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(R)-1-phenyl-1,2-ethanediol + O2
(2R)-hydroxy(phenyl)ethanoic acid + H2O2
-
-
product identification by NMR
-
?
(R)-1-phenyl-1,2-ethanediol + O2
?
-
-
-
-
?
(S)-1-phenyl-1,2-ethanediol + O2
?
-
-
-
-
?
1,2,4-butanetriol + O2
?
-
-
-
-
?
1,2-butanediol + O2
?
-
-
-
-
?
1,2-hexanediol + O2
?
-
-
-
-
?
1,2-pentanediol + O2
2-hydroxypentanoate + H2O2
-
-
product identification by NMR
-
?
1,3-butanediol + O2
2-hydroxypropanal + H2O2
-
-
product identification by GC-MS
-
?
1-phenyl-1,2-ethanediol + O2
hydroxy(phenyl)ethanoic acid + H2O2
-
-
-
-
r
2-amino-1-pentanol + O2
?
-
-
-
-
?
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
2-deoxy-D-glucose + O2
?
19.6% of the activity with D-glucose for the native enzyme, 5.9 for the recombinant enzyme
-
-
?
2-deoxy-d-glucose + O2
? + H2O2
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
3,6-methyl-D-glucose + O2
? + H2O2
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-butene-1,2-diol + O2
?
-
-
-
-
?
3-butenol + O2
?
-
-
-
-
?
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
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
-
-
?
4-pentene-1,2-diol + O2
?
-
-
-
-
?
6-deoxy-6-fluoro-D-glucose + O2 + H2O
6-deoxy-6-fluoro-D-glucono-1,5-lactone + H2O2
-
3% relative activity to beta-D-glucose, when determined with an unspecified enzyme at 0.5 M substrate concentration
-
?
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
alpha-methyl-D-glucoside + O2 + H2O
? + H2O2
-
13% relative activity to D-glucose
-
?
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 + 1,4-benzoquinone
D-glucono-1,5-lactone + hydroquinone
beta-D-glucose + 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + ?
beta-D-glucose + 4-benzoquinone
D-glucono-1,5-lactone + 4-benzoquinol
-
-
-
-
r
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 + N,N,N',N'-tetramethyl-1,4-phenylenediamine
?
-
-
-
-
r
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 + ?
-
-
-
-
?
cellobiose + O2 + H2O
? + H2O2
-
13% relative activity to D-glucose
-
?
D-fructose + O2
?
4.9% of the activity with D-glucose for the native enzyme, no activity with the recombinant enzyme
-
-
?
D-fructose + O2 + H2O
? + H2O2
-
4.9% relative activity to D-glucose
-
?
D-galactose + O2 + H2O
?
-
low GOD activity
-
-
?
D-galactose + O2 + H2O
? + H2O2
-
recombinant enzyme
-
?
D-glucono-1,5-lactone + O2 + H2O
? + H2O2
-
80% relative activity to D-glucose
-
?
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-glucosone + O2 + H2O
? + H2O2
-
30% relative activity to beta-D-glucose
-
?
D-maltose + O2 + H2O
? + H2O2
D-mannose + O2
? + H2O2
-
9% activity compared to beta-D-glucose
-
-
?
D-mannose + O2 + H2O
?
-
low GOD activity
-
-
?
D-xylose + O2 + H2O
? + H2O2
galactose + O2 + H2O
D-galactono-1,5-lactone + H2O2
-
18% of the activity with beta-D-glucose
-
-
?
glycerol + O2
?
-
-
-
-
?
L-gulono-gamma-lactone + O2 + H2O
? + H2O2
-
62% relative activity to D-glucose
-
?
L-threitol + O2
?
-
-
-
-
?
maltose + O2
?
21.3% of the activity with D-glucose for the native enzyme, 42.2% for the recombinant enzyme
-
-
?
mannose + O2 + H2O
? + H2O2
additional information
?
-
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
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
? + H2O2
-
10% of the activity compared to beta-D-glucose
-
-
?
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
-
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
recombinant enzyme
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
25% relative activity to beta-D-glucose, when determined with a commercial preparation of the enzyme at 0.1 M substrate concentration, 12% relative activity to beta-D-glucose, when determined with a commercial preparation of glucose oxidase, containing catalase, at 0.05 M substrate concentration
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
38% relative activity to D-glucose
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
36% of the activity with beta-D-glucose
-
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
36% of the activity with beta-D-glucose
-
-
?
2-deoxy-D-glucose + O2 + H2O
2-deoxy-D-glucono-1,5-lactone + H2O2
-
19.6% relative activity to D-glucose
-
?
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
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
? + H2O2
-
10% of the activity compared 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
4-deoxy-D-glucono-1,5-lactone + H2O2
-
7% activity compared to beta-D-glucose
-
-
?
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 + 1,4-benzoquinone
D-glucono-1,5-lactone + hydroquinone
-
-
-
-
?
beta-D-glucose + 1,4-benzoquinone
D-glucono-1,5-lactone + hydroquinone
-
-
-
-
?
beta-D-glucose + 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
beta-D-glucose + 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
beta-D-glucose + 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
beta-D-glucose + ferrocinium-methanol
?
-
-
-
-
?
beta-D-glucose + ferrocinium-methanol
?
-
-
-
-
?
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
-
-
-
?
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
-
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
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
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
enzyme assay using the ABTS/horseradish peroxidase system
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
the enzyme is highly specific for D-glucose
-
-
?
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
-
-
?
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
cofactor FAD is transiently reduced along the reaction mechanism
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
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
-
-
-
-
?
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
-
activities toward 2-deoxy-D-glucose, galactose and maltose are negligible when compared to the beta-D-glucose. The enzyme (GOD) does not show any activity toward arabinose, lactose, fructose, xylose and sucrose
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
activities toward 2-deoxy-D-glucose, galactose and maltose are negligible when compared to the beta-D-glucose. The enzyme (GOD) does not show any activity toward arabinose, lactose, fructose, xylose and sucrose
-
-
?
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
-
-
-
?
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
kinetic studies on the oxidation of beta-D-glucose combined with molecular modelling show the side chain of Arg516, which forms two hydrogen bonds with the 3-OH group of beta-D-glucose, to be absolutely essential for the efficient binding of beta-D-glucose. Of the residues forming the active site of glucose oxidase, Arg516 is the most critical amino acid for the efficient binding of beta-D-glucose by the enzyme, whereas aromatic residues at positions 73, 418 and 430 are important for the correct orientation and maximal velocity of glucose oxidation
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
kinetic studies on the oxidation of beta-D-glucose combined with molecular modelling show the side chain of Arg516, which forms two hydrogen bonds with the 3-OH group of beta-D-glucose, to be absolutely essential for the efficient binding of beta-D-glucose. Of the residues forming the active site of glucose oxidase, Arg516 is the most critical amino acid for the efficient binding of beta-D-glucose by the enzyme, whereas aromatic residues at positions 73, 418 and 430 are important for the correct orientation and maximal velocity of glucose oxidation
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
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
-
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
via cofactor FAD reduction to FADH2, reaction cycles, FADH2 reduces O2, overview
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
via cofactor FAD reduction to FADH2, reaction cycles, FADH2 reduces O2, overview
-
-
?
