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Merck
CN

G0543

Glucose Oxidase from Aspergillus niger

≤0.1 units/mg protein catalase, buffered aqueous solution, pH 4.5, low catalase activity

Synonym(s):

β-D-Glucose:oxygen 1-oxidoreductase, G.Od., GOx

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About This Item

CAS Number:
UNSPSC Code:
12352204
EC Number:
MDL number:
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Product Name

Glucose Oxidase from Aspergillus niger, ≤0.1 units/mg protein catalase, buffered aqueous solution, pH 4.5, low catalase activity

InChI key

WQZGKKKJIJFFOK-VFUOTHLCSA-N

InChI

1S/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5-,6-/m1/s1

form

buffered aqueous solution

specific activity

≥200 units/mg protein

mol wt

160 kDa

composition

, ≥15 mg/mL

impurities

≤0.1 units/mg protein catalase

pH

4.5

storage temp.

2-8°C

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Application

Glucose oxidase is widely used in the food and pharmaceutical industries as well as a major component of glucose biosensors.

Biochem/physiol Actions

Glucose oxidase catalyses the oxidation of β-d-glucose to d-glucono-β-lactone and hydrogen peroxide, with molecular oxygen as an electron acceptor.

Disclaimer

For U.S. Customers: Contains mercury; Do not place in trash - dispose according to local, state, or federal laws.

General description

Molecular Weight: 160 kDa (gel filtration)
pI: 4.2
Extinction coefficient: E1% = 16.7 (280 nm)

Glucose oxidase from Aspergillus niger is a dimer consisting of 2 equal subunits with a molecular mass of 80 kDa each. Each subunit contains one flavin adenine dinulceotide moiety and one iron. The enzyme is a glycoprotein containing ~16% neutral sugar and 2% amino sugars. The enzyme also contains 3 cysteine residues and 8 potential sites for N-linked glycosylation.

Glucose oxidase is capable of oxidizing D-aldohexoses, monodeoxy-D-glucoses, and methyl-D-glucoses at varying rates.

The pH optimum for glucose oxidase is 5.5, while it has a broad activity range of pH 4-7. Glucose oxidase is specific for β-D-glucose with a KM of 33-110 mM.

Glucose oxidase does not require any activators, but it is inhibited by Ag+, Hg2+, Cu2+, phenylmercuric acetate, and p-chloromercuribenzoate. It is not inhibited by the nonmetallic SH reagents: N-ethylmaleimide, iodoacetate, and iodoacetamide.

Glucose oxidase can be utilized in the enzymatic determination of D-glucose in solution. As glucose oxidase oxidizes β-D-glucose to D-gluconolactate and hydrogen peroxide, horseradish peroxidase is often used as the coupling enzyme for glucose determination. Although glucose oxidase is specific for β-D-glucose, solutions of D-glucose can be quantified as α-D-glucose will mutorotate to β-D-glucose as the β-D-glucose is consumed by the enzymatic reaction.

Other Notes

One unit will oxidize 1.0 μmole of β-D-glucose to D-gluconolactone and H2O2 per min at pH 5.1 at 35 °C, equivalent to an O2 uptake of 22.4 μl per min. If the reaction mixture is saturated with oxygen, the activity may increase by up to 100%.

Physical form

Solution in 50 mM potassium phosphate, 100 mM sodium acetate, 250 mM KCl, with 0.004% thimerosal, pH 4.5.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter

Regulatory Information

常规特殊物品
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