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Enzymes for Research, Diagnostic and Industrial Use

Native Aspergillus niger Glucose Oxidase

Cat No.
NATE-0311
Description
The glucose oxidase enzyme (GOx) also known as notatin (EC number 1.1.3.4) is an oxido-reductase that catalyses the oxidation of glucose to hydrogen peroxide and D-glucono-δ-lactone. This enzyme is produced by certain species of fungi and insects and displays antibacterial activity when oxygen and glucose are present.
Abbr
GOD, Native (Aspergillus niger)
Alias
GOD; Gox
Source
Aspergillus niger
Applications
Glucose oxidase is widely used in the food and pharmaceutical industries as well as a major component of glucose biosensors.
Product Overview
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.
Form
Type I, buffered aqueous solution; Solution in 50 mM potassium phosphate, 100 mM sodium acetate, 250 mM KCl, with 0.004% thimerosal, pH 4.5; Type II, Type VI, lyophilized powder. Type V, Lyophilized powder containing phosphate buffer salts and sodium chloride
Enzyme Commission Number
EC 1.1.3.4
Activity
Type I, <0.1 units/mg protein; Type II, 100,000-250,000 units/g solid (without added oxygen); Type III, 2,000-10,000 units/g solid (without added oxygen); Type IV, 15,000-50,000 units/g solid (without added oxygen); Type V, > 100,000 units/g solid (without added oxygen); Type VI, ~200 units/mg; Type VII, > 15,000 units/g solid (without added oxygen).
CAS No.
9001-37-0
Contaminants
<0.1 units/mg protein catalase
Molecular Weight
160 kDa (gel filtration)
Isoelectric point
4.2
pH Stability
42467
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%.
Optimum pH
5.5
Storage
−20°C
Synonyms
EC 1.1.3.4; glucose oxyhydrase; corylophyline; penatin; glucose aerodehydrogenase; microcid; β-D-glucose oxidase; D-glucose oxidase; D-glucose-1-oxidase; β-D-glucose:quinone oxidoreductase; glucose oxyhydrase; deoxin-1; GOD; 9001-37-0; glucose oxidase enzyme; GOx; notatin; glucose oxidase
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