Crystallographic and catalytic study of α-l-fucosidase from Paenibacillus thiaminolyticus

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

1Department of Biochemistry and Microbiology, University of Chemistry and Technology,Prague, Technicka 5, 166 28 Praha 6, Czech Republic

2Institue of Macromolecular Chemistry,Heyerovského nam.2, 162 06 Praha 6-Břevnov, Czech Republic


Fucosylated oligosaccharides have an important role in many biological processes such as fertilization, cell adhesion, cell proliferation and processes of inflammation. They are also responsible for existence of blood group antigens. They can also be used in pharmaceutical and food industry. Previous research indicates that α-l-fucosidase from Paenibacillus thiaminolyticus has great potential for artificial fucosylation which could be used in synthetizing of fucosylated oligosaccharides. Recombinant form of α-l-fucosidase was produced, purified and characterized. Preliminary test of substrate specificity was conducted using selected substrates and ability to catalyze transglycosylation reactions was tested. Recombinant α-l-fucosidase was used for crystallization experiments. Conditions for crystal growth were found.


The project was supported by COST actions MultiGlycoNano (CM1102, LD13024). Participation at the conference is supported by specific university research (MSMT No 20/2015, No MSMT 21/2015).