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beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
2-deoxy-6-fluoro-D-glucose + O2 + H2O
2-deoxy-6-fluoro-D-glucono-1,5-lactone + H2O2
-
1.85% relative activity to beta-D-glucose
-
?
2-deoxy-D-glucose + O2
2-deoxy-D-glucono-1,5-lactone + H2O2
-
10% activity compared to beta-D-glucose
-
-
?
2-deoxy-d-glucose + O2
? + H2O2
-
10% of the activity compared to beta-D-glucose
-
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
3,6-methyl-D-glucose + O2
3-O,6-O-dimethyl-D-glucono-1,5-lactone + H2O2
-
10% activity compared to beta-D-glucose
-
-
?
3,6-methyl-D-glucose + O2
? + H2O2
-
10% of the activity compared to beta-D-glucose
-
-
?
3,6-methyl-D-glucose + O2 + H2O
3,6-methyl-D-glucono-1,5-lactone + H2O2
-
1.85% relative activity to beta-D-glucose
-
?
3-deoxy-D-glucose + O2 + H2O
3-deoxy-D-glucono-1,5-lactone + H2O2
-
1% relative activity to D-glucose
-
?
4,6-methyl-D-glucose + O2 + H2O
4,6-methyl-D-glucono-1,5-lactone + H2O2
-
1.22% relative activity to beta-D-glucose
-
?
4-deoxy-D-glucose + O2
4-deoxy-D-glucono-1,5-lactone + H2O2
-
7% activity compared to beta-D-glucose
-
-
?
4-deoxy-d-glucose + O2
? + H2O2
-
7% of the activity compared to beta-D-glucose
-
-
?
4-deoxy-D-glucose + O2 + H2O
4-deoxy-D-glucono-1,5-lactone + H2O2
-
2% relative activity to D-glucose
-
?
4-O-methy-D-glucose + O2 + H2O
4-O-methyl-D-glucono-1,5-lactone + H2O2
-
15% relative activity to D-glucose
-
?
4-O-methyl-D-glucose + O2
4-O-methyl-D-glucono-1,5-lactone + H2O2
-
8% activity compared to beta-D-glucose
-
-
?
4-O-methyl-D-glucose + O2
? + H2O2
-
8% of the activity compared to beta-D-glucose
-
-
?
6-deoxy-D-glucose + O2
6-deoxy-D-glucono-1,5-lactone + H2O2
-
12% activity compared to beta-D-glucose
-
-
?
6-deoxy-d-glucose + O2
? + H2O2
-
12% of the activity compared to beta-D-glucose
-
-
?
6-deoxy-D-glucose + O2 + H2O
6-deoxy-D-glucono-1,5-lactone + H2O2
-
10% relative activity to D-glucose
-
?
6-O-methyl-D-glucose + O2 + H2O
6-O-methyl-D-glucono-1,5-lactone + H2O2
-
1% relative activity to D-glucose
-
?
alpha-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
beta-D-glucose
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
beta-D-glucose + 1,2-naphthoquinone
D-glucono-1,5-lactone + ?
-
-
-
-
?
beta-D-glucose + 1,2-naphthoquinone-4-sulfonic acid
D-glucono-1,5-lactone + ?
-
-
-
-
?
beta-D-glucose + 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
beta-D-glucose + benzoquinone
D-glucono-1,5-lactone + hydroquinone
-
enzyme immobilized onto alumina
immobilized enzyme, yield of conversion: 100%
?
beta-D-glucose + ferrocinium-methanol
?
-
-
-
-
?
beta-D-glucose + methyl-1,4-benzoquinone
D-glucono-1,5-lactone + ?
-
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
beta-D-glucose + p-benzoquinone
D-glucono-1,5-lactone + ?
-
-
-
-
?
beta-D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
-
-
-
-
?
beta-D-glucose + potassium ferricyanide
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-galactose + O2 + H2O
?
-
low GOD activity
-
-
?
D-glucose + di-(2,2'-bipyridinyl)ruthenium(III)dichloride
D-glucono-1,5-lactone + di-(2,2'-bipyridinyl)ruthenium(II)dichloride
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
D-glucose + [(1,10-phenanthroline)2(Cl)2Ru(III)]
D-glucono-1,5-lactone + [(1,10-phenanthroline)2(Cl)2Ru(II)]
-
-
-
-
?
D-glucose + [(1,8-dimethyl-4,5-phenanthroline)3Ru(II)]PF6-
D-glucono-1,5-lactone + [(1,8-dimethyl-4,5-phenanthroline)3Ru(III)]PF6-
-
-
-
-
?
D-glucose + [(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(III)]
D-glucono-1,5-lactone + [(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(II)]
-
-
-
-
?
D-glucose + [(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(III)]PF6-
D-glucono-1,5-lactone + [(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(II)]PF6-
-
-
-
-
?
D-glucose + [(2,2'-bipyridine)2(CO32-)1/2Ru(III)]
D-glucono-1,5-lactone + [(2,2'-bipyridine)2(CO32-)1/2Ru(II)]
-
-
-
-
?
D-glucose + [(2,2'-bipyridine)2(H2O)2Ru(III)]PF6-
D-glucono-1,5-lactone + [(2,2'-bipyridine)2(H2O)2Ru(II)]PF6-
-
-
-
-
?
D-glucose + [(2,2'-bipyridine)2(SCN-)2Ru(III)]
D-glucono-1,5-lactone + [(2,2'-bipyridine)2(SCN-)2Ru(II)]
-
-
-
-
?
D-glucose + [(2,2'-bipyridine)3Ru(II)]PF6-
D-glucono-1,5-lactone + [(2,2'-bipyridine)3Ru(III)]PF6-
-
-
-
-
?
D-mannose + O2
? + H2O2
-
9% activity compared to beta-D-glucose
-
-
?
D-mannose + O2 + H2O
?
-
low GOD activity
-
-
?
mannose + O2
? + H2O2
-
9% of the activity compared to beta-D-glucose
-
-
?
mannose + O2 + H2O
? + H2O2
-
1% relative activity to D-glucose
-
?
additional information
?
