Structural and catalytic properties of α-L-fucosidase from Paenibacillus thiaminolyticus

Terézia Kovaľová¹, Patricie Buchtová¹, Eva Benešová¹, Tomáš Kovaľ², Petra Lipovová¹

¹Department of Biochemistry and Microbiology, Institute of Chemical Technology,

Prague, Technická 3, Prague 6, 166 28, Czech Republic,

²Institute of Macromolecular Chemistry AS CR, v.v.i., Heyrovského nám. 2,
162 06 Prague 6, Czech Republic

α-l-Fucosidase is a glycosidase with ability to catalyze removal of α-l-fucose residues from the non-reducing terminus of glycoconjugates. This enzyme is also able to catalyze transglycosylation reactions. Fucosylated oligosaccharides have an important role in many biological processes, they can also be used in pharmaceutical and food industry. An application of enzymes could facilitate the process of synthesis of these compounds. Previous studies have shown that α-l-fucosidase from Paenibacillus thiaminolyticus may have great potential for synthesis of glycosylated molecules. Recombinant form of this enzyme was prepared. The protein was purified and characterized. Several sugar acceptors were tested in transglycosylation reactions. 3D-model of α-l-fucosidase will be prepared. Crystallization experiments will be carried out provided that a sufficient quantity and appropriate purity of this enzyme is obtained.

The project was supported by COST action MultiGlycoNano (CM1102, LD13024). Participation at the conference is supported by specific university research (MSMT No 21/2014).