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A2264

Sigma-Aldrich

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

ammonium sulfate suspension, ≥10 units/mg protein

Synonym(s):

β-N-Acetyl-D-hexosaminide N-acetylhexosaminohydrolase, β-N-Acetylhexosaminidase

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Canavalia ensiformis

Quality Level

form

ammonium sulfate suspension

specific activity

≥10 units/mg protein

foreign activity

α- and β-galactosidase, and α-L-fucosidase ≤0.1%
α-mannosidase ≤0.2%

storage temp.

2-8°C

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Application

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 .

Biochem/physiol Actions

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.

Unit Definition

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.

Physical form

Suspension in 2.5 M (NH4)2SO4, pH 7.0

Analysis Note

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.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Mohammed A Al-Fattani et al.
Journal of medical microbiology, 55(Pt 8), 999-1008 (2006-07-20)
Matrix material was extracted from biofilms of Candida albicans and Candida tropicalis and analysed chemically. Both preparations contained carbohydrate, protein, hexosamine, phosphorus and uronic acid. However, the major component in C. albicans matrix was glucose (32%), whereas in C. tropicalis
T Berger et al.
Journal of reproduction and fertility, 86(2), 559-565 (1989-07-01)
An assay to determine the binding of pig spermatozoa to the zona pellucida (ZP) of pig oocytes was developed using conditions compatible with in-vitro fertilization of pig eggs and with pig sperm penetration of zona-free hamster ova. These conditions were
Chaeyoung Kim et al.
Neurobiology of aging, 34(1), 275-285 (2012-04-17)
Deposition of β-amyloid (Aβ) as senile plaques and disrupted glucose metabolism are two main characteristics of Alzheimer's disease (AD). It is unknown, however, how these two processes are related in AD. Here we examined the relationship between O-GlcNAcylation, which is
Studies on the glycosidases of jack bean meal. 3. Crystallization and properties of beta-N-acetylhexosaminidase.
S C Li et al.
The Journal of biological chemistry, 245(19), 5153-5160 (1970-10-10)
Motoshi Ouchi et al.
Journal of clinical laboratory analysis, 26(6), 473-480 (2012-11-13)
Urinary N-acetyl-β-D-glucosaminidase (NAG) excretion is increased in patients with impaired glucose tolerance (IGT). This study investigated when during the oral glucose tolerance test (OGTT) the plasma glucose, urine glucose, and insulin levels correlate most strongly with urinary N-acetyl-β-d-glucosaminidase (NAG) levels

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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