-
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
electrocatalytical reduction of hydrogen peroxide derived from glucose oxidase, biochemical reactivity of glucose oxidase imaged by Scanning electrochemical microscopy, Prussian Blue film modified disk ultramicroelectrode
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
glucose oxidase used as a model protein for immobilization on a conducting polymer surface bearing abundant carboxyl groups, cyclic voltammetry applied to probe response to glucose
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
immobilization of biocatalysts in a membranous form, glucose oxidase as a model protein for biosensor analysis
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
multilayer films of glucose oxidase (GOX) and poly(dimethyl diallyl ammonium chloride, PDDA) prepared by layer-by-layer deposition and analyzed by Scanning electrochemical microscopy
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
D-glucose is oxidised at a much faster rate than 2-deoxy-D-glucose and D-mannose, whereas L-glucose, D-galactose, D-arabinose, D-xylose are not oxidised
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
enzyme assay using the ABTS/horseradish peroxidase system
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
the reaction can be divided into reductive and oxidative step. In the reductive half of the reaction, beta-D-glucose is oxidized to D-glucono-1,5-lactone, subsequently hydrolyzed to gluconic acid, with simultaneous reduction of FAD to FADH2. In the oxidative half of the reaction, FADH2 in GOx is re-oxidized by oxygen to yield H2O2
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
the addition of ferrous ions (Fe2+) induces the formation of hydroxyl radicals from the hydrogen peroxide, which act as initiating species for the microgel synthesis
-
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
-
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
20% relative activity to D-glucose
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
30% relative activity to beta-D-glucose
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
25% relative activity to beta-D-glucose
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
low GOD activity
-
-
?
alpha-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
0.64% relative activity to beta-D-glucose
-
?
alpha-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
very slow reaction
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
GOx enzyme catalyzes the oxidation of glucose to gluconolactone via reduction of the FAD cofactor to FADH2. The reoxidation of FADH2 in the ping-pong mechanism is normally achieved using oxygen as the electron acceptor
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
cofactor FAD is transiently reduced along the reaction mechanism
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
enzymatic oxidation by glucose oxidase reduces FAD to FADH2, releasing H2O2 in the presence of O2
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
the enzyme is highly specific for D-glucose
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
654185, 654659, 656782, 695600, 696068, 696777, 696864, 696884, 699078, 699771, 699922, 699941, 700599, 710858, 710908, 712533, 712857, 713259 -
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
-
ir
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
highly specific
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
soluble enzyme and immobilized enzyme on collagen
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
kinetic mechanism
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
glucose is the primary substrate for the enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
glucose is the primary substrate for the enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
glucose is the primary substrate for the enzyme
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
native enzyme and enzyme immobilized on activated carbon
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
the enzyme can use 2,6-dichlorophenolindophenol as hydrogen acceptor in addition to oxygen, the rate of glucose oxidation in the presence of 2,6-dichlorophenolindophenol is only 3.3% of that in the presence of oxygen
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
hydrogel microspheres of crosslinked poly(hydroxyethyl methylacrylate-co-dimethylaminoethyl methacrylate) are used for physical and covalent immobilization. Matrix entrapment (physical immobilization) affords the higher loading capacity and higher specific activity of the immobilized enzyme. The substrate has almost solution-like access to the immobilized enzyme within the microsphere and the hydrogel presents no significant diffusional barrier to enzyme-substrate reaction. Two functional groups, imidazolium and sulfhydryl, of His and Cys respectively, may be involved at the active site for the oxidation of glucose
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
GOD is highly specific for the beta-anomer of D-glucose
-
-
ir
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
highly substrate specific enzyme
-
-
?
L-sorbose + O2
? + H2O2
-
15% activity compared to beta-D-glucose
-
-
?
L-sorbose + O2
? + H2O2
-
15% of the activity compared to beta-D-glucose
-
-
?
additional information
?
-
His516 plays an important role in the reductive and oxidative half reaction
-
-
?
additional information
?
-
usage of the nitroso-aniline assay for determination of GOx activity
-
-
?
additional information
?
-
-
usage of the nitroso-aniline assay for determination of GOx activity
-
-
?
additional information
?
-
-
the enzyme is rapidly cleared from blood stream after application to rats, enzyme-produced H2O2 has toxic effects of rat liver and causes inflammation, at nontoxic levels it causes increased glutathione oxidation and induction of heme oxygenase 1 in the liver, overview
-
-
?
additional information
?
-
-
analysis of interaction of the enzyme with complexes of pentacyanoferrate(III) and nucleophilic ligands ammonia, imidazole or pyrazole, overview
-
-
?
additional information
?
-
-
the enzyme binds to concanavalin A forming insoluble complexes, overview
-
-
?
additional information
?
-
-
alpha-D-glucose is not a suitable substrate
-
-
?
additional information
?
-
-
construction of a nanodevice coupled with an integrated real-time detection system for evaluation of the function of biomolecules in biological processes, and enzymatic reaction kinetics occurring at the confined space or interface. A nanochannel-enzyme system in which the enzymatic reaction is coupled with an electrochemical method is constructed. The model system is established by covalently linking glucose oxidase (GOD) onto the inner wall of the nanochannels of the porous anodic alumina (PAA)membrane. An gold disc is attached at the end of the nanochannel of the PAA membrane as the working electrode for detection of H2O2 product of enzymatic reaction. The effects of ionic strength, amount of immobilized enzyme and pore diameter of the nanochannels on the enzymatic reaction kinetics are analysed, method evaluation, overview
-
-
?
additional information
?
-
-
no activity with 2-deoxy-6-fluoro-D-glucose, 4,6-dimethyl-D-glucose, beta-deoxy-D-glucose, 6-O-methyl-D-glucose, D-glucono-delta-lactone, L-gulono-gamma-lactone, D-gulono-gamma-lactone, D-glucuronolactone, altrose, galactose, xylose, idose, cellobiose, D-kabinose, L-arabinose, or D-fructose
-
-
?
additional information
?
-
the enzyme is specific for D-glucose, it shows less than 10% activity with trehalose, D-galactose, melibiose, and raffinose compared to D-glucose, no activity with L-mannomethylose, D-fructose, D-xylose, lactose, and sucrose
-
-
?
additional information
?
-
-
the enzyme is specific for D-glucose, it shows less than 10% activity with trehalose, D-galactose, melibiose, and raffinose compared to D-glucose, no activity with L-mannomethylose, D-fructose, D-xylose, lactose, and sucrose
-
-
?
additional information
?
