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 Citations (Scopus)

Abstract

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
Volume16
Issue number4
DOIs
StatePublished - Jul 2000
Externally publishedYes

Fingerprint

UDPglucose 4-Epimerase
galactosyltransferases
Galactosyltransferases
Oligosaccharides
oligosaccharides
epitopes
Epitopes
azides
Glycosyltransferases
glycosyltransferases
Azides
cells
Lactose
Galactose
galactose
Primates
lactose
clinical trials
Swine
chemical derivatives

ASJC Scopus subject areas

  • Food Science
  • Biotechnology
  • Microbiology

Cite this

Production of α-Galactosyl epitopes via combined use of two recombinant whole cells harboring UDP-galactose 4-epimerase and α-1,3-galactosyltransferase. / Chen, Xi; Zhang, Wei; Wang, Jianqiang; Fang, Jianwen; Wang, Peng George.

In: Biotechnology Progress, Vol. 16, No. 4, 07.2000, p. 595-599.

Research output: Contribution to journalArticle

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abstract = "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.",
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AB - 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.

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