887123711&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84887123711&partnerID=8YFLogxK
U2 - 10.1016/j.procbio.2013.07.005
DO - 10.1016/j.procbio.2013.07.005
M3 - Article
AN - SCOPUS:84887123711
VL - 48
SP - 1744
EP - 1748
JO - Process Biochemistry
JF - Process Biochemistry
SN - 1359-5113
IS - 11
ER -