-
the enzyme oxidizes the anomeric carbon of beta-D-glucose using molecular oxygen as an electron acceptor, producing H2O2 and D-glucono-delta-lactone, which in the presence of water spontaneously hydrolyzes to gluconic acid. Poor activity with xylose, maltose, cellobiose, cellotetraose, and xylo-oligosaccharides
-
-
?
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A173T/A332S
increased electron transfer (1.2fold)
A173T/F414L
increased electron transfer (1.2fold), 70% decrease in O2 sensitivity
A173V/A332S/F414I/V560T
increased electron transfer (6.4fold), decrease in O2 sensitivity
A332S/V560T
increased electron transfer (1.2fold), 70% decrease in O2 sensitivity
F414Y
increased electron transfer
I94V/T30S
increased O2 sensitivity, increased electron transfer (1.9fold)
N2Y/K13E/T30V/I94V/K152R
site-directed mutagenesis of mutant M12, pH optimum and sugar specificity of M12 mutant of GOx is similar to the wild-type enzyme, while thermostability is slightly decreased. Mutant M12 GOx expressed in Pichia pastoris shows three times higher activity compared to wild-type GOx towards redox mediators like N,N-dimethyl-nitroso-aniline used for glucose strips manufacturing. Mutant M12 GOx remains very specific for glucose but has higher activity for galactose compared to wild-type GOx
T110A
the mutant enzyme displays 12.3fold reduced O2 consumption
T110S
increased electron transfer
T110S/T34V
increased electron transfer
T110S/V20Y
increased O2 sensitivity
T30V/I94V/A162T
2.9fold increase in kcat/Km, decrease in t1/2(60°C) by 1.5°C
T30V/I94V/A162T/R537K/M556V
4.0fol2.6fold increase in kcat/Km, increase in t1/2(60°C) by 5.25°C
T56V/T132S
mutant enzyme displays better catalytic properties than the native enzyme
V20Y
increased electron transfer
A449C
-
site-directed mutagenesis, the mutation results in almost completely diminished activity compared to the wild-type enzyme
E84C
-
site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity
H172K
site-directed mutagenesis, mutant H172K shows increased thermosensitivity compared to the wild-type enzyme
H172K/H220D
site-directed mutagenesis, mutant H172K/H220D does not show significant differences in thermal stability but about 70% increased initial activity compared to the wild-type enzyme
H220D
site-directed mutagenesis, mutant H220D shows increased thermosensitivity and reduced activity compared to the wild-type enzyme
H447C
-
site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity
L500D
site-directed mutagenesis, inactive mutant
Q124R/L569E
site-directed mutagenesis, the mutation has no significant effect on stability but causes a twofold increase of the enzyme's specific activity
Q469K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q90R
site-directed mutagenesis, the mutant shows increased sensitivity to thermal denaturation, with R1 and R2 values 60% and 80% lower than wild-type enzyme respectively
Q90R/Y509E/T554M
the triple mutant is a glucose oxidase with high stability
S307C
-
site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity
T554M
random mutagenesis, the mutation generates a sulfur-pi interaction, the mutant shows 60% reduced activity and 40% increased thermal stability compared to the wild-type enzyme
T56V/T132S
-
site-directed mutagenesis, the mutant shows improved catalytic efficiency. The protein has three native cysteines, of which two are involved in a disulfide bond and the third is a free cysteine, Cys 521
T56V/T132S/C521S
-
site-directed mutagenesis, the mutant shows improved catalytic efficiency, mutation C521S does not alter enzyme activity, but the attachment of AuNPs to the native free thiol is prevented
Y435C
-
site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity
Y509E
site-directed mutagenesis, the mutation does not cause a significant change in the thermal stability of the enzyme, but causes increased enzyme activity compared to the wild-type enzyme
H447K
site-directed mutagenesis, introduction of two symmetrical, intermolecular salt bridges at the dimer interface, between K447 and D70
H447K
site-directed mutagenesis, the shows similar initial activity but higher thermal sensitivity compared to the wild-type enzyme
L569E
site-directed mutagenesis, the mutant shows about 50% increased initial activity compared to the wild-type enzyme
L569E
site-directed mutagenesis, the thermal stability of the mutant is similar to the wild-type enzyme, but the initial activity is increased compared to the wild-type enzyme
Q345K
site-directed mutagenesis, introduction of the mutation to create a salt bridge with D177
Q345K
site-directed mutagenesis, the mutant shows highly reduced thermal stability and about 50% increased initial activity compared to the wild-type enzyme
Q469K/L500D
site-directed mutagenesis, the mutant shows strongly reduced activity compared to the wild-type enzyme
Q469K/L500D
site-directed mutagenesis, the thermal stability of the mutant is similar to the wild-type enzyme, but the initial activity is reduced compared to the wild-type enzyme
Q90R/Y509E
site-directed mutagenesis, the mutation does not cause a significant change in the thermal stability of the enzyme, but causes increased enzyme activity compared to the wild-type enzyme
Q90R/Y509E
site-directed mutagenesis, the mutation introduces a new salt bridge near the interphase of the dimeric protein structure, the mutation does not cause a significant change in the thermal stability of the enzyme, but causes increased enzyme activity compared to the wild-type enzyme
T30S/I94V
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T30S/I94V
site-directed mutagenesis, a thermoresistant mutant
additional information
construction of enzyme mutant B11 with a C-terminal fusion with Saccharomyces cerevisiae Aga2 protein, the fusion proteins display on the surface of yeast EBY100 cells and show 2fold increased activity compared to the wild-type enzyme at pH 5.5 Aga2-GOx fusion proteins in the yeast cell wall can also be used as immobilized catalysts for the production of gluconic acid. The yeast surface display is developed for the directed evolution of antibodies in Saccharomyces cerevisiae, and involves the fusion of antibody variable domains to Aga2p, the adhesion subunit of the yeast agglutinin protein. Aga2p binds via disulfide bonds to the membrane protein Aga1p, which is embedded in the membrane via a glycosylphosphatidylinositol (GPI) anchor. The Aga2-antibody fusion gene is cloned in the vector pCTCON, whereas the Aga1p gene is integrated into the yeast genome, but both are under the control of galactose-inducible promoters. The surface display system is used for the directed evolution of horseradish peroxidase and expression of GOx for applications in biofuel cells. The kcat of the wild-type and B11 fusion enzymes are 1.65fold and 1.30fold lower than of the non-fusion enzymes, respectively, and the Km values of the wild-type and B11 fusion enzymes are 1.52fold and 1.74fold higher than of the non-fusion enzymes, respectively