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
-
the beta-D-glucose serves as a donor of electrons and hydrogen ions, on other side of this complex reaction, oxygen dissolved in water-based reaction media is as an acceptor. Coenzyme FAD acts as electron shuttle during catalytic action of the enzyme, FAD is converted to FADH2
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
the beta-D-glucose serves as a donor of electrons and hydrogen ions, on other side of this complex reaction, oxygen dissolved in water-based reaction media is as an acceptor. Coenzyme FAD acts as electron shuttle during catalytic action of the enzyme, FAD is converted to FADH2
-
-
?
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
-
-
-
?
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
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
-
native enzyme and enzyme immobilized on mycelium pellets
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
native enzyme and enzyme immobilized on mycelium pellets
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
in a subsequent step D-glucono-1,5-lactone is nonenzymatically hydrolyzed to D-gluconic acid
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
cellular organism
-
-
-
?
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
Mycoderma aceti
-
-
-
?
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
-
kinetic mechanism
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
glucose is the primary substrate, recombinant enzyme
-
?
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
-
-
-
-
?
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
-
highly specific
-
?
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
-
highly specific
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
in a subsequent step D-glucono-1,5-lactone is nonenzymatically hydrolyzed to D-gluconic acid
?
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
-
2,6-dichloroindophenol, N,N,N',N'-tetramethyl-1,4-phenylenediamine, and 4-benzoquinone can function as electron acceptors
-
?
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
-
-
-
?
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
-
specific for D-glucose, 2,6-dichloroindophenol can act as artificial electron acceptor
-
?
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
-
highly specific
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
-
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
highly specific
-
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
-
highly specific
-
?
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
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
highly substrate specific enzyme
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
highly substrate specific enzyme
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
the enzyme is involved in apple fruit tissue browning
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
r
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
best substrate
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
best substrate
-
-
?
D-maltose + O2 + H2O
?
-
4.5% of D-glucose reactivity
-
?
D-maltose + O2 + H2O
?
-
4.5% of D-glucose reactivity
-
?
D-maltose + O2 + H2O
? + H2O2
-
22% of the activity with beta-D-glucose
-
-
?
D-maltose + O2 + H2O
? + H2O2
-
22% of the activity with beta-D-glucose
-
-
?
D-maltose + O2 + H2O
? + H2O2
-
21.3% relative activity to D-glucose
-
?
D-mannitol + O2
?
-
-
-
-
?
D-mannitol + O2
?
-
-
-
-
?
D-mannose + O2
?
7.2% of the activity with D-glucose for the native enzyme, 13.4 for the recombinant enzyme
-
-
?
D-mannose + O2
?
7.2% of the activity with D-glucose for the native enzyme, 13.4 for the recombinant enzyme
-
-
?
D-sorbitol + O2
?
-
-
-
-
?
D-sorbitol + O2
?
-
-
-
-
?
D-xylose + O2
?
3.0% of the activity with D-glucose for the native enzyme, 5.8 for the recombinant enzyme
-
-
?
D-xylose + O2
?
3.0% of the activity with D-glucose for the native enzyme, 5.8 for the recombinant enzyme
-
-
?
D-xylose + O2 + H2O
?
-
recombinant enzyme
-
?
D-xylose + O2 + H2O
?
-
4.8% of D-glucose reactivity
-
?
D-xylose + O2 + H2O
?
-
4.8% of D-glucose reactivity
-
?
D-xylose + O2 + H2O
?
-
3% relative activity to D-glucose
-
?
D-xylose + O2 + H2O
? + H2O2
-
11% of the activity with beta-D-glucose
-
-
?
D-xylose + O2 + H2O
? + H2O2
-
11% of the activity with beta-D-glucose
-
-
?
L-arabinose + O2
?
-
-
-
-
?
L-arabinose + O2
?
-
-
-
-
?
L-sorbose + O2
? + H2O2
-
15% activity compared to beta-D-glucose
-
-
?
L-sorbose + O2
? + H2O2
-
15% of the activity compared to beta-D-glucose
-
-
?
L-sorbose + O2
? + H2O2
-
15% of the activity compared to beta-D-glucose
-
-
?
L-sorbose + O2 + H2O
?
-
5.8% of D-glucose reactivity
-
?
L-sorbose + O2 + H2O
?
-
5.8% of D-glucose reactivity
-
?
L-sorbose + O2 + H2O
?
-
86% relative activity to D-glucose
-
-
?
mannose + O2
? + H2O2
-
9% of the activity compared to beta-D-glucose
-
-
?
mannose + O2
? + H2O2
-
9% of the activity compared to beta-D-glucose
-
-
?
mannose + O2 + H2O
? + H2O2
-
1% relative activity to D-glucose
-
?
mannose + O2 + H2O
? + H2O2
-
recombinant enzyme
-
?
mannose + O2 + H2O
? + H2O2
-
9% relative activity to D-glucose
-
?
mannose + O2 + H2O
? + H2O2
-
7.2% relative activity to D-glucose
-
?
sorbitol + O2
?
-
-
-
-
?
sorbitol + O2
?
-
-
-
-
?
xylitol + O2
?
-
-
-
-
?
xylitol + O2
?
-
best substrate
-
-
?
xylitol + O2
?
-
best substrate
-
-
?
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
?
-
His516 plays an important role in the reductive and oxidative half reaction
-
-
?
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
-
-
?
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 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
?
-
-
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
?
-
-
Rab8, Cdc42, Rho1, and Rho4 are associated with enriched vesicles carrying GOX activity
-
-
?
additional information
?
-
-
Rab8, Cdc42, Rho1, and Rho4 are associated with enriched vesicles carrying GOX activity
-
-
?
additional information
?
-
-
characterization of the allergen Mala s12, sequence similarity to glucose-methanol-choline (GMC) oxidoreductase enzyme superfamily, no enzyme activity of the recombinant protein in oxidase or dehydrogenase assay determined
-
-
?
additional information
?
-
-
the enzyme is the predominant source of H2O2 in ligninolytic cultures, H2O2 plays a central role in lignin biodegradation, it is obligately required for the activity of ligninases, a family of lignin peroxidases that is important in the oxidative depolymerization of lignin
-
-
?
additional information
?
-
-
the enzyme is the predominant source of H2O2 in ligninolytic cultures, H2O2 plays a central role in lignin biodegradation, it is obligately required for the activity of ligninases, a family of lignin peroxidases that is important in the oxidative depolymerization of lignin
-
-
?
additional information
?
-
-
important role in lignin-degradation
-
-
?
additional information
?
-
-
AldO catalyzes the C1 oxidation of several polyols
-
-
?
additional information
?
-
-
substrate specificity,besides alditols, 1,2-diols are reasonable substrates indicating that two adjacent hydroxy groups at C-1 and C-2 seem to be a minimal requirement for a compound in order to be effectively oxidized by AldO, overview
-
-
?
additional information
?
