Production of α-Galactosyl epitopes via combined use of two recombinant whole cells harboring UDP-galactose 4-epimerase and α-1,3-galactosyltransferase

Xi Chen, Wei Zhang, Jianqiang Wang, Jianwen Fang, Peng George Wang

Research output: Contribution to journalArticle

23 Scopus citations


α-Galactosyl epitopes (or α-Gal, oligosaccharides with a terminal Galα1,3Gal sequence) are a class of biologically important oligosaccharides in great demand in bulk quantities for basic and clinical studies on preventing hyperacute rejection in pig-to-primate organ xenotransplantaion. A truncated bovine α-1,3-galactosyltransferase, the key enzyme responsible for the biosynthesis of the terminal structure of α-Gal, was cloned and overexpressed previously. The acceptor specificity was further studied in the present paper, and lactose and galactose derivatives were found to be good acceptors. To develop a more proficient reaction process, we report herein an example of an efficient enzymatic synthesis of α-Gal oligosaccharides catalyzed by the combination of two recombinant Escherichia coli whole cells harboring the genes of a UDP-galactose 4-epimerase and the α-1,3-galactosyltransferase, respectively. Using lactosyl azide (LacN3) as the acceptor for the glycosyltransferase, the combined use of the two recombinant cells efficiently produced α-Gal epitope Galα1,3LacN3 in 60-68% yield.

Original languageEnglish (US)
Pages (from-to)595-599
Number of pages5
JournalBiotechnology Progress
Issue number4
StatePublished - Jul 2000
Externally publishedYes


ASJC Scopus subject areas

  • Food Science
  • Biotechnology
  • Microbiology

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