72358-28-2

Upstream product

• 133-89-1 UDP-glucose 
• 14200-67-0 N,N'-diacetylchitobiose 
• 2956-16-3 uridine 5'-diphospho-D-galactose 
• 3150-24-1 4-nitrophenyl-β-D-galactopyranoside 
• 14200-67-0 (GlcNAc)2 

Relevant academic research and scientific papers

β-glucosylation of chitooligomers by galactosyltransferase

Galactosyltransferase from bovine milk was found to be able to utilise UDP-Glc to transfer Glc onto GlcNAc and chitooligomers [-β-GlcNAc-(1 → 4)- ](n), n = 2-4. β-Glucosylated products were used in binding studies with NKR-P1A protein cloned from rat natural killer cells.

Enzymatic galactosylation of cello- and chito-oligomers

Terminal galactosylations of cello- and chito-oligomers are studied employing galactosyltransferase with and without α-lactalbumin. The lactose synthase complex allows just for galactosylation of cellobiose in lower yield but not for higher cello-oligomers. In contrast, the affinity in galactosylation of chito-oligomers increases with higher members to reach the maximum at chitohexaose with only a 30% reduction in transfer rate. In addition to kinetic data, preparative studies with a number of acceptor substrates gave galactosylated oligosaccharides in high yields. (Figure Presented). Copyright Taylor & Francis Group, LLC.

Galactosidase-assisted synthesis en route to type I and type II structures of chitooligomers1

Transgalactosylation of chitobiose and chitotriose led to formation of terminally (β1-3)- and (β1-4)-galactosylated chitooligosaccharides ready for fucosylation to give Lewisa and Lewisx motifs. Their structures could be assigned emp

Synthesis of galactose-terminated oligosaccharides by use of galactosyltransferase

Galactosyltransferase catalyzes the galactosylation of oligosaccharides terminated by glucose and by 2-acetamido-2-deoxy glucopyranose, respectively. Variations concerning the acceptor substrate as well as the donor substrate are described.