Andrea Martschini
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Andrea Martschini has a total of 3 co-authors. Here are the top co-authors by number of shared publications:
- Anja Kostelac
Food Biotechnology Laboratory, Department of Food Science and Technology, BOKU University, 1190 Vienna, Austria
1 shared publication - Clemens Karl Peterbauer
Department of Biotechnology and Food Sciences, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria
1 shared publication - Dietmar Haltrich
Laboratory of Food Biotechnology, Department of Biotechnology and Food Science, Universität für Bodenkultur (BOKU)-University, 1190 Vienna, Austria
1 shared publication
Latest Publications
- Open Access
- 26 November 2024
- Published by MDPI AG in Biomolecules
- Vol. 14 (12) , 1510
Characterization of a Pyranose Oxidase/C-Glycoside Oxidase from Microbacterium sp. 3H14, Belonging to the Unexplored Clade II of Actinobacterial POx/CGOx
Pyranose oxidase (POx) is an FAD-dependent oxidoreductase and belongs to the glucose–methanol–choline (GMC) superfamily of oxidoreductases. As recently reported, POxs and FAD-dependent C-glycoside oxidases (CGOxs) share the same sequence space, and phylogenetic analysis of actinobacterial sequences belonging to this shared sequence space showed that it can be divided into four clades. Here, we report the biochemical characterization of a POx/CGOx from Microbacterium sp. 3H14 (MPOx), belonging to the hitherto unexplored clade II of actinobacterial POx/CGOx. Overall, MPOx demonstrates comparable features to POxs/CGOxs of clades III and IV, including the preference for glycosides over monosaccharides as electron donors. However, as MPOx efficiently oxidizes the C-glycoside aspalathin as well as the O-glycoside phlorizin, it shows activity with yet another set of glycoside structures compared to other POx/CGOx members.
- 26 November 2024
- Published by MDPI AG in Biomolecules
- Vol. 14 (12) , 1510
Open AccessCharacterization of a Pyranose Oxidase/C-Glycoside Oxidase from Microbacterium sp. 3H14, Belonging to the Unexplored Clade II of Actinobacterial POx/CGOx
Pyranose oxidase (POx) is an FAD-dependent oxidoreductase and belongs to the glucose–methanol–choline (GMC) superfamily of oxidoreductases. As recently reported, POxs and FAD-dependent C-glycoside oxidases (CGOxs) share the same sequence space, and phylogenetic analysis of actinobacterial sequences belonging to this shared sequence space showed that it can be divided into four clades. Here, we report the biochemical characterization of a POx/CGOx from Microbacterium sp. 3H14 (MPOx), belonging to the hitherto unexplored clade II of actinobacterial POx/CGOx. Overall, MPOx demonstrates comparable features to POxs/CGOxs of clades III and IV, including the preference for glycosides over monosaccharides as electron donors. However, as MPOx efficiently oxidizes the C-glycoside aspalathin as well as the O-glycoside phlorizin, it shows activity with yet another set of glycoside structures compared to other POx/CGOx members.