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

Toxicity: Standard Handling (A)

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.

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.

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

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