β(1-2,3,4,6)-N-acetylglucosaminidase [For Glycan Release] (CAT#: CB-P268-K) Datasheet

Kit

N-acetylglucosaminidase cleaves all non-reducing terminal β-linked N-acetylglucosamine residues from complex carbohydrates and glycoproteins.

The cleavage rate of the different bonds of GlcNAc on two-antenna, three-antenna, and four-antenna oligosaccharides largely depends on the steric hindrance of adjacent residues. Β(1-2) GlcNAc residues linked to β(1-3)-linked mannose are cleaved at the highest rate, while β(1-2) residues linked to β(1-6)-linked mannose) GlcNAc residues were cleaved at the highest rate in 2000. All three oligosaccharides have the lowest ratios. β(1-6)GlcNAc residues (if present) are removed at the second highest rate, while β(1-4)GlcNAc is removed at the third highest rate. On the three-antenna structure, the residue is removed at the second highest rate. The bisected β(1-4)GlcNAc linked to β-linked mannose severely hinders the cleavage of other GlcNAc residues-cleavage requires high concentrations of enzymes and prolonged incubation time.

Source: Recombinant from Streptococcus pneumoniae in E. Coli.

EC: 3.2.1.52

Alternate Names: β-N-acetylglucosaminidase, N-acetyl-β-d-glycosaminide N-acetylglucosaminohydrolase, glucosaminidase, hexosaminidase

Specific Activity:>80 U/mg
Activity:>50 U/mL

Molecular weight: ~140,000 daltons

pH range: 5-7, optimum 5.0

Specificity: Cleaves all non-reducing terminal β-linked N-acetylglucosamine. Bisecting GlcNAc slows the reaction.

Specific Activity Assay: Defined as the amount of enzyme required to produce 1 µmole of p-nitrophenol (pNP) in 1 minute at 37°C, pH 5.0 from p-nitrophenyl-β-D-N-acetyl-glucosaminide

N-acetylglucosaminidase cleaves all non-reducing terminal β-linked N-acetylglucosamine residues from complex carbohydrates and glycoproteins.