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G6641 Sigma

Glucose Oxidase from Aspergillus niger

Type II-S, 15,000-50,000 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-S
form   powder
composition   , 20-40%
foreign activity   Catalase ≤10 Sigma units/mg protein
  Maltase ≤10%
  amylase ≤0.5%
  galactose oxidase 0.5 - 4.0%
  glycogenase ≤0.5%
  invertase ≤0.5%
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.

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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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

Documents

Certificate of Analysis

Certificate of Origin

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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