G7141
Glucose Oxidase from Aspergillus niger
Type X-S, lyophilized powder, 100,000-250,000 units/g solid (without added oxygen)
Synonym(s):
β-D-Glucose:oxygen 1-oxidoreductase, G.Od., GOx
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About This Item
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type
Type X-S
Quality Level
form
lyophilized powder
specific activity
100,000-250,000 units/g solid (without added oxygen)
mol wt
160 kDa
composition
Protein, ≥65%
greener alternative product characteristics
Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
sustainability
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application(s)
diagnostic assay manufacturing
foreign activity
Catalase ≤5 units/mg protein
greener alternative category
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
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General description
Mass of glucose oxidase (GOX), a flavoprotein ranges from approximately 130 to 175 kDa. Some fungi and insects are capable of producing GOX.
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.
We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in fuel cell research. For more information see the article in biofiles.
Application
Glucose Oxidase from Aspergillus niger has been used:
- in the (glucose oxidase) GO reagent to measure the glucose content by the glucose oxidase (GO) method
- to activate the human renal carcinoma cell line for constructing the oxidative stress model
- to study its influence in the paste on the analytical performance of the bioelectrode
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 (GOX) oxidizes D-glucose to D-gluconolactone and hydrogen peroxide. Hydrogen peroxide, the catalytic product of GOX, serves as an anti-bacterial and anti-fungal agent. It is safe and can be used in several industrial applications like baking, dry egg powder production, wine production, gluconic acid production, etc. It possesses electrochemical activity, which makes it extremely important in glucose sensors and in fuel cell applications.
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
May contain traces of 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
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
Certificates of Analysis (COA)
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Glucose oxidase-An overview
Biotechnology Advances, 27(4), 489-501 (2009)
Glucose oxidase: natural occurrence, function, properties and industrial applications
Wong CM, et al.
Applied Microbiology and Biotechnology, 78(6), 927-938 (2008)
Raluca-Elena Munteanu et al.
Scientific reports, 9(1), 15196-15196 (2019-10-28)
If the analyte does not only change the electrochemical but also the optical properties of the electrode/solution interface, the spatial resolution of an electrochemical sensor can be substantially enhanced by combining the electrochemical sensor with optical microscopy. In order to
Ectopic Expression of Human MutS Homologue 2 on Renal Carcinoma Cells Is Induced by Oxidative Stress with Interleukin-18 Promotion via p38 Mitogen-activated Protein Kinase (MAPK) and c-Jun N-terminal Kinase (JNK) Signaling Pathways
Mo C, et al.
The Journal of Biological Chemistry, 287(23), 19242-19254 (2012)
Ewa Szczęsna et al.
European journal of cell biology, 95(12), 521-530 (2016-09-10)
End-binding proteins are capable of tracking the plus-ends of growing microtubules (MTs). The motor protein Ncd, a member of the kinesin-14 family, interacts with EB1 protein and becomes a non-autonomous tip-tracker. Here, we attempted to find out whether at least
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