β-N-Acetylglucosaminidase from Canavalia ensiformis (Jack bean)

β -N-acetylglucosaminidase is a lysosomal enzyme used to hydrolyze N-acetyl-β-D-glucosaminides and N-acetyl-β-Dgalactosaminides. It is used in chemoenzymatic synthesis of oligosaccharides based on their effective transglycosylation of β-GlcNAc and β-GalNAcc. It may be a useful tool to study Alzheimer′s Disease . Acetylglucosaminidase from Canavalia ensiformis has been used to study enzymic detachment of biofilms .

This enzyme, sometimes called β-N-acetylhexosaminidase, is reported to liberate terminal β-linked N-acetylglucosamine and N-acetylgalactosamine from a variety of substrates. The activity of β-N-actylglucosaminidase may be determined with the chromogenic substrate p-nitrophenyl-N-acetyl-β-D-glucosaminide. β-N-actylglucosaminidase hydrolyzes the terminal nonreducing N-acetyl-D-hexosamine residues. This enzyme contains two predominant isozymes, Hex A, a heterodimer, and Hex B, a homodimer. N-acetylglucosamine, acetamide, N-2-acetamido-2-deoyglucosylamine, N-acetylnojirimycin, and N-acetyldeoxynojirmycin are known inhibitors.

This enzyme, sometimes called β-N-acetylhexosaminidase, is reported to liberate terminal β-linked N-acetylglucosamine and N-acetylgalactosamine from a variety of substrates.

One unit will hydrolyze 1.0 μmole of p-nitrophenyl N-acetyl-β-D-glucosaminide to p-nitrophenol and N-acetyl-D-glucosamine per min at pH 5.0 at 25 °C.

Suspension in 2.5 M (NH₄)₂SO₄, pH 7.0

At pH 4.0, p-nitrophenyl β-N-acetylgalactosaminide is hydrolyzed at approximately 50% of the rate of hydrolysis of p-nitrophenyl β-N-acetylglucosaminide at pH 5.0.