|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
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Keywords: Cell culture, Cell disruption, Cell signaling, Diagnostic, Digestions, Drug discovery, Functional genomics, Gene expression, Genomics, Metabolic Pathways, Molecular biology, Neuroscience, Proteomics
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)
An efficient fluorescent sensing platform for biomolecules based on fenton reaction triggered molecular beacon cleavage strategy. Hu R, Liu YR, Zhang XB, et al. Biosens. Bioelectron. 41, 442-5, (2013)
Size-tunable Pt nanoparticles assembled on functionalized ordered mesoporous carbon for the simultaneous and on-line detection of glucose and L-lactate in brain microdialysate. Yu Y, Yang Y, Gu H, et al. Biosens. Bioelectron. 41, 511-8, (2013)
Controllable growth of Prussian blue nanostructures on carboxylic group-functionalized carbon nanofibers and its application for glucose biosensing. Wang L, Ye Y, Zhu H, et al. Nanotechnology 23(45), 455502, (2012)
Graphene quantum dots as a new substrate for immobilization and direct electrochemistry of glucose oxidase: application to sensitive glucose determination. Razmi H and Mohammad-Rezaei R Biosens. Bioelectron. 41, 498-504, (2013)
Encapsulation of yeast displaying glucose oxidase on their surface in graphene oxide hydrogel scaffolding and its bioactivation. Bahartan K, Gun J, Sladkevich S, et al. Chem. Commun. 48(98), 11957-9, (2012)
Using thermally regenerable cerium oxide nanoparticles in biocomputing to perform label-free, resettable, and colorimetric logic operations. Lin Y, Xu C, Ren J, et al. Angew. Chem. Int. Ed. Engl. 51(50), 12579-83, (2012)
Modification of polypyrrole nanowires array with platinum nanoparticles and glucose oxidase for fabrication of a novel glucose biosensor. Xu G, Adeloju SB, Wu Y, et al. Anal. Chim. Acta 755, 100-7, (2012)
An aptamer-based biosensing platform for highly sensitive detection of platelet-derived growth factor via enzyme-mediated direct electrochemistry. Deng K, Xiang Y, Zhang L, et al. Anal. Chim. Acta 759, 61-5, (2013)
Incorporation of beta-sitosterol into the membrane increases resistance to oxidative stress and lipid peroxidation via estrogen receptor-mediated PI3K/GSK3beta signaling. Shi C, Wu F, Zhu XC, et al. Biochim. Biophys. Acta 1830(3), 2538-44, (2013)
Direct electron transfer type disposable sensor strip for glucose sensing employing an engineered FAD glucose dehydrogenase. Yamashita Y, Ferri S, Huynh ML, et al. Enzyme Microb. Technol. 52(2), 123-8, (2013)
Preparation and characterization of glucose oxidase nanoparticles and their application in dissolved oxygen metric determination of serum glucose. Kundu N, Yadav S, and Pundir CS J. Nanosci. Nanotechnol. 13(3), 1710-6, (2013)
Notatin: an anti-bacterial glucose-aerodehydrogenase from Penicillium notatum Westling and Penicillium resticulosum sp. nov. Coulthard CE, Michaelis R, Short WF, et al. Biochem. J. 39(1), 24-36, (1945)
Glucose transforming enzymes A. Crueger, W. Crueger Microbial Enzymes and Biotechnology, (1990), 177-226
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