-
-
AldO catalyzes the C1 oxidation of several polyols
-
-
?
additional information
?
-
-
substrate specificity,besides alditols, 1,2-diols are reasonable substrates indicating that two adjacent hydroxy groups at C-1 and C-2 seem to be a minimal requirement for a compound in order to be effectively oxidized by AldO, overview
-
-
?
additional information
?
-
-
less than 2.5% of the activity with beta-D-glucose with arabinose, lactose, mannitol, sucrose and fructose
-
-
?
additional information
?
-
-
the enzyme interacts with redox mediators, e.g. 9,10-phenantroline-5,6-dione, 9,10-phenanthrenequinone, N-methylphenazonium methyl sulfate, ferrocene, ferrocenecarboxylic acid, alpha-methylferrocenemethanol, ferrocenecarboxaldehyde. 9,10-phenantroline-5,6-dione and 9,10-phenanthrenequinone are the best redox mediators or electron acceptors for this type of GOx. The redox mediators in a reaction mixture containing glucose, GOx and 1,4-benzoquinone lead to a 1.4-7.9fold rise of the 1,4-benzoquinone reduction rate, method evaluation
-
-
?
additional information
?
-
-
the enzyme interacts with redox mediators, e.g. 9,10-phenantroline-5,6-dione, 9,10-phenanthrenequinone, N-methylphenazonium methyl sulfate, ferrocene, ferrocenecarboxylic acid, alpha-methylferrocenemethanol, ferrocenecarboxaldehyde. 9,10-phenantroline-5,6-dione and 9,10-phenanthrenequinone are the best redox mediators or electron acceptors for this type of GOx. The redox mediators in a reaction mixture containing glucose, GOx and 1,4-benzoquinone lead to a 1.4-7.9fold rise of the 1,4-benzoquinone reduction rate, method evaluation
-
-
?
additional information
?
-
-
less than 2.5% of the activity with beta-D-glucose with arabinose, lactose, mannitol, sucrose and fructose
-
-
?
additional information
?
-
no activity with L-arabinose and D-galactose with the native and recombinant enzyme
-
-
?
additional information
?
-
no activity with L-arabinose and D-galactose with the native and recombinant enzyme
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
D-glucose + O2
D-glucono-1,5-lactone + H2O2
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
beta-D-glucose + O2
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
-
-
in a subsequent step D-glucono-1,5-lactone is nonenzymatically hydrolyzed to D-gluconic acid
?
beta-D-glucose + O2 + H2O
D-glucono-1,5-lactone + H2O2
cellular organism
-
-
-
?
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
Mycoderma aceti
-
-
-
?
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
-
-
in a subsequent step D-glucono-1,5-lactone is nonenzymatically hydrolyzed to D-gluconic acid
?
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
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
the enzyme is involved in apple fruit tissue browning
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
-
-
-
?
D-mannitol + O2
?
-
-
-
-
?
D-mannitol + O2
?
-
-
-
-
?
D-sorbitol + O2
?
-
-
-
-
?
D-sorbitol + O2
?
-
-
-
-
?
sorbitol + O2
?
-
-
-
-
?
sorbitol + O2
?
-
-
-
-
?
xylitol + O2
?
-
-
-
-
?
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
?
-
-
Rab8, Cdc42, Rho1, and Rho4 are associated with enriched vesicles carrying GOX activity
-
-
?
additional information
?
-
-
Rab8, Cdc42, Rho1, and Rho4 are associated with enriched vesicles carrying GOX activity
-
-
?
additional information
?
-
-
the enzyme is the predominant source of H2O2 in ligninolytic cultures, H2O2 plays a central role in lignin biodegradation, it is obligately required for the activity of ligninases, a family of lignin peroxidases that is important in the oxidative depolymerization of lignin
-
-
?
additional information
?
-
-
the enzyme is the predominant source of H2O2 in ligninolytic cultures, H2O2 plays a central role in lignin biodegradation, it is obligately required for the activity of ligninases, a family of lignin peroxidases that is important in the oxidative depolymerization of lignin
-
-
?
additional information
?
-
-
important role in lignin-degradation
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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10
(R)-1-phenyl-1,2-ethanediol
-
pH 7.5, 30°C
86
(S)-1-phenyl-1,2-ethanediol
-
pH 7.5, 30°C
170
1,2,4-butanetriol
-
pH 7.5, 30°C
150
1,2-Butanediol
-
pH 7.5, 30°C
97
1,2-hexanediol
-
pH 7.5, 30°C
52
1,2-pentanediol
-
pH 7.5, 30°C
3.33
1,4-benzoquinone
-
pH 5.5, 35°C
83
1-phenyl-1,2-ethanediol
-
pH 7.5, 30°C
0.0368
2,6-dichloroindophenol
-
-
35
2-amino-1-pentanol
-
pH 7.5, 30°C
8.3 - 49.8
2-deoxy-D-glucose
250
3-butene-1,2-diol
-
pH 7.5, 30°C
480
3-butenol
-
pH 7.5, 30°C
42
4-pentene-1,2-diol
-
pH 7.5, 30°C
0.019 - 733
beta-D-glucose
36
D-mannitol
-
pH 7.5, 30°C
1.4
D-sorbitol
-
pH 7.5, 30°C
0.19
di-(2,2'-bipyridinyl)ruthenium(III)dichloride
-
pH 7.3, 30°C
0.0638 - 0.1107
ferrocinium-methanol
350
glycerol
-
pH 7.5, 30°C
430
L-arabinose
-
pH 7.5, 30°C
25
L-Threitol
-
pH 7.5, 30°C
2.9 - 7
methyl-1,4-benzoquinone
2.43
phenazine methosulfate
-
pH 4.7
0.32
xylitol
-
pH 7.5, 30°C
0.694
[(1,10-phenanthroline)2(Cl)2Ru(III)]
-
pH 7.3, 30°C
0.019
[(1,8-dimethyl-4,5-phenanthroline)3Ru(II)]PF6-
-
pH 7.3, 30°C
0.52
[(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(III)]
-
pH 7.3, 30°C
0.0313
[(2,2'-(4,4'dimethyl)bipyridine)2(Cl)2Ru(III)]PF6-
-
pH 7.3, 30°C
0.0922
[(2,2'-bipyridine)2(CO32-)1/2Ru(III)]
-
pH 7.3, 30°C
0.153
[(2,2'-bipyridine)2(H2O)2Ru(III)]PF6-
-
pH 7.3, 30°C
0.0513
[(2,2'-bipyridine)2(SCN-)2Ru(III)]
-
pH 7.3, 30°C
0.057
[(2,2'-bipyridine)3Ru(II)]PF6-
-
pH 7.3, 30°C
additional information
additional information
-
8.3
2-deoxy-D-glucose
-
recombinant enzyme
28.1 - 49.8
2-deoxy-D-glucose
-
pH 5.0, 25°C
0.019
beta-D-glucose
-
native enzyme in solution, pH 5.5, temperature not specified in the publication
0.149
beta-D-glucose
immobilized enzyme, pH and temperature not specified in the publication
1.51 - 3.4
beta-D-glucose
-
depending on O2-concentration, comparison of values with enzyme immobilized on various materials
1.6
beta-D-glucose
-
