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G6125 Sigma

Glucose Oxidase from Aspergillus niger

Type II, ≥15,000 units/g solid (without added oxygen)

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

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Properties

Related Categories 1.1.x.x Acting on hydroxyl groups, 1.x.x.x Oxidoreductases, Application Index, Biochemicals and Reagents, Diagnostic and Analytical Enzymes,
type   Type II
form   powder
foreign activity   amylase ≤0.5%
  catalase ≤2 Sigma units/mg solid
  galactose oxidase ≤3%
  glycogenase ≤0.5%
  invertase ≤0.5%
  maltase ≤2%
storage temp.   −20°C

Description

Analysis Note

Protein determined by biuret.

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.

Caution

Some loss of activity may occur after more than 3 days at room temperature. This product may be shipped with or without dry ice.

Linkage

This preparation is formulated from Type VII, G2133, by addition of potassium gluconate.

Packaging

10000, 50000, 250000, 1000000 units in poly bottle

Unit Definition

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%.

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.

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Biomedical Applications
Safety & Documentation

Safety Information

Symbol 
GHS08  GHS08
Signal word 
Danger
Hazard statements 
Precautionary statements 
Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
1
RTECS 
RQ8452000
Protocols & Articles

Protocols

Enzymatic Assay of Glucose Oxidase

Derived from procedure SPGLUC01. Includes template updates to current SOP specification and incorporation of notes into the procedure. Refer to CR SOP-DEK ENZ 36.
Keywords: Extinction coefficient

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers
15

References

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