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Medical Laboratory Reagents

Glucose Oxidase
CAS No. 9001-37-0     EC No.
From yeast cells with cloned gene encoding genetically engineered fungus Aspergillus niger glucose oxidase.
Catalog/Part No.    CT-GO-017
Synonyms -D-Glucose: oxygen 1- oxidoreductase, G.Od., GOx
pH range pH 4-7
optimum pH 4.5
Molecular Weight Approx.160 KDa
Storage Temperature -20 C for lyophilized powder
Form lyophilized powder
Temperature profile Optimum temperature 42C
Temperature range of enzyme activity: 40~50C
Specific activity = 45 U/mg lyophilized powder
Unit definition: One unit will oxidize 1.0 mole of -D-glucose to D-gluconolactone and H2O2 per min at pH 5.1 at 35 C, equivalent to an O2 uptake of 22.4 l per min. If the reaction mixture is saturated with oxygen, the activity may increase by up to 100%.
Activity = 45 U/mg lyophilized powder
Purity and Quality
Reagent Grade Diagnostic Reagent Grade(superior purity)
May contain traces of amylase, maltase, glycogenase, invertase, and galactose oxidase
Product Description
General Description Glucose oxidase is a well-characterised flavoprotein that catalyses oxidation of -D-Glucose at its first hydroxyl group, utilizing molecular oxygen as the electron acceptor, to produce D-glucono-delta-lactone and hydrogen peroxide. Glucose oxidase is a homodimeric enzyme, with an FAD molecule moncovalently but tightly bound at the active site of each 80 KDa subunit. The enzyme consists of two identical polypeptide chain subunits (80,000 Daltons) covalently linked by disulfide bonds. Each subunit contains one mole of Fe and one mole of FAD (flavin-adenine dinucleotide). The molecule consists of approximately 74% protein, 16% neutral sugar and 2% amino sugars. The FAD is replaceable with FHD (flavin-hypoxanthine dinucleotide) without loss of activity.
Advantages An important characteristic of A.niger-derived GOD is its very high substrate specificity for glucose, which makes it perfectly fits in enzymes application for measuring glucose in the presence of other sugars.
Recombinant production of glucose oxidase has resulted in lower price/unit charges of enzyme products that allows our customers to experience substantial cuts in cost.
Application: Diagnostic application: Glucose oxidase can be utilized in the enzymatic determination of D-glucose in solution. As glucose oxidase oxidizes -D-glucose to D-gluconolactate and hydrogen peroxide, horseradish peroxidase is often used as the coupling enzyme to visualize colorimetrically the formed hydrogen peroxide for the rapid determination of free glucose in samples.
Enzymatic glucose biosensors use an electrode instead of O2 to take up the electrons needed to oxidize glucose and produce an electronic current in proportion to glucose concentration, which is the technology behind the disposable glucose sensor strips used by diabetics to monitor serum glucose levels.
Food industrial application: Glucose oxidase assay allows the monitoring of glucose levels in fermentation and bioreactors. It also helps food preservation by removing oxygen from food, wine, beer packaging and bottling. Glucose oxidase is widely used to remove residual glucose to inhibit non-enzymatic browning.
Preparation Notes
Activators Glucose oxidase does not require any activator, but it is inhibited by Ag+, Hg2+, Cu2+, phenylmercuric acetate, and p-chloromercuribenzoate (pCMB). It is not inhibited by the nonmetallic SH reagents: N-ethylmaleimide, iodoacetate, and iodoacetamide.
Stability Lyophilized powder is stable for 3 years when stored below 4C.
Buffered aqueous glycerol solution is stable for 1 years when stored at -20C.
Transportation and Storage:
Buffered aqueous glycerol solution: transport with blue ice (below 4C ). Storage Recommended at -20C
lyophilized powder: transport at room temperature. Storage Recommended below 4C.
Storage buffer: 20 mM Tris-Cl (pH 8.0), 2 mM MgCl2, 20 mM NaCl, 50% glycerol.
Dilution buffer: 20 mM Tris-Cl (pH 8.0), 2 mM MgCl2, 20 mM NaCl.
Precautions and Disclaimer This product is for R&D use only, not for drug, household, or other uses.

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