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3-Fucosyllactose (3-FL), one of the major oligosaccharides in human breast milk, was produced in engineered Escherichia coli. In order to search for a good α-1,3-fucosyltransferase, three bacterial α-1,3-fucosyltransferases were expressed in engineered E. coli deficient in β-galactosidase activity and expressing the essential enzymes for production of GDP-l-fucose, the donor of fucose for 3-FL biosynthesis. Among the three enzymes tested, the fucT gene from Helicobacter pylori NCTC 11637 gave the best 3-FL production in a simple batch fermentation using glycerol as a carbon source and lactose as an acceptor. In order to use glucose as a carbon source, the chromosomal ptsG gene considered as the main regulator of the glucose repression mechanism was disrupted. The resulting E. coli strain of ∆LP-YA+FT showed much lower performance of 3-FL production (4.50 g/L) than the ∆L-YA+FT strain grown in a glycerol-medium (10.7 g/L), suggesting that glycerol is a better carbon source than glucose. Finally, the engineered E. coli ∆LW-YA+FT expressing the essential genes for 3-FL production and blocking the colanic acid biosynthetic pathway (∆wcaJ) exhibited the highest concentration (11.5 g/L), yield (0.39 mol/mol) and productivity (0.22 g/L-h) of 3-FL in a glycerol-limited fed-batch fermentation. This article is protected by copyright. All rights reserved.
This article was published in the following journal.
Name: Biotechnology journal
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