G6766
Glucose Oxidase from Aspergillus niger
2,000-10,000 units/g solid (without added oxygen)
Synonym(s):
β-D-Glucose:oxygen 1-oxidoreductase, G.Od., GOx
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
Recommended Products
form
powder
specific activity
2,000-10,000 units/g solid (without added oxygen)
mol wt
160 kDa
storage temp.
−20°C
InChI
1S/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5-,6-/m1/s1
InChI key
WQZGKKKJIJFFOK-VFUOTHLCSA-N
Looking for similar products? Visit Product Comparison Guide
General description
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.
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.
Application
Glucose oxidase is widely used in the food and pharmaceutical industries as well as a major component of glucose biosensors.
Biochem/physiol Actions
Glucose oxidase catalyses the oxidation of β-d-glucose to d-glucono-β-lactone and hydrogen peroxide, with molecular oxygen as an electron acceptor.
Quality
Crude. May contain catalase, 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.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
Habib Razmi et al.
Biosensors & bioelectronics, 41, 498-504 (2012-10-27)
Graphene quantum dots (GQD) were introduced as a novel and suitable substrate for enzyme immobilization. Glucose oxidase (GOx) was immobilized on GQD modified carbon ceramic electrode (CCE) and well-defined quasi-reversible redox peaks were observed. The UV-vis photoluminescence spectroscopy, transition electron
Rong Hu et al.
Biosensors & bioelectronics, 41, 442-445 (2012-10-16)
A universal sensing platform for fluorescence turn-on detection of biomolecules is developed based on Fenton reaction triggered molecular beacon cleavage. Due to its high quenching efficiency, molecular beacons (MBs)-based sensing systems usually show low background fluorescence and large signal-to-background ratio.
Kun Deng et al.
Analytica chimica acta, 759, 61-65 (2012-12-25)
In this work, a new label-free electrochemical aptamer-based sensor (aptasensor) was constructed for detection of platelet-derived growth factor (PDGF) based on the direct electrochemistry of glucose oxidase (GOD). For this proposed aptasensor, poly(diallyldimethylammonium chloride) (PDDA)-protected graphene-gold nanoparticles (P-Gra-GNPs) composite was
Yinhui Yi et al.
Chemical communications (Cambridge, England), 49(6), 612-614 (2012-12-12)
Si quantum dots have been demonstrated to be environmentally friendly photoluminescence probes and their fluorescence was quenched by H(2)O(2) that was produced from the glucose oxidase-catalyzed oxidation of glucose. This strategy could be used to detect glucose with high sensitivity
Karnit Bahartan et al.
Chemical communications (Cambridge, England), 48(98), 11957-11959 (2012-11-06)
Yeast displaying glucose oxidase on their surface were encapsulated in a graphene oxide hydrogel. The ability of the modified yeast to reduce graphene oxide by glucose assimilation while maintaining viability was tested with time and deemed suitable for biofuel cell
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service