64°C, pH not specified in the publication
1.9
beta-D-glucose
-
0.05 M Tris buffer, pH 8
1.9
beta-D-glucose
-
purified enzyme under argon, in 20 mM phosphate buffer pH 7.4 at 37°C
2
beta-D-glucose
-
0.1 M Tris buffer, pH 8
2 - 4
beta-D-glucose
25°C, pH 6.0, mutant enzyme Y73F
2 - 14
beta-D-glucose
-
pH 3.45, 35°C
2.1
beta-D-glucose
-
second polyethyleneimine/GOD bilayer
2.5
beta-D-glucose
-
non-purified enzyme under argon, in 20 mM phosphate buffer pH 7.4 at 37°C
2.5
beta-D-glucose
-
recombinant wild-type enzyme, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
2.6
beta-D-glucose
-
recombinant mutant K424E, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
2.9
beta-D-glucose
-
first polyethyleneimine/GOD bilayer
3.2
beta-D-glucose
-
recombinant mutant K424E, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
3.4
beta-D-glucose
-
recombinant mutant K424I, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
3.8
beta-D-glucose
-
recombinant wild-type enzyme, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme
4
beta-D-glucose
-
immobilized enzyme, immobilized membrane with ratio stretching 1.25
4 - 5.4
beta-D-glucose
-
immobilized enzyme
4.4
beta-D-glucose
-
0.6 M sodium acetate buffer, pH 6
4.5
beta-D-glucose
-
immobilized enzyme, methanol treated
5
beta-D-glucose
-
0.1 M sodium acetate buffer, pH 5
5.2
beta-D-glucose
-
0.1 M sodium acetate buffer, pH 6
5.4
beta-D-glucose
-
immobilized enzyme, immobilized membrane with ratio stretching 3
5.7
beta-D-glucose
-
native enzyme
5.8
beta-D-glucose
25°C, pH 6.0, mutant enzyme H520A
6.2
beta-D-glucose
-
recombinant enzyme
6.2
beta-D-glucose
25°C, pH 6.0, wild-type enzyme
6.3
beta-D-glucose
-
deglycosylated enzyme
6.3
beta-D-glucose
-
wild-type enzyme conjugated to gold nanoparticles, pH and temperature not specified in the publication
6.4
beta-D-glucose
-
0.1 M sodium phosphate buffer, pH 7
6.7
beta-D-glucose
-
0.1 M potassium phosphate buffer, pH 7
6.7
beta-D-glucose
25°C, pH 6.0, mutant enzyme H520V
7.1
beta-D-glucose
-
0.1 M sodium acetate buffer, pH 4.5
7.9
beta-D-glucose
-
randomly mixed polyethyleneimine/GOD
8
beta-D-glucose
-
enzyme adsorbed on 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol) coated matrix, high enzyme concentration, pH 5.5, temperature not specified in the publication
8.1
beta-D-glucose
-
0.1 M potassium phosphate buffer, pH 6
8.2
beta-D-glucose
-
mutant H447C conjugated to gold nanoparticles, pH and temperature not specified in the publication
10.5
beta-D-glucose
-
in 50 mM sodium acetate buffer (pH 5.4). at 45°C
11.43
beta-D-glucose
recombinant mutant M12 expressed in Pichia pastoris, pH 7.4, 25°C
11.7
beta-D-glucose
-
recombinant enzyme yGOXpenag, using O2 as cosubstrate, pH 6.0, 50°C
11.9
beta-D-glucose
-
purified enzyme under O2, in 20 mM phosphate buffer pH 7.4 at 37°C
12
beta-D-glucose
-
enzyme adsorbed on 11-amino-1-undecanethiol coated matrix, pH 5.5, temperature not specified in the publication
12.42
beta-D-glucose
-
in the presence of 0.6 M trehalose, at 25°C
13.3
beta-D-glucose
25°C, pH 6.0, mutant enzyme F418V
13.33
beta-D-glucose
recombinant mutant M12 enzyme expressed in Pichia pastoris, pH 5.5, 25°C
14.7 - 15.3
beta-D-glucose
-
pH 5.0, 25°C
14.98
beta-D-glucose
pH 5.5, temperature not specified in the publication, mutant enzyme T30V/I94V/A162T
15
beta-D-glucose
-
mutant H447C, pH and temperature not specified in the publication
16
beta-D-glucose
recombinant enzyme mutant B11, pH 5.5, 25°C
16
beta-D-glucose
pH 5.5, 25°C, mutant enzyme B11-GOx
16.5
beta-D-glucose
-
0.1 M sodium acetate buffer, pH 4
16.95
beta-D-glucose
recombinant enzyme, in 0.1 M sodium phosphate buffer, pH 6.0, at 35°C
17.5
beta-D-glucose
pH 5.1, 37°C, unmodified enzyme
18.1
beta-D-glucose
recombinant mutant M12 enzyme expressed in Saccharomyces cerevisiae, pH 5.5, 25°C
18.2
beta-D-glucose
-
recombinant enzyme yGOXpenag, using ferrocinium-methanol as cosubstrate, pH 6.0, 50°C
18.4
beta-D-glucose
-
pH 7.0, 25°C
18.54
beta-D-glucose
pH 5.5, temperature not specified in the publication, mutant enzyme T30V/I94V/A162T/R537K/M556V
18.76
beta-D-glucose
-
in the absence of trehalose, at 25°C
19.76
beta-D-glucose
pH 5.5, temperature not specified in the publication, mutant enzyme T30V/R37K/I94V/V106I/A162T/M556V
22
beta-D-glucose
-
soluble enzyme
22
beta-D-glucose
pH 5.5, 25°C, wild-type enzyme
22
beta-D-glucose
-
enzyme adsorbed on 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol) coated matrix, low enzyme concentration, pH 5.5, temperature not specified in the publication
22
beta-D-glucose
-
recombinant mutant K424I, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme
22
beta-D-glucose
recombinant wild-type enzyme expressed in Saccharomyces cerevisiae, pH 5.5, 25°C
22
beta-D-glucose
recombinant wild-type enzyme, pH 5.5, 25°C
22.5
beta-D-glucose
-
0.6 M sodium acetate buffer, pH 4.5
23.19
beta-D-glucose
recombinant wild-type enzyme expressed in Pichia pastoris, pH 7.4, 25°C
23.2
beta-D-glucose
pH 5.1, 37°C, aniline-modified enzyme
23.7
beta-D-glucose
-
BTL wild-type strain enzyme
25.2
beta-D-glucose
-
free enzyme
26 - 30
beta-D-glucose
-
enzymes obtained from different companies
27
beta-D-glucose
25°C, pH 6.0, mutant enzyme W430A
27.9
beta-D-glucose
recombinant enzyme mutant B11 in fusion with Aga2, pH 5.5, 25°C
28
beta-D-glucose
-
periodate-oxidized enzyme
28.26
beta-D-glucose
recombinant wild-type enzyme expressed in Pichia pastoris, pH 5.5, 25°C
28.26
beta-D-glucose
pH 5.5, temperature not specified in the publication, wild-type enzyme
28.8
beta-D-glucose
recombinant free enzyme, pH 6.0, 30°C
29.7
beta-D-glucose
recombinant immobilized enzyme, pH 6.0, 30°C
30
beta-D-glucose
-
native enzyme
30
beta-D-glucose
pH 6.0, 25°C, glycosylated enzyme
31.8
beta-D-glucose
-
commercially available enzyme
32.4
beta-D-glucose
pH 5.1, 37°C, benzoate-modified enzyme
33
beta-D-glucose
-
soluble enzyme
33
beta-D-glucose
pH 6.0, 25°C, deglycosylated enzyme
33.4
beta-D-glucose
recombinant wild-type enzyme in fusion with Aga2, pH 5.5, 25°C
34.9
