Recombinant Whole Cells as Catalysts for the Enzymatic Synthesis of Oligosaccharides and Glycopeptides

✍ Scribed by Guido F. Herrmann; Peng Wang; Gwo-Jenn Shen; Chi-Huey Wong

• Publisher: John Wiley and Sons
• Year: 1994
• Tongue: English
• Weight: 279 KB
• Volume: 33
• Category: Article
• ISSN: 0044-8249
• DOI: 10.1002/anie.199412411

✦ Synopsis

Syntheses of oligosaccharides" using isolated glycosidases[" or glycosyl transferdse~,~~] or a combination of both,L4] have been studied extensively during the last decade. A general limitation of this methodology is the low availability and the high cost of glycosyl transferases, though some glycosyl transferases can be obtained in sufficient amounts for synthesis by cloning and overexpression.l'] Recently we reported on the expression of a cloned r-I .2-mannosyl transferase ( r -I ,2-ManT) in E. coli XLI-Blue strain at the level of = 1 U L-' for use in the mannosylation of saccharides and glycopeptides.[6] Since isolation of the enzyme and other glycosyl transferases in general is not trivial. we decided to exploit the feasibility of using whole cells of the recombinant E. coli as catalysts. Although biotransformations based on whole cells such as bakers' yeast"] are common, no example has been reported in which recombinant cells are used for glycosyl transfer reactions. To demonstrate the feasibility of the concept, we examined several acceptors for the enzymatic mannosylation reaction with GDP-Man as mannosyl donor (Fig. 1).