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Glucose Oxidase from Aspergillus niger

greener alternative

Type X-S, lyophilized powder, 100,000-250,000 units/g solid (without added oxygen)

G.Od., β-D-Glucose:oxygen 1-oxidoreductase, GOx
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:


Type X-S


lyophilized powder

specific activity

100,000-250,000 units/g solid (without added oxygen)

mol wt

160 kDa


Protein, ≥65%

greener alternative product characteristics

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.


diagnostic assay manufacturing

foreign activity

Catalase ≤5 units/mg protein

greener alternative category


storage temp.


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General description

We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in fuel cell research. For more information see the article in biofiles.
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.
Mass of glucose oxidase (GOX), a flavoprotein ranges from approximately 130 to 175 kDa. Some fungi and insects are capable of producing GOX.


Glucose Oxidase from Aspergillus niger has been used:
  • in the (glucose oxidase) GO reagent to measure the glucose content by the glucose oxidase (GO) method
  • to activate the human renal carcinoma cell line for constructing the oxidative stress model
  • to study its influence in the paste on the analytical performance of the bioelectrode

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


10000, 50000, 250000, 1000000, 2500000 units in poly bottle

Biochem/physiol Actions

Glucose oxidase (GOX) oxidizes D-glucose to D-gluconolactone and hydrogen peroxide. Hydrogen peroxide, the catalytic product of GOX, serves as an anti-bacterial and anti-fungal agent. It is safe and can be used in several industrial applications like baking, dry egg powder production, wine production, gluconic acid production, etc. It possesses electrochemical activity, which makes it extremely important in glucose sensors and in fuel cell applications.
Glucose oxidase catalyses the oxidation of β-d-glucose to d-glucono-β-lactone and hydrogen peroxide, with molecular oxygen as an electron acceptor.


May contain traces of amylase, maltase, glycogenase, invertase, and galactose oxidase.

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%.

Analysis Note

Protein determined by biuret


Health hazard

Signal Word


Hazard Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids



Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificate of Analysis

Enter Lot Number to search for Certificate of Analysis (COA).

Certificate of Origin

Enter Lot Number to search for Certificate of Origin (COO).

Product Information Sheet

Technical Information

More documents

Quotes and Ordering

  1. Which document(s) contains shelf-life or expiration date information for a given product?

    If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

  2. How do I get lot-specific information or a Certificate of Analysis?

    The lot specific COA document can be found by entering the lot number above under the "Documents" section.

  3. What buffer is used during the preparation of Glucose oxidase, Product G7141?

    Glucose oxidase contains potassium phosphate and tris acetate salts (which were present in the lyophilization buffer).

  4. Is Glucose oxidase, Product G7141, inhibited by sodium azide, phenol, heparin, citrate or EDTA?

    Glucose oxidase is not inhibited by sodium azide (1.5 mM), low concentrations of phenol (10 mM), heparin, citrate or EDTA.

  5. How should solutions of Glucose oxidase, Product G7141, be stored?

    No solution stability studies have been performed by Sigma.  However, we would expect solutions prepared in buffer in the pH range of 5-7 to be stable at 2-8°C for at least one week.  For longer term storage, solutions can be stored as frozen aliquots at -20°C (only one freeze/thaw cycle) for at least 6 months.

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  7. What is the Department of Transportation shipping information for this product?

    Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product. 

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Raluca-Elena Munteanu et al.
Scientific reports, 9(1), 15196-15196 (2019-10-28)
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Luque GL, et al.
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Interspecies Interactions Determine the Impact of the Gut Microbiota on Nutrient Allocation in Drosophila melanogaster
Newell PD, et al.
Applied and Environmental Microbiology, 80(2), 788-796 (2014)
Ectopic Expression of Human MutS Homologue 2 on Renal Carcinoma Cells Is Induced by Oxidative Stress with Interleukin-18 Promotion via p38 Mitogen-activated Protein Kinase (MAPK) and c-Jun N-terminal Kinase (JNK) Signaling Pathways
Mo C, et al.
The Journal of Biological Chemistry, 287(23), 19242-19254 (2012)
Glucose oxidase-An overview
Biotechnology Advances, 27(4), 489-501 (2009)

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