beta-D-glucose
-
at pH 8.2, 40°C
35
beta-D-glucose
-
deglycosylated enzyme
36
beta-D-glucose
25°C, pH 6.0, mutant enzyme N518T
37
beta-D-glucose
-
native enzyme
37 - 38
beta-D-glucose
-
-
37 - 38
beta-D-glucose
-
-
38
beta-D-glucose
-
carbohydrate-depleted enzyme
38.1
beta-D-glucose
-
at pH 8.2, 50°C
44
beta-D-glucose
-
immobilized enzyme
44.9
beta-D-glucose
-
at pH 8.2, 60°C
50
beta-D-glucose
-
pH 6.01, 35°C
50.3
beta-D-glucose
-
native enzyme, using O2 as cosubstrate, pH 6.5, 70°C
53.24
beta-D-glucose
-
pH 4.5, 60°C
55.2
beta-D-glucose
-
at pH 8.2, 70°C
65.7
beta-D-glucose
pH 6.0, 30°C
67
beta-D-glucose
-
pH 4.82, 35°C
69
beta-D-glucose
pH 7.0, 20-25°C, mutant enzyme Y169C/A211C
71.2
beta-D-glucose
-
native enzyme, using ferrocinium-methanol as cosubstrate, pH 6.5, 70°C
72
beta-D-glucose
-
immobilized enzyme
78
beta-D-glucose
25°C, pH 6.0, mutant enzyme F418
87
beta-D-glucose
-
pH 4.52, 35°C
89.13
beta-D-glucose
-
pH 6.0, 37°C
89.13
beta-D-glucose
-
pH and temperature not specified in the publication
96.4
beta-D-glucose
-
wild-type enzyme, pH and temperature not specified in the publication
103
beta-D-glucose
pH 7.0, 20-25°C, wild-type enzyme
106
beta-D-glucose
-
pH 4.27, 35°C
130
beta-D-glucose
-
pH 3.88, 35°C
513
beta-D-glucose
25°C, pH 6.0, mutant enzyme R516K
537
beta-D-glucose
-
pH 2.84, 35°C
733
beta-D-glucose
25°C, pH 6.0, mutant enzyme R516Q
76.9 - 126.3
D-galactose
-
pH 5.0, 25°C
952
D-galactose
-
recombinant enzyme
12.5
D-glucose
-
-
13.5
D-glucose
pH 5.0, 28°C, native enzyme
15.25
D-glucose
pH 5.0, 28°C, recombinant enzyme
15.6
D-glucose
-
pH 5.0, 25°C, enzyme fraction 1
21.9
D-glucose
-
pH 5.0, 25°C, enzyme fraction 2
25
D-glucose
-
pH 5.5, 40°C
26
D-glucose
-
native enzyme
55.5
D-maltose
-
-
57.3
D-maltose
-
pH 5.0, 25°C
44
D-mannose
-
-
106
D-mannose
-
recombinant enzyme
33
D-xylose
-
-
42.9 - 70.7
D-xylose
-
pH 5.0, 25°C
384
D-xylose
-
recombinant enzyme
0.0638
ferrocinium-methanol
-
recombinant enzyme yGOXpenag, pH 6.0, 50°C
0.1107
ferrocinium-methanol
-
native enzyme, pH 6.5, 70°C
2.9
methyl-1,4-benzoquinone
-
low pH, 35°C
3.25
methyl-1,4-benzoquinone
-
pH 2.84, 35°C
3.97
methyl-1,4-benzoquinone
-
pH 3.45, 35°C
4.98
methyl-1,4-benzoquinone
-
pH 3.88, 35°C
5.7
methyl-1,4-benzoquinone
-
pH 4.27, 35°C
6.22
methyl-1,4-benzoquinone
-
pH 4.52, 35°C
6.63
methyl-1,4-benzoquinone
-
pH 4.82, 35°C
6.94
methyl-1,4-benzoquinone
-
pH 6.01, 35°C
7
methyl-1,4-benzoquinone
-
pH 7, 35°C
0.18
O2
-
periodate-oxidized enzyme
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
values for glyco-enzyme and aglyco-enzyme
-
additional information
additional information
-
KM-value of immunoaffinity-layered glucose oxidase preparations remains unaltered
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
thermodynamics
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
kinetics of enzyme-pentacyanoferrate(III)-nucleophilic ligands-complex interactions, detailed overview
-
additional information
additional information
-
steady-state kinetics, overview
-
additional information
additional information
-
choline, glucose, myo-inositol, methanol, ethanol, 1-pentanol, benzyl alcohol, 2-phenylethanol, cholesterol or lauryl alcohol tested as potential substrates, recombinant protein devoid of either oxidase or dehydrogenase activity
-
additional information
additional information
-
substrate specificity and steady state kinetics, overview
-
additional information
additional information
-
enzyme thermodynamics and kinetics
-
additional information
additional information
Michaelis-Menten kinetics of immobilized enzyme GOx and free enzyme GOx
-
additional information
additional information
kinetic limitations of a bioelectrochemical electrode using carbon nanotube-attached glucose oxidase for biofuel cells. Carbon nanotube-supported glucose oxidase is examined in the presence of 1,4-benzoquinone. The intrinsic Michaelis parameters of the reaction catalyzed by carbon nanotube-glucose-oxidase are very close to those of native enzyme. However, the Nafion entrapment of carbon nanotube-glucose-oxidase for an electrode results in a much lower activity due to the limited availability of the embedded enzyme. Kinetic studies reveal that the biofuel cell employing such an enzyme electrode only generate a power density equivalent to less than 40% of the reaction capability of the enzyme on electrode. Factors such as electron and proton transfer resistances can be more overwhelming than the heterogeneous reaction kinetics in limiting the power generation of such biofuel cells
-
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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
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
F414Y
increased electron transfer
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
I94V/T30S
increased O2 sensitivity, increased electron transfer (1.9fold)
L500D
site-directed mutagenesis, inactive mutant
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
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
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
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/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
V20Y
increased electron transfer
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
H220D
-
site-directed mutagenesis, mutant H220D shows increased thermosensitivity and reduced activity compared to the wild-type enzyme
-
Q124R/L569E
-
site-directed mutagenesis, the mutation has no significant effect on stability but causes a twofold increase of the enzyme's specific activity
-
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
-
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
-
F418A
12.6fold increase in apparent Km value
H520A
the enzyme variant is almost completely inactive
H520V
the enzyme variant is almost completely inactive
H563A
the enzyme variant is completely inactive
H563V
the enzyme variant is completely inactive
K19E
-
site-directed mutagenesis
K23E
-
site-directed mutagenesis
K260E.
