A new fermentation process allows large-scale production of human milk oligosaccharides by metabolically engineered bacteria.

@article{Priem2002ANF,
  title={A new fermentation process allows large-scale production of human milk oligosaccharides by metabolically engineered bacteria.},
  author={B. Priem and M. Gilbert and W. Wakarchuk and A. Heyraud and E. Samain},
  journal={Glycobiology},
  year={2002},
  volume={12 4},
  pages={
          235-40
        }
}
When fed to a beta-galactosidase-negative (lacZ(-)) Escherichia coli strain that was grown on an alternative carbon source (such as glycerol), lactose accumulated intracellularly on induction of the lactose permease. We showed that intracellular lactose was efficiently glycosylated when genes of glycosyltransferase that use lactose as acceptor were expressed. High-cell-density cultivation of lacZ(-) strains that overexpressed the beta 1,3 N acetyl glucosaminyltransferase lgtA gene of Neisseria… Expand
Galactose-limited fed-batch cultivation of Escherichia coli for the production of lacto-N-tetraose.
TLDR
A large-scale synthesis of lacto-N-tetraose was demonstrated using fed-batch cultivation with galactose as sole energy and carbon source and the influence of the carbon source on the formation of lactosaccharide structures and on the intracellular availability of the glycosyltransferase substrates was investigated. Expand
Large scale in vivo synthesis of globotriose and globotetraose by high cell density culture of metabolically engineered Escherichia coli.
Large amounts of globotriose (Galalpha-4Galbeta-4Glc) are shown to be produced by the high cell density culture of an Escherichia coli strain over-expressing the Neisseria meningitidis lgtC gene forExpand
Metabolic engineering of Escherichia coli for the production of Lacto-N-neotetraose (LNnT)
Lacto-N-neotetraose (LNnT), one of the most important human milk oligosaccharides, can be used as infants’ food additives. Nowadays, extraction, chemical and biological synthesis were utilized toExpand
Glucuronylation in Escherichia coli for the bacterial synthesis of the carbohydrate moiety of nonsulfated HNK-1.
TLDR
The catalytic domain of mouse glucuronyl transferase GlcAT-P was cloned and expressed in an engineered strain which performed the in vivo synthesis of neolactotetraose, and the final glucurONYlated oligosaccharides are precursors of the brain carbohydrate motif HNK-1, involved in neural cell adhesion. Expand
Genetic engineering of Escherichia coli for the economical production of sialylated oligosaccharides.
We have previously described a microbiological process for the conversion of lactose into 3'sialyllactose and other ganglioside sugars by living Escherichia coli cells expressing the appropriateExpand
Synthesis of fucosylated lacto-N-tetraose using whole-cell biotransformation.
TLDR
A microbial conversion of lactose, D-glucose and L-fucose to fucosylated lacto-N-tetraose by growing Escherichia coli cultures is presented. Expand
Modular pathway engineering of key precursor supply pathways for lacto-N-neotetraose production in Bacillus subtilis
TLDR
It is shown that the LNnT biosynthesis could be significantly increased by optimizing enzymes expression levels and modular pathway engineering for balancing the precursors supply in B. subtilis. Expand
Genetic engineering of Escherichia coli for the production of NI,NII-diacetylchitobiose (chitinbiose) and its utilization as a primer for the synthesis of complex carbohydrates.
Chitinbiose was produced at more than 4 g L-1 by a high cell density culture of an Escherichia coli strain that co-expressed the rhizobial chitinoligosaccharide synthase gene nodC and a truncatedExpand
Production of human milk oligosaccharides by enzymatic and whole-cell microbial biotransformations.
TLDR
In view of an industrial production of HMOs, the whole cell biotransformation is at this stage the most promising option to provide human milk oligosaccharides as food additive. Expand
Synthesis of α-galactosyl epitopes by metabolically engineered Escherichia coli.
TLDR
The replacement of LgtA by a more specific β-1,3-N-acetylglucosaminyltransferase from H. pylori prevented the formation of these unwanted compounds and allowed the successful formation of the Galili pentasaccharide and longer α-Gal epitopes. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 17 REFERENCES
The living factory: In vivo Production of N-acetyllactosamine containing carbohydrates in E. coli
TLDR
The compound was found to be an acceptor in vitro for βGal( 1,4)GlcNAc α(1,3)galactosyltransferase, which suggests that the expression of additional glycosyltransferases in E. coli will allow the production of more complex oligosaccharides. Expand
Large-scale production of UDP-galactose and globotriose by coupling metabolically engineered bacteria
TLDR
The strategy of producing sugar nucleotides by combining metabolically engineered recombinant E. coli with a nucleoside 5′-triphosphate producing microorganism, and the concept of producing oligosaccharides by coupling sugar nucleotide production systems with glycosyltransferases, can be applied to the manufacture of other sugarucleotides and oligosACcharides. Expand
Gram-scale synthesis of recombinant chitooligosaccharides in Escherichia coli.
TLDR
Cultivation of Escherichia coli harbouring heterologous genes of oligosaccharide synthesis is presented as a new method for preparing large quantities of high-value oligosACcharides and its utilisation as a precursor for the preparation of synthetic nodulation factors by chemical acylation is tested. Expand
Large-scale production of N-acetyllactosamine through bacterial coupling.
A large-scale production system of N-acetyllactosamine, a core structure of various oligosaccharides, was established by a whole-cell reaction through the combination of recombinant Escherichia coliExpand
Large-scale production of CMP-NeuAc and sialylated oligosaccharides through bacterial coupling
TLDR
The production of 3′-sialyllactose at a 5-l jar fermenter scale was almost the same as that at a beaker scale, which indicated the high potential of the 3′, sialyloligosaccharide production on an industrial scale. Expand
Functional Relationships of the Genetic Locus Encoding the Glycosyltransferase Enzymes Involved in Expression of the Lacto-N-neotetraose Terminal Lipopolysaccharide Structure in Neisseria meningitidis*
The biosynthetic function of the lgtABE genetic locus of Neisseria meningitidis was determined by structural analysis of lipopolysaccharide (LPS) derived from mutant strains and enzymic assay forExpand
Production of O-acetylated and sulfated chitooligosaccharides by recombinant Escherichia coli strains harboring different combinations of nod genes.
TLDR
High cell density cultivation of recombinant Escherichia coli strains harboring the nodBC genes and substituted chitooligosaccharides obtained as tetramers are extended to the production of sulfated and O-acetylated derivatives of these two compounds, which should be useful precursors for the preparation of Nod factor analogues by chemical modification. Expand
Cloning of the Lipooligosaccharide α-2,3-Sialyltransferase from the Bacterial Pathogens Neisseria meningitidis and Neisseria gonorrhoeae*
TLDR
This study is the first example of the cloning, expression, and examination of α-2,3-sialyltransferase activity from a bacterial source. Expand
Oligosaccharides in human milk: structural, functional, and metabolic aspects.
TLDR
Research on HMOs is certainly needed to increase the knowledge of infant nutrition as it is affected by complex oligosaccharides, but more is needed to know about the metabolism of oligosACcharides in the gastrointestinal tract. Expand
Large-scale production of oligosaccharides using engineered bacteria.
TLDR
The large-scale production of oligosaccharides using either glycosyltransferases isolated from engineered microorganisms or whole cells as an enzyme source could promote a new era in the field of carbohydrate synthesis. Expand
...
1
2
...