additional information
-
construction of enzyme mutant B11 with a C-terminal fusion with Saccharomyces cerevisiae Aga2 protein, the fusion proteins display on the surface of yeast EBY100 cells and show 2fold increased activity compared to the wild-type enzyme at pH 5.5 Aga2-GOx fusion proteins in the yeast cell wall can also be used as immobilized catalysts for the production of gluconic acid. The yeast surface display is developed for the directed evolution of antibodies in Saccharomyces cerevisiae, and involves the fusion of antibody variable domains to Aga2p, the adhesion subunit of the yeast agglutinin protein. Aga2p binds via disulfide bonds to the membrane protein Aga1p, which is embedded in the membrane via a glycosylphosphatidylinositol (GPI) anchor. The Aga2-antibody fusion gene is cloned in the vector pCTCON, whereas the Aga1p gene is integrated into the yeast genome, but both are under the control of galactose-inducible promoters. The surface display system is used for the directed evolution of horseradish peroxidase and expression of GOx for applications in biofuel cells. The kcat of the wild-type and B11 fusion enzymes are 1.65fold and 1.30fold lower than of the non-fusion enzymes, respectively, and the Km values of the wild-type and B11 fusion enzymes are 1.52fold and 1.74fold higher than of the non-fusion enzymes, respectively
additional information
glucose oxidase is chemically modified to increase the stability of GOx using N-(3-dimethylaminopropyl)-N'-ethylcarbodiimide hydrochloride and sodium benzoate or aniline. The modification forms an amide bond between benzoate and lysines or aniline with glutamate and aspartate residues. The labeling of primary amines (lysines and the N-terminus) by benzoate is measured through a trinitrobenzene sulfonic acid (TNBS) assay
additional information
glucose oxidase is immobilized on mesoporous SBA-15 silica and two mesocellular foams (MCF) characterized by similar surface area and pore volumes but different pore/cell dimensions, covalent grafting of the enzyme through amide bonds, overview. The immobilized protein activity is significantly higher for the mesocellular foam with both cells and windows size larger than the enzyme dimensions. Enzyme GOx exhibits higher thermal stability when immobilized on the mesocellular foam compared to thefree enzyme
additional information
mutant glucose oxidase (B11-GOx) is obtained from directed protein evolution and wild-type enzyme. Higher glucose oxidation currents are obtained from B11-GOx both in solution and polymer electrodes compared to wild type enzyme. Improved electrocatalytic activity towards electrochemical oxidation of glucose from the mutant enzyme. The enzyme electrode with the mutant enzyme B11-GOx shows a faster electron transfer indicating a better electronic interaction with the polymer mediator
additional information
-
preparation of surface variants that contain artificial polymer poylethylene glycol. All surface modifications of glucose oxidase beyond that of the wild-type enzyme give rise to altered behavior for hydrogen transfer in the active site such that the kinetic isotope effect becomes more temperature-dependent upon perturbation
additional information
-
engineering of glucose oxidase by site-specific attachment of a maleimide-modified gold nanoparticle to the enzyme for enabling direct electrical communication between the conjugated enzyme and an electrode required for using the enzyme as biosensor, evaluation, overview
additional information
-
enzyme adsorption on different particles with homogeneous or nanostructured surfaces and coated with different compounds, i.e. 11-amino-1-undecanethiol, 12-mercaptododecanoic acid, 1-dodecanethiol, and 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol), only 9% of the activity of the native protein is preserved on 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol), but the substrate affinity of the adsorbed GOx is best on 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol) where its catalytic activity is worst, secondary structure of thhe enzyme is altered compared to enzyme in solution, overview
additional information
-
laccase and glucose oxidase in poly(ethyleneimine) microcapsules for immobilization in paper, activity, conformation and thermal stability, overview. The KM for GOx does not change after microencapsulation. Microencapsulation improves the thermal stability of GOx at temperatures up to 60°C due to stabilization of its active conformation but reduces the thermal stability of laccase because of the increased coordination between PEI and copper atoms in the enzyme's active site
additional information
-
macroporous silica foam is used as a nanoreactor to co-confine glucose oxidase and horseradish peroxidase with enzymatic cascade reactions, which act in tandem inside nanoreactors, for oxidation of glucose and 3,3',5,5'-tetramethylbenzidine, the catalytic activity of the co-confined enzymes is reduced, but stabilities of co-confined enzymes in denaturing agents, such as guanidinium chloride (GdmCl) and urea, are higher than those of free enzymes in solution compared to that of free enzymes in solution at room temperature. Adsorption amounts of glucose oxidase and horseradish peroxidase into macropores under different conditions, overview
additional information
-
modulation of calibration parameters of biosensors, in which glucose oxidase is used for biorecognition, in the presence of different chlorides by following the transient phase dynamics ofoxygen concentration with an oxygen optrode, mechanism, overview. the maximum calculated signal change was amplifiedfor about 20% in the presence of sodium and magnesium chlorides. The value of the kinetic parameter decreases along with the addition of salts and increases only at sodium chloride concentrations over 0.5 mM, MgCl2 causes a 1.3fold essential increase of the maximum signal change parameter A in a salt concentration, ranging from 0.1 to 0.4 M. AlCl3 inhibits the enzyme at 5 mM, and at higher salt concentrations over 0.1 M, the catalytic activity is completely inhibited
additional information
-
PEGylation of GOx provides stability against denaturation or hydrolytic cleavage, glycosylation site-targeted PEGylation of glucose oxidase retains native enzymatic activity, bioconjugate's potential of the enzyme in an optical biosensing assay, overview. The bioconjugate is entrapped within a poly(2-hydroxyethyl methacrylate) hydrogel containing an oxygen-sensitive phosphor, and the construct is shown to respond approximately linearly over the physiologically-relevant glucose range, overview
additional information
-
