G2133
Glucose Oxidase from Aspergillus niger
Type VII, lyophilized powder, ≥100,000 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 VII
form
lyophilized powder
specific activity
≥100,000 units/g solid (without added oxygen)
mol wt
160 kDa
does not contain
extender
composition
Protein, ≥60%
application(s)
diagnostic assay manufacturing
foreign activity
Catalase ≤10 Sigma units/mg protein
shipped in
wet ice
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
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
Several publications cite use of the G2133 glucose oxidase in their protocols and in various applications, such as the following:
a) Biosensor development:
c) Enzymatic fuel-cells with chitosan-based membranes: Bahar, T., and Yazici, M.S., Electroanalysis, 32(6), 1304-1314 (2020).
a) Biosensor development:
- Diazoresin nanofilm coatings on alginate microspheres: Srivastava, R. et al., Biotechnol. Bioeng., 91(1), 124-131 (2005).
- Paper-based glucose biosensor: Lankelma, J. et al., Anal. Chem., 84(9), 417-4152 (2012)
- Microfluidic device with glucose oxidase immobilized on hydrogel for glucose analysis of blood: He, R.-Y. et al., RSC Adv., 9, 32367-32374 (2019).
c) Enzymatic fuel-cells with chitosan-based membranes: Bahar, T., and Yazici, M.S., Electroanalysis, 32(6), 1304-1314 (2020).
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
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%.
Physical form
Lyophilized powder containing phosphate buffer salts and sodium chloride
Analysis Note
Protein determined by biuret.
signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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Feng Liu et al.
The Journal of investigative dermatology, 129(2), 422-431 (2008-10-31)
Microphthalmia-associated transcription factor (MiTF) is a key transcription factor for melanocyte lineage survival. Most previous work on this gene has been focused on its role in development. A role in carcinogenesis has emerged recently, but the mechanism is unclear. We
Komal Sodhi et al.
Scientific reports, 8(1), 9721-9721 (2018-06-28)
As aging involves oxidant injury, we examined the role of the recently described Na/K-ATPase oxidant amplification loop (NKAL). First, C57Bl6 old mice were given a western diet to stimulate oxidant injury or pNaKtide to antagonize the NKAL. The western diet
Amjad Askary et al.
Nature biotechnology, 38(1), 66-75 (2019-11-20)
Molecular barcoding technologies that uniquely identify single cells are hampered by limitations in barcode measurement. Readout by sequencing does not preserve the spatial organization of cells in tissues, whereas imaging methods preserve spatial structure but are less sensitive to barcode
Hua Zhang et al.
Cancer cell, 37(1), 37-54 (2019-12-31)
Cyclin-dependent kinase 7 (CDK7) is a central regulator of the cell cycle and gene transcription. However, little is known about its impact on genomic instability and cancer immunity. Using a selective CDK7 inhibitor, YKL-5-124, we demonstrated that CDK7 inhibition predominately
Shiri Barad et al.
Molecular plant-microbe interactions : MPMI, 27(1), 66-77 (2013-09-13)
Penicillium expansum, the causal agent of blue mold rot, causes severe postharvest fruit maceration through secretion of D-gluconic acid (GLA) and secondary metabolites such as the mycotoxin patulin in colonized tissue. GLA involvement in pathogenicity has been suggested but the
Protocols
Glucose oxidase activity measured via continuous spectrophotometric assay at 500 nm, indicating glucose oxidation rate.
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