-
site-directed mutagenesis
K424I
-
site-directed mutagenesis, the mutation does not significantly affect the enzyme activity
K48/50E
-
site-directed mutagenesis
Q184E
-
site-directed mutagenesis
Q75E
-
site-directed mutagenesis
R516K
the mutant enzyme whose side chain forms only one hydrogen bond with the 3-OH group of beta-D-glucose, exhibits an 80fold higher apparent Km (513 mM) but a Vmax only 70% lower than the wild type
R516Q
the complete elimination of a hydrogen-bond interaction between residue 516 and the 3-OH group of beta-D-glucose through the substitution R516Q effects a 120fold increase in the apparent Km for glucose (to 733 mM) and a decrease in the Vmax to 1/30
S114A/F355L
increased electron transfer, 88% decrease in O2 sensitivity
V464A/K424E
2.4fold increase in electron transfer, 95% decrease in O2 sensitivity
V564S
1.1fold increase in electron transfer, 88% decrease in O2 sensitivity
F418A
-
12.6fold increase in apparent Km value
-
H520A
-
the enzyme variant is almost completely inactive
-
R516K
-
the mutant enzyme whose side chain forms only one hydrogen bond with the 3-OH group of beta-D-glucose, exhibits an 80fold higher apparent Km (513 mM) but a Vmax only 70% lower than the wild type
-
R516Q
-
the complete elimination of a hydrogen-bond interaction between residue 516 and the 3-OH group of beta-D-glucose through the substitution R516Q effects a 120fold increase in the apparent Km for glucose (to 733 mM) and a decrease in the Vmax to 1/30
-
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
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
mutant enzyme displays better catalytic properties than the native enzyme
Y169C/A211C
compared with wild-type enzyme, the half-life of the mutant, at 40 °C increases approximately 48fold. The kcat and catalytic efficiency are enhanced 0.7fold and 1.6fold, respectively
Y169C/A211C
-
compared with wild-type enzyme, the half-life of the mutant, at 40 °C increases approximately 48fold. The kcat and catalytic efficiency are enhanced 0.7fold and 1.6fold, respectively
-
G423D
-
site-directed mutagenesis, the mutant shows no activity compared to the wild-type enzyme
G423D
-
site-directed mutagenesis, the mutants containing the mutation G423D leads to quadruple mutants that are not able to reconstitute. The mutant enzymes displays a dramatic decrease in activity compared to thré wild-type enzyme
K424E
-
site-directed mutagenesis, the single mutation results in a significant increase in the current density which becomes 2.4 fold higher than the current obtained for the wild-type
K424E
increased electron transfer (2.4fold), 20% decrease in O2 sensitivity
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
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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
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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
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
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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
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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
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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
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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
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
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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
the removal of aromatic or bulky residues at positions 73, 418 or 430 result in decreases in the maximum rates of glucose oxidation to less than 1/90
additional information
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the removal of aromatic or bulky residues at positions 73, 418 or 430 result in decreases in the maximum rates of glucose oxidation to less than 1/90
additional information
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for use on electrode surfaces, the key amino acid at the entrance of the active site of glucose oxidase from Penicilium amagasakiense, Lys424, Gln75, Gln184, and Gly423, are redesign by nonactive site mutations, leading to enzymatic anodes with 2.4fold higher current densities, making the biosensor more effective. 424 is the key position
additional information
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the removal of aromatic or bulky residues at positions 73, 418 or 430 result in decreases in the maximum rates of glucose oxidation to less than 1/90
-
additional information
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construction of a Penicillium funiculosum highly active strain 46.1 from parental strain BIM F-15 as a producer of extracellular GOx by induced mutagenesis technique. The GOx from Penicillium funiculosum strain 46.1 differs from GOx purified from the parent strain BIM F-15 by reduced Michaelis constant, higher efficiency of glucose oxidation, pH dependence, and thermal stability, but it has similar thermal optimum. The enzyme-encoding gene has no special mutation
additional information
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construction of a Penicillium funiculosum highly active strain 46.1 from parental strain BIM F-15 as a producer of extracellular GOx by induced mutagenesis technique. The GOx from Penicillium funiculosum strain 46.1 differs from GOx purified from the parent strain BIM F-15 by reduced Michaelis constant, higher efficiency of glucose oxidation, pH dependence, and thermal stability, but it has similar thermal optimum. The enzyme-encoding gene has no special mutation
-
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15 - 70
-
the enzyme shows a pH-dependent response to the high pressure homogenization treatment, with reduction or maintenance of activity at pH 4.5-6.0 and a remarkable activity increase (30-300%) at pH 6.5 at all tested temperatures. i.e. 15°C, 50°C and 75°C. The enzyme's thermal tolerance is reduced due to high pressure homogenization treatment and the storage for 24 h at high temperatures of 50°C and 75°C also causes a reduction of activity
20 - 40
50% of enzyme activity is maintained after 90 min incubation at 20-40°C
20 - 60
the activity of recombinant GOD increases slightly at the reaction temperature ranging from 20-40°C, and then falls moderately till 60°C. The recombinant enzyme retains more than 90% of activity within 40°C. Over 30% of activity is lost at 50°C, whereas almost no activity is detected above 60°C
25
-
10 h, purified enzyme, stable
25 - 70
-
70% relative activity after 30 min at 25°C, 100% activity after 30 min at 30°C, 90% relative activity after 30 min at 37°C, 75% relative activity after 30 min at 50°C, 30% relative activity after 30 min at 70°C
30 - 50
purified recombinant free enzyme and immobilized enzyme, the enzyme activity remains rather unchanged from 30-45°C and then drops at higher temperatures. The thermal stability of immobilized GOx is only slightly higher than that of the free enzyme
4 - 54
-
1 h, the enzyme retains at least 80% activity
40 - 60
purified recombinant enzyme, more than 90% activity remaining after incubation for 30 min at 50°C and 54% at temperatures up to 55°C
45 - 65
-
at 45°C the enzyme half-life is 99 min and at 65°C it is 20.38 min under similar conditions
47
-
after 6 h of incubation the percentage of activity is 68%
50 - 60
-
at pH 6.0 and at 50°C, the half life of the enzyme is about 20 h, thermal denaturation is observed above 60°C