construction of a nanodevice coupled with an integrated real-time detection system for evaluation of the function of biomolecules in biological processes, and enzymatic reaction kinetics occurring at the confined space or interface. A nanochannel-enzyme system in which the enzymatic reaction is coupled with an electrochemical method is constructed. The model system is established by covalently linking glucose oxidase (GOD) onto the inner wall of the nanochannels of the porous anodic alumina (PAA)membrane. For enzyme assembling, the PAA membranes are first treated with silane to form epoxy groups modified inner surface of PAA nanochannels. Then GOD is assembled onto the membrane and the inner wall of the nanochannels through a ring-opening reaction. An gold disc is attached at the end of the nanochannel of the PAA membrane as the working electrode for detection of H2O2 product of enzymatic reaction. The effects of ionic strength, amount of immobilized enzyme and pore diameter of the nanochannels on the enzymatic reaction kinetics are analysed, method evaluation, overview
additional information
-
in situ RAFT polymerization of four different monomers including acrylic acid (AA), methyl acrylate (MA), poly (ethylene glycol) acrylate (PEG-A) and tert-butyl acrylate (TBA) are polymerized directly on the surface of enzyme GOx to afford GOx-poly (PEG-A)(GOx-PPEG-A), GOx-poly(MA)(GOx-PMA), GOx-poly(AA)(GOx-PAA), and GOx-poly(TBA)(GOx-PTBA) conjugates, respectively. PAA and PPEG-A represent the hydrophilic polymers, while PMA and PTBA stand for the hydrophobic ones. Higher bioactivity is obtained for GOx modified with hydrophilic polymers compared with that modified with hydrophobic ones. All the tested polymers can enhance the stability of the GOx, while the hydrophobic GOx-polymers conjugates exhibit much better stability than the hydrophilic ones. Method overview
additional information
-
the enzyme adopts a stable secondary conformation with some degree of freedom at active sites under acidic-neutral pH values, when either free in solution or immobilized on Nafion. Immobilization on Nafion actually increases the amount of active enzyme (Vmax) and affinity for glucose (inversely proportional to Km) at pH 6.0
additional information
usage of a strategy that combined random and rational approaches to isolate uncharacterized mutations of Aspergillus niger glucose oxidase with improved properties. GOX library construction in Saccharomyces cerevisiae and random mutagenesis and screening for mutants with improved thermal stability
additional information
-
usage of a strategy that combined random and rational approaches to isolate uncharacterized mutations of Aspergillus niger glucose oxidase with improved properties. GOX library construction in Saccharomyces cerevisiae and random mutagenesis and screening for mutants with improved thermal stability
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Comparison of rates and kinetic isotope effects using PEG-modified variants and glycoforms of glucose oxidase: the relationship of modification of the protein envelope to C-H activation and tunneling
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Ivanova, E.V.; Ershov, A.Y.; Laurinavicius, V.; Meskus, R.; Ryabov, A.D.
Comparative kinetic study of D-glucose oxidation by ruthenium(III) compounds catalyzed by FAD-dependent glucose oxidase and PQQ-dependent glucose dehydrogenase
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Mechanism for high stability of liposomal glucose oxidase to inhibitor hydrogen peroxide produced in prolonged glucose oxidation
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Kinetics in microemulsion V. Glucose oxidase catalyzed oxidation of beta-D-glucose in aqueous, micellar and water-in-oil microemulsion media
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Zoldak, G.; Zubrik, A.; Musatov, A.; Stupak, M.; Sedlak, E.
Irreversible thermal denaturation of glucose oxidase from Aspergillus niger is the transition to the denatured state with residual structure
J. Biol. Chem.
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Aspergillus niger
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Brahim, S.; Narinesingh, D.; Guiseppi-Elie, A.
Kinetics of glucose oxidase immobilized in p(HEMA)-hydrogel microspheres in a packed-bed bioreactor
J. Mol. Catal. B
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2002
Aspergillus niger
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Wohlfahrt, G.; Trivic, S.; Zeremski, J.; Pericin, D.; Leskovac, V.
The chemical mechanism of action of glucose oxidase from Aspergillus niger
Mol. Cell. Biochem.
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2004
Aspergillus niger
brenda
Ko, J.H.; Hahm, M.S.; Kang, H.A.; Nam, S.W.; Chung, B.H.
Secretory expression and purification of Aspergillus niger glucose oxidase in Saccharomyces cerevisiae mutant deficient in PMR1 gene
Protein Expr. Purif.
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2002
Aspergillus niger
brenda
Tetianec, L.; Kulys, J.
Study of kinetics of Aspergillus niger glucose oxidase reaction with pentacyanoferrates containing nucleophilic ligands
Biologija (Vilnius)
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2005
Aspergillus niger
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brenda
Ferreira, L.F.; Taqueda, M.E.; Converti, A.; Vitolo, M.; Pessoa, A.
Purification of glucose oxidase from Aspergillus niger by liquid-liquid cationic reversed micelles extraction
Biotechnol. Prog.
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2005
Aspergillus niger
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Bhatti, H.N.; Madeeha, M.; Asgher, M.; Batool, N.
Purification and thermodynamic characterization of glucose oxidase from a newly isolated strain of Aspergillus niger
Can. J. Microbiol.
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2006
Aspergillus niger, Aspergillus niger NFCCP
brenda
Rost, D.; Welker, A.; Welker, J.; Millonig, G.; Berger, I.; Autschbach, F.; Schuppan, D.; Mueller, S.
Liver-homing of purified glucose oxidase: A novel in vivo model of physiological hepatic oxidative stress (H(2)O(2))
J. Hepatol.
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2006
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brenda
Jan, U.; Khan, A.A.; Husain, Q.
A study on the comparative stability of insoluble complexes of glucose oxidase obtained with concanavalin A and specific polyclonal antibodies
World J. Microbiol. Biotechnol.
22
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2006
Aspergillus niger
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brenda
Li, J.; Yu, J.
Fabrication of Prussian Blue modified ultramicroelectrode for GOD imaging using scanning electrochemical microscopy
Bioelectrochemistry
72
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2008
Aspergillus niger (P13006)
brenda
Burchardt, M.; Wittstock, G.
Kinetic studies of glucose oxidase in polyelectrolyte multilayer films by means of scanning electrochemical microscopy (SECM)
Bioelectrochemistry
72
66-76
2008
Aspergillus niger (P13006)
brenda
Chen, S.; Chen, W.; Xue, G.
