Trehalose analogue, non-reducing dissacharide of 1α-D-glucopyranosyl α-D-galactopyranoside, was synthesized by Pyrococcus horikoshii glycosyltransferase transglycosylation reaction with sugar nucleotides and galactose. This disaccharide analogue was effective inhibitor for several disaccharidases including rat intestinal trehalase and sucrase. Trehalose was also modified by Escherichia coli β-galactosidase transglycosylation reaction with lactose to give trehalose trisaccharide analogues. These trisaccharide analogues have been supposed to be indigestible oligosaccharides exhibiting enhanced hygroscopic, cryoprotective, anti-cariogenic, and prebiotic effects. The enzymatic techniques using glycosyltransferase and glycosidase might lead to create more trehalose-based analogues with a wide variety of acceptor and donor sugars.
|Title of host publication||Carbohydrate-Active Enzymes|
|Subtitle of host publication||Structure, Function and Applications|
|Number of pages||8|
|Publication status||Published - 2008 Sep|
Bibliographical noteFunding Information:
We thank for financial support from the Marine and Extreme Genome Research Center Program, Ministry of Maritime Affairs and Fisheries, Republic of Korea.
All Science Journal Classification (ASJC) codes
- Agricultural and Biological Sciences(all)
- Biochemistry, Genetics and Molecular Biology(all)