50 - 70
-
the half-life is diminished from 210 min at 50°C to 0.61 min at 70°C, the inactivation rate constant decreases by up to 50% at temperatures between 50 and 70°C in the presence of 0.6 M trehalose
50.6
Tm-value of wild-type enzyme: 50.6°C
54
-
after 6 h of incubation the percentage of activity is 11%
55.8
-
transition temperature is independent of the protein concentration. The thermally denatured enzyme is a compact structure, a form of molten globule-like apoenzyme
56
-
half-life of native enzyme without additive: 86 min, half-life of enzyme in presence of lysozyme: 322 min, half-life of enzyme in presence of 1 M NaCl: 1806 min, half-life of enzyme in presence of 0.2 M K2SO4: 1446 min
58.6
Tm-value of mutant enzyme Y169C/A211C
59
-
midpoint for thermal inactivation of residual activity and dissocation of FAD
62
-
midpoint for loss of secondary and tertiary structure
63
-
half-life of native enzyme without additive: 7.5 min, half-life of enzyme in presence of lysozyme: 24 min, half-life of enzyme in presence of 1 M NaCl: 146 min, half-life of enzyme in presence of 0.2 M K2SO4: 62 min
67
-
half-life of native enzyme without additive: 4.5 min, half-life of enzyme in presence of lysozyme: 12 min, half-life of enzyme in presence of 1 M NaCl: 58 min, half-life of enzyme in presence of 0.2 M K2SO4: 27.5 min
72.4
-
denaturation point of native enzyme
72.8
-
denaturation point of periodate-oxidized enzyme
73
-
70% loss of activity after 60 min
75
purified recombinant free enzyme, loss of 50% activity
30
-
purified enzyme, completely stable for at least 180 min
30
-
stable for a minimum of 180 min
30
1 h, 10% loss of activity, recombinant enzyme
30
-
after 6 h of incubation the percentage of activity is 79%
35
-
half-life: 78.48 h
37
-
GOD has half-life of approximately 30 min at 37°C, immobilized GOD is more effective for applications at 37°C
37
-
at 37°C and in pH 7.5 buffer, the half life of the native enzyme is 48 h
37
-
loss in specific activity of PEGylated GOx and native GOx in the absence of glucose and at 37°C, the PEGylated enzyme is more stable and retains 62.6% after 24 h and about 40% after 30 days, the native enzyme retains 67.3% after 24 h and about 20% after 30 days, overview
37
-
at 37°C and in pH 7.5 buffer, the half life of the recombinant enzyme yGOXpenag is 6 h
37
-
half-life: 30 min, purified enzyme
40
-
60 min
40
-
at or below both the BTL wild-type strain enzyme and the commercially available enzyme are stable for at least 48 h
40
-
up to, soluble enzyme
40
-
purified enzyme, half-life: 30 min
40
1 h, no loss of activity, mutant enzyme Y169C/A211C. Half-life of mutant enzyme Y169C/A211C: 720 min. Half-life of wild-type enzyme: 15 min
40
-
up to, soluble enzyme
40
-
at pH 2-4 and pH 7-8, half life: less than 1 day
40
half-life native enzyme: 103 min, half-life recombinant enzyme: 26 min
45
-
bound to Blue Dextran, in the absence of added FAD, 60% activity retained after 3 h
45
1 h, complete loss of activity, recombinant enzyme. 30 min, 60% loss of activity, mutant enzyme Y169C/A211C
45
-
30 min, considerable inactivation
45
half-life native enzyme: 23 min, half-life recombinant enzyme: 3 min
50
-
up to, immobilized enzyme
50
-
both native and carbonhydrate-depleted enzyme retain full activity below
50
-
up to, native and deglycosylated enzyme
50
-
the poly(methyl methacrylate)-bovine serum albumin particle-adsorbed GOx only loses 28% of its activity in comparison with a 64% activity loss of free GOx when it is incubated at 50°C for 35 h
50
stable up to. At 50°C the enzyme is inactivated by 30% over a period of 11 h. The thermal stability is unaffected by the depletion of carbohydrate
50
the purified recombinant enzyme retains 90% activity at 50°C for 30 min
50
-
the activity of the free enzyme decreases to 30% of the original value, the activity of the immobilized enzyme scarcely decreases
50
-
at pH 6.0 and at 50°C, the half life of the enzyme is about 20 h, thermal denaturation is observed above 50°C
50
-
stable below, pH 5.6 for 15 min
55
-
native and carbohydrate-depleted enzyme, inactivation above
55
-
bound to Blue Dextran, in the absence of added FAD, 20% activity retained after 3 h
55
-
the commercially available enzyme is more stable than the BTL wild-type strain enzyme
55
purified dimeric enzyme, pH 5.8, stable up to, rapid inactivation above, the enzyme forms aggregates at incubation temperatures above 55°C, overview
55
-
purified enzyme, retains 57 % activity after 180 min
60
-
affinity-layered preparation retains 55% of the original activity after 2 h of preincubation, soluble enzyme loses almost 80% activity in 15 min
60
-
half-life of native enzyme without additive: 13 min, half-life of enzyme in presence of lysozyme: 46 min, half-life of enzyme in presence of 1 M NaCl: 434 min, half-life of enzyme in presence of 0.2 M K2SO4: 308 min
60
-
2 h, stable, insoluble enzyme complex
60
purified enzyme, residual activity after 10 min is 32.9% for the wild-type enzyme and 14.7% for enzyme mutant M12
60
t1/2: 10.5 min (wild-type enzyme), 9.0 (mutant enzyme T30V/I94V/A162T), 11.74 (mutant enzyme T30V/I94V/A162T/R537K/M556V), 15.75 (mutant enzyme T30V/R37K/I94V/V106I/A162T/M556V)
60
cellular organism
-
complete inactivation
65
-
the commercially available enzyme is more stable than the BTL wild-type strain enzyme
65
-
purified enzyme, loss of 50% activity after 27 min
65
-
soluble enzyme: inactivation, mycelia-bound: 85% activity retained
70
t1/2: 5 min
70
-
purified enzyme, inactivation
70
-
native GOx retains 48% activity after 10 min, the bioactivity is completely lost after 1 h at 70°C. The bioactivity of the enzyme-polymer conjugates (GOx-PPEG-A, GOx-PAA, GOx-PMA and GOx-PTBA) only slowly declines, GOx-PPEG-A, GOx-PAA, GOx-PMA and GOx-PTBA retain about 61%, 67%, 79%, and 73%, after 10 min and 28%, 24%, 35%, and 37% after 1 h, respectively, at 70°C. The four polymers, hydrophilic or hydrophobic, improve the thermal stability of enzyme GOx. Enzyme modified by hydrophobic polymers (PMA and PTBA) exhibit better thermal stability than that modified by hydrophilic ones (PPEG-A and PAA)
70
-
inmobilized enzyme, more than 60% of the activity remains
70
-
completely inactivated after 15 min in the absence of glucose and 50% inactivated in the presence of glucose
80
-
the pure enzyme is inactive at 80°C, thermal resistance is high only at pH 7.0
80
purified recombinant immobilizedenzyme, loss of 50% activity
80
at 240 MPa and 80.0°C, the first order rate constant of inactivation (k(inact)) of aniline-modified enzyme is 0.02/min, or 3.7 times smaller than for the native enzyme, while the k(inact) for benzoate-modified enzyme is 0.26/min, or 2.8times smaller than for the native enzyme at the same temperature. At 240 MPa and 80.0°C, the k(inact) of the aniline-modified enzyme is 69times smaller than the k(inact) of native enzyme (15.3/min) at 0.1 MPa and 80.0°C
additional information
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comparison of stability of enzyme from different sources
additional information
-
the enzyme is very stable at cold temperatures
additional information
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native and carbohydrate-depleted enzyme, no decrease of activity after 100 freeze-thaw cycles
additional information
-
the irreversible nature of thermal inactivation is caused by a change in the state of association of apoenzyme. The dissociation of FAD results in the loss of secondary and tertiary structure, leading the unfolding and nonspecific aggregation of the enzyme molecule because of hydrophobic interactions of side chains