Electrogeneration of polypyrrole/alginate films for immobilization of glucose oxidase
Macromol. Biosci.
8
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2008
Aspergillus niger (P13006)
brenda
Kumar, J.; DSouza, S.F.
Preparation of PVA membrane for immobilization of GOD for glucose biosensor
Talanta
75
183-188
2008
Aspergillus niger (P13006)
brenda
Bahshi, L.; Frasconi, M.; Tel-Vered, R.; Yehezkeli, O.; Willner, I.
Following the biocatalytic activities of glucose oxidase by electrochemically cross-linked enzyme-Pt nanoparticles composite electrodes
Anal. Chem.
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2008
Aspergillus niger
brenda
Yu, J.H.; Kang, S.G.; Jung, U.Y.; Jun, C.H.; Kim, H.
Effects of omega-3 fatty acids on apoptosis of human gastric epithelial cells exposed to silica-immobilized glucose oxidase
Ann. N. Y. Acad. Sci.
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2009
Aspergillus niger
brenda
Guo, Y.; Lu, F.; Zhao, H.; Tang, Y.; Lu, Z.
Cloning and heterologous expression of glucose oxidase gene from Aspergillus niger Z-25 in Pichia pastoris
Appl. Biochem. Biotechnol.
162
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2010
Aspergillus niger (P13006), Aspergillus niger Z-25 (P13006), Aspergillus niger Z-25
brenda
Wong, C.M.; Wong, K.H.; Chen, X.D.
Glucose oxidase: natural occurrence, function, properties and industrial applications
Appl. Microbiol. Biotechnol.
78
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2008
Aspergillus niger
brenda
Miron, J.; Vazquez, J.; Gonzalez, M.; Murado, M.
Joint effect of nitrogen and phosphorous on glucose oxidase production by Aspergillus niger: Discussion of an experimental design with a risk of co-linearity
Biochem. Eng. J.
40
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2008
Aspergillus niger
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brenda
Jairajpuri, D.S.; Fatima, S.; Saleemuddin, M.
Complexing of glucose oxidase with anti-glucose oxidase antibodies or the F(ab)(2)/F(ab) fragments derived therefrom protects both the enzyme and antibody/antibody fragments against glycation
Biochemistry
73
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2008
Aspergillus niger
brenda
Tao, Z.; Raffel, R.A.; Souid, A.K.; Goodisman, J.
Kinetic studies on enzyme-catalyzed reactions: oxidation of glucose, decomposition of hydrogen peroxide and their combination
Biophys. J.
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2009
Aspergillus niger
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Gao, F.; Courjean, O.; Mano, N.
An improved glucose/O2 membrane-less biofuel cell through glucose oxidase purification
Biosens. Bioelectron.
25
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2009
Aspergillus niger
brenda
Bankar, S.B.; Bule, M.V.; Singhal, R.S.; Ananthanarayan, L.
Glucose oxidase - an overview
Biotechnol. Adv.
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2009
Aspergillus niger
brenda
Johnstone-Robertson, M.; Clarke, K.; Harrison, S.
Characterization of the distribution of glucose oxidase in Penicillium sp. CBS 120262 and Aspergillus niger NRRL-3 cultures and its effect on integrated product recovery
Biotechnol. Bioeng.
99
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2008
Aspergillus niger, Penicillium canescens, Penicillium canescens CBS 120262, Aspergillus niger NRRL-3
brenda
Jo, S.M.; Lee, H.Y.; Kim, J.C.
Glucose-sensitivity of liposomes incorporating conjugates of glucose oxidase and poly(N-isopropylacrylamide-co-methacrylic acid-co-octadecylacrylate)
Int. J. Biol. Macromol.
45
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2009
Aspergillus niger
brenda
Paz-Alfaro, K.J.; Ruiz-Granados, Y.G.; Uribe-Carvajal, S.; Sampedro, J.G.
Trehalose-mediated thermal stabilization of glucose oxidase from Aspergillus niger
J. Biotechnol.
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2009
Aspergillus niger
brenda
Guiseppi-Elie, A.; Choi, S.; Geckeler, K.
Ultrasonic processing of enzymes: Effect on enzymatic activity of glucose oxidase
J. Mol. Catal. B
58
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2009
Aspergillus niger
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brenda
Wu, X.; Zhao, B.; Wu, P.; Zhang, H.; Cai, C.
Effects of ionic liquids on enzymatic catalysis of the glucose oxidase toward the oxidation of glucose
J. Phys. Chem. B
113
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2009
Aspergillus niger
brenda
He, C.; Liu, J.; Xie, L.; Zhang, Q.; Li, C.; Gui, D.; Zhang, G.; Wu, C.
Activity and thermal stability improvements of glucose oxidase upon adsorption on core-shell PMMA-BSA nanoparticles
Langmuir
25
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2009
Aspergillus niger
brenda
Kumar, S.; Sitasawad, S.L.
N-acetylcysteine prevents glucose/glucose oxidase-induced oxidative stress, mitochondrial damage and apoptosis in H9c2 cells
Life Sci.
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2009
Aspergillus niger
brenda
Liu, Q.; Rauth, A.M.; Liu, J.; Babakhanian, K.; Wang, X.; Bendayan, R.; Wu, X.Y.
Characterization of a microsphere formulation containing glucose oxidase and its in vivo efficacy in a murine solid tumor model
Pharm. Res.
26
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2009
Aspergillus niger
brenda
Hashemifard, N.; Mohsenifar, A.; Ranjbar, B.; Allameh, A.; Lotfi, A.S.; Etemadikia, B.
Fabrication and kinetic studies of a novel silver nanoparticles-glucose oxidase bioconjugate
Anal. Chim. Acta
675
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2010
Aspergillus niger
brenda
Altikatoglu, M.; Basaran, Y.; Arioz, C.; Ogan, A.; Kuzu, H.
Glucose oxidase-dextran conjugates with enhanced stabilities against temperature and pH
Appl. Biochem. Biotechnol.
160
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2010
Aspergillus niger
brenda
Courjean, O.; Mano, N.
