α1,6-Fucosidase, Chryseobacterium meningosepticum, Recombinant, E. coli

Note: 1 mU = 1 milliunit.

Recombinant, Chryseobacterium meningosepticum α1,6-fucosidase expressed in E. coli. This enzyme from Chryseobacterium (formerly Flavobacterium) meningosepticum catalyzes the hydrolysis of branched non-reducing terminal α1,6-linked fucose residues from the N-acetylglucosamine core of N-Linked oligosaccharides. The reducing terminus of the oligosaccharide must be covalently bonded to a reporter molecule, such as aminonaphthalene disulfonic acid (ANDSA), aminonaphthalene trisulfonate (ANTS), and 2-aminoanthanilic acid (2-AA). The one exception is that a terminal unbranched α1,3-fucose is cleaved in the absence of any reporter molecule. Does not cleave fucose from glycoproteins.

In 25 mM NaCl, 20 mM Tris-HCl, pH 7.5.

One unit is defined as the amount of enzyme that will release 1.0 µmol methylumbelliferone from 4-methylumbelliferyl-α-L-fucoside per min at 37°C, pH 5.0.

Zheng, Q., et al. 2002. J. Biol. Chem.277, 39823.

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Toxicity: Standard Handling (A)