This sialidase has a 260-fold kinetic preference for the α2,3 sialyl linkage. The enzyme efficiently cleaves sialyl groups from glycoproteins and glycolipids. It may not release sialic acid from O-linked oligosaccharides on glycoproteins.

This enzyme specifically hydrolyzes oligosaccharides with type I chains and produces lacto-N-biose (Galb-3GlcNAc). It does not hydrolyze oligosaccharides with type II chain. The structure of the substrate essential for the enzyme activity is the terminal lacto-N-biosyl residue (Galb1-3GlcNAc). The enzyme does not hydrolyze a 2,3-sialyllacto-N-tetraose, lacto-N-fucopentaose I and II. One vial of this product (100 μl) allows 50–100 reactions of enzyme digestion of sugar chain up to 10 pmol.

This enzyme catalyses the hydrolytic cleavage of α-fucoside bonds and releases L-fucose. This enzyme specifically cleaves α1, 3- and α1, 4-fucoside bonds. It also releases L-fucose from α1-acid glycoprotein.