ACS OMEGA, 11, 32, 47335-47345 (2026)

IF 5,2

Identification of a Novel Fungal α-L-Fucosidase with Transfucosylation Potential

Pavlína Nekvasilová, Michaela Glozlová, Andrea Vopálenská, Lucie Petrásková, Natalia Kulik, Pavla Bojarová

 Abstract

Fucosylated carbohydrates are a vital part of human nutrition. They act as prebiotics, nourishing beneficial gut bacteria and helping shape the gut microbiome. Enzymatic synthesis is a convenient method to access these molecules. Fungal α-L-fucosidases are glycoside hydrolases that naturally cleave terminal α-linked fucose residues from glycans; those with synthetic capabilities are conveniently applicable in glycoengineering. This study investigates the fucosylation potential and regioselectivity of rare GH29 α-L-fucosidases from filamentous fungi. The screening of production of putative α-L-fucosidases by fungal strains using various inducers was combined with in silico analysis. Recombinant α-L-fucosidases were produced on a large scale and characterized with respect to their substrate specificities and pH optima. A novel transfucosylating α-L-fucosidase from Aspergillus phoenicis was thus identified and characterized. It was capable of regioselective formation of an α-(1 → 2)-linked fucosylated product. These findings highlight the potential of selected fungal α-L-fucosidases as promising tools for glycoengineering of fucosylated carbohydrates.

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