Recombinant glucose oxidase from Penicillium amagasakiense for efficient bioelectrochemical applications in physiological conditions
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2011
Aspergillus niger, Penicillium amagasakiense
brenda
Wang, Q.; Xu, W.; Wu, P.; Zhang, H.; Cai, C.; Zhao, B.
New insights into the effects of thermal treatment on the catalytic activity and conformational structure of glucose oxidase studied by electrochemistry, IR spectroscopy, and theoretical calculation
J. Phys. Chem. B
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2010
Aspergillus niger
brenda
Maruthasalam, S.; Liu, Y.L.; Sun, C.M.; Chen, P.Y.; Yu, C.W.; Lee, P.F.; Lin, C.H.
Constitutive expression of a fungal glucose oxidase gene in transgenic tobacco confers chilling tolerance through the activation of antioxidative defence system
Plant Cell Rep.
29
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2010
Aspergillus niger
brenda
Cao, X.; Li, Y.; Zhang, Z.; Yu, J.; Qian, J.; Liu, S.
Catalytic activity and stability of glucose oxidase/horseradish peroxidase co-confined in macroporous silica foam
Analyst
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2012
Aspergillus niger
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Ritter, D.W.; Roberts, J.R.; McShane, M.J.
Glycosylation site-targeted PEGylation of glucose oxidase retains native enzymatic activity
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2013
Aspergillus niger
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Kagan, M.; Kivirand, K.; Rinken, T.
Modulation of enzyme catalytic properties and biosensor calibration parameters with chlorides: Studies with glucose oxidase
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2013
Aspergillus niger
brenda
Holland, J.T.; Lau, C.; Brozik, S.; Atanassov, P.; Banta, S.
Engineering of glucose oxidase for direct electron transfer via site-specific gold nanoparticle conjugation
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Aspergillus niger
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Seehuber, A.; Dahint, R.
Conformation and activity of glucose oxidase on homogeneously coated and nanostructured surfaces
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Aspergillus niger
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Zhang, Y.; Rochefort, D.
Activity, conformation and thermal stability of laccase and glucose oxidase in poly(ethyleneimine) microcapsules for immobilization in paper
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Aspergillus niger
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Wohlfahrt, G.; Witt, S.; Hendle, J.; Schomburg, D.; Kalisz, H.M.; Hecht, H.J.
1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes
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Kalisz, H.M.; Hecht, H.J.; Schomburg, D.; Schmid, R.D.
Effects of carbohydrate depletion on the structure, stability and activity of glucose oxidase from Aspergillus niger
Biochim. Biophys. Acta
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Hecht, H.J.; Schomburg, D.; Kalisz, H.; Schmid, R.D.
The 3D structure of glucose oxidase from Aspergillus niger. Implications for the use of GOD as a biosensor enzyme
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Meyer, M.; Wohlfahrt, G.; Knblein. J.; Schomburg, D.
Aspects of the mechanism of catalysis of glucose oxidase: a docking, molecular mechanics and quantum chemical study
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Aspergillus niger (P13006)
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Mecheri, B.; De Porcellinis, D.; Campana, P.T.; Rainer, A.; Trombetta, M.; Marletta, A.; Oliveira, O.N.; Licoccia, S.
Tuning structural changes in glucose oxidase for enzyme fuel cell applications
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Aspergillus niger
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Ansari, Z.; Karimi, A.; Ebrahimi, S.; Emami, E.
Improvement in ligninolytic activity of Phanerochaete chrysosporium cultures by glucose oxidase
Biochem. Eng. J.
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Aspergillus niger (P13006)
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brenda
Yu, J.; Zhang, Y.; Liu, S.
Enzymatic reactivity of glucose oxidase confined in nanochannels
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55
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2014
Aspergillus niger
brenda
Halalipour, A.; Duff, M.R.; Howell, E.E.; Reyes-De-Corcuera, J.I.
Glucose oxidase stabilization against thermal inactivation using high hydrostatic pressure and hydrophobic modification
Biotechnol. Bioeng.
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2017
Aspergillus niger (P13006)
brenda
Zia, M.; Riaz, A.; Rasul, S.; Abbas, R.
Evaluation of antimicrobial activity of glucose oxidase from Aspergillus niger EBL-A and Penicillium notatum
Braz. Arch. Biol. Technol.
56
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Aspergillus niger, Penicillium chrysogenum (K9L4P7), Aspergillus niger EBL-A
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Balistreri, N.; Gaboriau, D.; Jolivalt, C.; Launay, F.
Covalent immobilization of glucose oxidase on mesocellular silica foams Characterization and stability towards temperature and organic solvents
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Aspergillus niger (P13006)
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Xu, G.; Xu, Y.; Li, A.; Chen, T.; Liu, J.
Enzymatic bioactivity investigation of glucose oxidase modified with hydrophilic or hydrophobic polymers via in situ RAFT polymerization
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Aspergillus niger
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Meng, Y.; Zhao, M.; Yang, M.; Zhang, Q.; Hao, J.; Meng, Y.
Production and characterization of recombinant glucose oxidase from Aspergillus niger expressed in Pichia pastoris
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Aspergillus niger (Q0PGS3), Aspergillus niger, Aspergillus niger ATCC 9029 (Q0PGS3)
brenda
Kovacevic, G.; Blazic, M.; Draganic, B.; Ostafe, R.; Gavrovic-Jankulovic, M.; Fischer, R.; Prodanovic, R.
Cloning, heterologous expression, purification and characterization of M12 mutant of Aspergillus niger glucose oxidase in yeast Pichia pastoris KM71H
Mol. Biotechnol.
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Aspergillus niger (P13006), Aspergillus niger
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Sim, H.J.; Kim, J.H.; Kook, S.H.; Lee, S.Y.; Lee, J.C.
Glucose oxidase facilitates osteogenic differentiation and mineralization of embryonic stem cells through the activation of Nrf2 and ERK signal transduction pathways
Mol. Cell. Biochem.
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Aspergillus niger (P13006)
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Marin-Navarro, J.; Roupain, N.; Talens-Perales, D.; Polaina, J.
Identification and structural analysis of amino acid substitutions that increase the stability and activity of Aspergillus niger glucose oxidase
PLoS ONE
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Aspergillus niger (A0A068CB13), Aspergillus niger, Aspergillus niger CECT 2775 (A0A068CB13)
brenda
Tribst, A.A.; Cota, J.; Murakami, M.T.; Cristianini, M.
