Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (32)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Priem, B.
Right arrow Articles by Samain, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Priem, B.
Right arrow Articles by Samain, E.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Glycobiology, 2002, Vol. 12, No. 4 235-240
© 2002 Oxford University Press

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

Bernard Priem2, Michel Gilbert3, Warren W. Wakarchuk3, Alain Heyraud2 and Eric Samain1,2

2Centre de Recherches sur les Macromolécules Végétales, CNRS (affiliated with the Joseph Fourier University) BP 53, 38041 Grenoble cedex 9 France, and 3Institute for Biological Sciences, NRCC, Ottawa, Ontario, K1A 0R6, Canada

When fed to a ß-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 ß1,3 N acetyl glucosaminyltransferase lgtA gene of Neisseria meningitidis resulted in the synthesis of 6 g · L–1 of the expected trisaccharide (GlcNAcß1-3Galß1-4Glc). When the ß1,4 galactosyltransferase lgtB gene of N. meningitidis was coexpressed with lgtA, the trisaccharide was further converted to lacto-N-neotetraose (Galß1-4GlcNAcß1-3Galß1-4Glc) and lacto-N-neoheaxose with a yield higher than 5 g · L–1. In a similar way, the nanA– E. coli strain that was devoid of NeuAc aldolase activity accumulated NeuAc on induction of the NanT permease and the lacZ– nanA– strain that overexpressed the N. meningitidis genes of the {alpha}2,3 sialyltransferase and of the CMP-NeuAc synthase efficiently produced sialyllactose (NeuAc{alpha}2-3Galß1-4Glc) from exogenous NeuAc and lactose.

1 To whom correspondence should be addressed


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 GlycobiologyHome page
E. Yavuz, S. Drouillard, E. Samain, I. Roberts, and B. Priem
Glucuronylation in Escherichia coli for the bacterial synthesis of the carbohydrate moiety of nonsulfated HNK-1
Glycobiology, February 1, 2008; 18(2): 152 - 157.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.