Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10234728 | Metabolic Engineering | 2005 | 7 Pages |
Abstract
Chitinbiose was produced at more than 4 g Lâ1 by a high cell density culture of an Escherichia coli strain that co-expressed the rhizobial chitinoligosaccharide synthase gene nodC and a truncated form of the chitinase gene chiA which has been designed to be functionally produced in the E. coli cytoplasm. Chitinpentaose, which has previously been shown to be produced by the nodC protein in growing E. coli, was formed as an intermediate that was subsequently hydrolyzed into chitinbiose by the chitinase encoded by chiA. Chitinbiose was mainly recovered in the extracellular medium and to prevent its catabolism, the genes for the chitinbiose PTS permease had to be disrupted. When the additional gene lgtB for β1,4-galactosyltransferase was expressed, intracellular chitinbiose was converted into the trisaccharide Galβ-4GlcNAcβ-4GlcNAc which could serve as acceptor for glycosyltransferase that recognize the terminal N-acetyllactosamine structure.
Keywords
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Sylvain Cottaz, Eric Samain,