Effects of high pressure homogenization on the activity, stability, kinetics and three-dimensional conformation of a glucose oxidase produced by Aspergillus niger
PLoS ONE
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Aspergillus niger
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Blazic, M.; Kovacevic, G.; Prodanovic, O.; Ostafe, R.; Gavrovic-Jankulovic, M.; Fischer, R.; Prodanovic, R.
Yeast surface display for the expression, purification and characterization of wild-type and B11 mutant glucose oxidases
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2013
Aspergillus niger (P13006), Aspergillus niger
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Jithendar, T.; Sairam, K.; Verma, V.
Research journal of pharmaceutical, biological and chemical sciences purification, characterization, thermostability and shelf life studies of glucose oxidase from Aspergillus niger PIL7
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Aspergillus niger, Aspergillus niger PIL7
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Vuong, T.V.; Foumani, M.; MacCormick, B.; Kwan, R.; Master, E.R.
Direct comparison of gluco-oligosaccharide oxidase variants and glucose oxidase substrate range and H2O2 stability
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Aspergillus niger (Q9HFQ1)
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Sattari, Z.; Pourfaizi, H.; Dehghan, G.; Amani, M.; Moosavi-Movahedi, A.
Thermal inactivation and conformational lock studies on glucose oxidase
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Aspergillus niger (P13006)
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Yu, E.; Prodanovic, R.; Gven, G.; Ostafe, R.; Schwaneberg, U.
Electrochemical oxidation of glucose using mutant glucose oxidase from directed protein evolution for biosensor and biofuel cell applications
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Aspergillus niger (P13006)
brenda
Won, K.; Kim, Y.; An, S.; Lee, H.; Park, S.; Choi, Y.; Kim, J.; Hwang, H.; Kim, H.; Kim, H.; Lee, S.
Glucose oxidase/cellulose-carbon nanotube composite paper as a biocompatible bioelectrode for biofuel cells
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Aspergillus niger (P13006)
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Zhao, X.; Jia, H.; Kim, J.; Wang, P.
Kinetic limitations of a bioelectrochemical electrode using carbon nanotube-attached glucose oxidase for biofuel cells
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2009
Aspergillus niger (P13006)
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Fischback, M.; Kwon, K.; Lee, I.; Shin, S.; Park, H.; Kim, B.; Kwon, Y.; Jung, H.; Kim, J.; Ha, S.
Enzyme precipitate coatings of glucose oxidase onto carbon paper for biofuel cell applications
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2012
Aspergillus niger (P13006)
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La Rotta H., C.; Ciniciato, G.; Gonzalez, E.
Triphenylmethane dyes, an alternative for mediated electronic transfer systems in glucose oxidase biofuel cells
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Aspergillus niger (P13006)
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Yamamoto, K.; Matsumoto, T.; Shimada, S.; Tanaka, T.; Kondo, A.
Starchy biomass-powered enzymatic biofuel cell based on amylases and glucose oxidase multi-immobilized bioanode
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Aspergillus niger (P13006)
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Petrovic, D.; Frank, D.; Kamerlin, S.C.L.; Hoffmann, K.; Strodel, B.
Shuffling active site substate populations affects catalytic activity the case of glucose oxidase
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Mano, N.
Engineering glucose oxidase for bioelectrochemical applications
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Halalipour, A.; Duff, M.R.; Howell, E.E.; Reyes-De-Corcuera, J.I.
Catalytic activity and stabilization of phenyl-modified glucose oxidase at high hydrostatic pressure
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Aspergillus niger (P13006)
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Belyad, F.; Karkhanei, A.A.; Raheb, J.
Expression, characterization and one step purification of heterologous glucose oxidase gene from Aspergillus niger ATCC 9029 in Pichia pastoris
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Aspergillus niger (P13006), Aspergillus niger ATCC 9029 (P13006), Aspergillus niger ATCC 9029
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Gau, E.; Flecken, F.; Ksiazkiewicz, A.; Pich, A.
Enzymatic synthesis of temperature-responsive poly(N-vinylcaprolactam) microgels with glucose oxidase
Green Chem.
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Aspergillus niger (P13006)
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Jiang, P.; Liu, H.; Zhao, X.; Ding, Q.
Physicochemical properties of soybean protein isolate affected by the cross-linking with horseradish peroxidase, glucose oxidase and glucose
J. Food Meas. Charact.
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Aspergillus niger (P13006)
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Sedlak, E.; Sedlakova, D.; Marek, J.; Hancar, J.; Garajova, K.; Zoldak, G.
Ion-specific protein/water interface determines the Hofmeister effect on the kinetic stability of glucose oxidase
J. Phys. Chem. B
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Aspergillus niger (P13006), Aspergillus niger
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Khadivi Derakshan, F.; Darvishi, F.; Dezfulian, M.; Madzak, C.
Expression and characterization of glucose oxidase from Aspergillus niger in Yarrowia lipolytica
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Aspergillus niger (P13006), Aspergillus niger, Aspergillus niger ATCC 9202 (P13006)
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Wang, Y.; Wang, J.; Leng, F.; Ma, J.; Bagadi, A.
Expression of Aspergillus niger glucose oxidase in Pichia pastoris and its antimicrobial activity against Agrobacterium and Escherichia coli
PeerJ
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Aspergillus niger (E3VW38), Aspergillus niger, Aspergillus niger ZM-8 (E3VW38)
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Jagathy, K.; Kalpana, K.; Rajeshkumar, S.
Production, optimization, characterization and immobilization of glucose oxidase from Aspergillus species
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Aspergillus niger, Aspergillus niger PIL7
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Kang, Z.; Jiao, K.; Yu, C.; Dong, J.; Peng, R.; Hu, Z.; Jiao, S.
Direct electrochemistry and bioelectrocatalysis of glucose oxidase in CS/CNC film and its application in glucose biosensing and biofuel cells
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Aspergillus niger (P13006)
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Wu, Y.; Chu, L.; Liu, W.; Jiang, L.; Chen, X.; Wang, Y.; Zhao, Y.
The screening of metal ion inhibitors for glucose oxidase based on the peroxidase-like activity of nano-Fe3O4
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Aspergillus niger (P13006)
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