Líffræðifélag Íslands
Líffræðiráðstefnan 2015
Erindi/veggspjald / Talk/poster E38
Guðmundur Hreggviðsson (1,2) Jon Oskar White (3), Olafur H. Friðjónsson (2), Justyna Dobruchowska (4), Hans Kamerling (5,6)
1. University of Iceland, 2. Matís ohf, 3. Orf Líftækni hf, 4. University of Georgia, Athens 5. University of Utrecht, 6. University of Groningen
Kynnir / Presenter: Guðmundur Hreggviðsson
Tengiliður / Corresponding author: Guðmundur Hreggviðsson (gudmundo@matis.is)
Glycoside hydrolases enzymes of family GH17 from proteobacteria (genera Pseudomonas, Azotobacter) catalyze (β1→3)-, (β1→6)- or (β1→4)-elongation reactions with laminari-oligosaccharides. The cloning and expression of a gene encoding the GH17 domain of the NdvB enzyme from Bradyrhizobium japonicum, designated Glt20, as well as its catalytic properties are described and compared to homologous bacterial GH17 enzymes previously investigated by the authors. The Glt20 is distinctly different from these enzymes, both regarding substrate specificity and product formation. The Glt20 GH17 appears to be a true beta-glucan branching enzymes of industrial interest that can be used for producing potent bioactive beta-glucan oligosachharides or complex beta-glucan polysaccharides for different applications.