|Related Categories||1.1.x.x Acting on hydroxyl groups, 1.x.x.x Oxidoreductases, Application Index, Biochemicals and Reagents, Diagnostic and Analytical Enzymes,|
|foreign activity||Catalase ≤10 Sigma units/mg protein|
|galactose oxidase 0.5 - 4.0%|
Protein determined by biuret.
Glucose oxidase is widely used in the food and pharmaceutical industries1 as well as a major component of glucose biosensors.2
Glucose oxidase catalyses the oxidation of β-d-glucose to d-glucono-β-lactone and hydrogen peroxide, with molecular oxygen as an electron acceptor.3,4
One unit will oxidize 1.0 μmole of β-
Molecular Weight: 160 kDa (gel filtration)
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
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-
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
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Type X-S, lyophilized powder, 100,000-250,000 units/g solid (without added oxygen)
Type II, ≥15,000 units/g solid (without added oxygen)
Type VII, lyophilized powder, ≥100,000 units/g solid (without added oxygen)
2,000-10,000 units/g solid (without added oxygen)
lyophilized, powder, ~200 U/mg
Certificate of Analysis
Certificate of Origin
|Precautionary statements||P261-P342 + P311|
|Personal Protective Equipment||dust mask type N95 (US), Eyeshields, Faceshields, Gloves|
|Hazard Codes (Europe)||Xn|
|Risk Statements (Europe)||42|
|Safety Statements (Europe)||22-45|
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
1. Elsevier Applied Science W.M. Fogarty & C.T. Kelly, Eds, Microbial Enzymes and Biotechnology, 177-226, (1990)
2. Flow-injection system with glucose oxidase immobilized on a tubular reactor for determination of glucose in blood samples A.C. Ayupe de Oliveira et al. Anal. Chim. Acta 535, 213-217, (2005)
3. Optimization of glucose oxidase synthesis in submerged cultures of Aspergillus niger G-13 mutant J. Rogalski et al. Enzyme Microb. Technol. 10, 508-511, (1988)
4. The production of glucose oxidase using the waste myceliums of Aspergillus niger and the effects of metal ions on the activity of glucose oxidase T. Lu et al. Enzyme Microb. Technol. 19, 339-342, (1996)
Reductive Activation Of The Prodrug 1,2-bis(methylsulfonyl)-1-(2-chloroethyl)-2-[[1-(4-nitrophenyl)ethoxy]carbonyl]hydrazine (KS119) Selectively Occurs In Oxygen-deficient Cells And Overcomes O(6)-alkylguanine-DNA Alkyltransferase Mediated KS119 Tumor Cell Resistance. Baumann, R.P., et al. Biochem. Pharmacol. 79, 1553-61, (2010)
Glucose transforming enzymes A. Crueger, W. Crueger Microbial Enzymes and Biotechnology, (1990), 177-226
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