additional information
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thermal denaturation of glucose oxidase is an irreversible transition to the compact denatured form with a defined oligomeric structure that is significantly different from the chemically denatured state of the enzyme, unfolded monomer
additional information
-
inactivation of the free enzyme within 10 min. 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 poly(ethyleneimine) and copper atoms in the enzyme's active site, 70% remaining activity after 60 min
additional information
analysis of thermal inactivation kinetics of enzyme GOD
additional information
glucose oxidase stabilization against thermal inactivation using high hydrostatic pressure and hydrophobic modification, method development, evaluation, and kinetics of thermal inactivation, detailed overview. Determination of the effect of temperature on the rate constant of inactivation of GOx at each of the selected pressures, and of the pressure effects on the rate constant of inactivation of GOx
additional information
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thermal inactivation thermodynamic parameters of GOx, overview
additional information
wild-type and mutant enzyme Y169C/A211C are cold adapted
additional information
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wild-type and mutant enzyme Y169C/A211C are cold adapted
additional information
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comparison of stability of enzyme from different sources
additional information
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enzyme denaturing process at different temperatures, localization of breaking points, analysis by molecular dynamics simulations, overview. Identification of the transition state of protein folding/unfolding, overview
additional information
-
glucose stabilizes against heat inactivation
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medicine
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analysis of the chronic inflammatory skin disorder Atopic eczema (AE)
pharmaceutical industry
-
enzyme immobilized both independently and together with catalase in gel of polyvinylalcohol in the form of membranes on cotton base, employment in food and pharmaceutical industries
agriculture
-
the enzyme can be used as pest control agent against Ephestia kuehniella. The enzyme shows approximately similar damage on the Ephestia kuehniella midgut including rupture and disintegration of the epithelial layer and cellular vacuolization
agriculture
-
the enzyme shows antifungal activity. It could become a natural alternative to synthetic fungicides to control certain important plant microbial diseases. The enzyme displays a wide inhibitory spectrum toward different fungi at a concentration of 20 AU. It has a strong inhibitor effect on mycelia growth and spore germination of Pythium ultimum
agriculture
-
the enzyme can be used as pest control agent against Ephestia kuehniella. The enzyme shows approximately similar damage on the Ephestia kuehniella midgut including rupture and disintegration of the epithelial layer and cellular vacuolization
-
agriculture
-
the enzyme shows antifungal activity. It could become a natural alternative to synthetic fungicides to control certain important plant microbial diseases. The enzyme displays a wide inhibitory spectrum toward different fungi at a concentration of 20 AU. It has a strong inhibitor effect on mycelia growth and spore germination of Pythium ultimum
-
analysis
-
coupling of the enzyme with Fenton's reagent used for the determination of glucose produced as a result of the hydrolysis of cellobiose catalyzed by beta-glucosidase
analysis
-
phosphate sensor consisting of glucose oxidase coimmobilized with glutaraldehyde with maltose phosphorylase and bovine serum albumin
analysis
-
enzyme immobilized in Bombyx mori silk fibroin membrane applied to glucose sensor
analysis
-
immobilized enzyme on polyacrylamide employed for the determination of glucose concentration in blood sera
analysis
-
biosensor system prepared for continuous flow analysis of enzyme activity
analysis
-
application in glucose biosensors. An unmediated, reagentless glucose biosensor is prepared with two polyethylenimine/glucose oxidase bilayers-modified pyrolytic graphite electrodes. A calibration linear range of glucose is 0.5-8.9 mM with a detection limit of 0.05 mM and sensitivity of 0.76 microA per mM
analysis
-
the enzym eis used in a model system to study physiological effects of hepatic H2O2 release on rat liver
analysis
the enzyme finds wide application in food industry and clinical analysis
analysis
-
the enzyme is useful in designing of biosensors for use in clinical, biochemical, and diagnostic assays
analysis
-
the enzyme might by useful in designing of biosensors for use in clinical, biochemical, and diagnostic assays
analysis
-
co-confined glucose oxidase and horseradish peroxidase bienzyme system as a biosensor for the detection of glucose gives a wider linear range of glucose than for free enzymes in solution
analysis
-
the enzyme is useful as biosensor for glucose detection
analysis
-
GOx is the main component in glucose biosensors for determination of glucose in industrial solutions and in body fluids such as blood and urine
analysis
-
te enzyme is used on electrode surfaces of biosensors
analysis
-
the enzyme GOx is applied in biosensor technologies
analysis
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. Promising application of enzymes developed by directed evolution tailored for the applications of biosensors and biofuel cells
analysis
-
the enzyme finds wide application in food industry and clinical analysis
-
analysis
-
the enzyme GOx is applied in biosensor technologies
-
analysis
-
the enzyme might by useful in designing of biosensors for use in clinical, biochemical, and diagnostic assays
-
analysis
-
GOx is the main component in glucose biosensors for determination of glucose in industrial solutions and in body fluids such as blood and urine
-
analysis
-
the enzyme is useful in designing of biosensors for use in clinical, biochemical, and diagnostic assays
-
biofuel production
-
glucose oxidase is typically used in the anode of biofuel cells to oxidise glucose
biofuel production
-
used in miniature membrane-less glucose/O2 biofuel cells
biofuel production
-
the enzyme used for biofuel cells
biofuel production
-
the enzyme used for biofuel cells
-
biotechnology
-
the enzyme encapsulated in the liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine is a useful biocatalyst for the prolonged glucose oxidation
biotechnology
-
GOX is the most widely used enzyme for the development of electrochemical glucose biosensors and biofuel cell in physiological conditions
biotechnology
-
GOX is the most widely used enzyme for the development of electrochemical glucose biosensors and biofuel cell in physiological conditions
biotechnology
-
transgenic expression of glucose oxidase may be deployed to improve cold tolerance potential of higher plants
biotechnology
bacteriostatic agent. The combination of different concentrations of glucose oxidase and glucose could significantly inhibit the growth of Agrobacterium and Escherichia coli in logarithmic phase during the fermentation process
biotechnology
the enzyme is used for a number of applications in biotechnology and clinical diagnostics
biotechnology
-
bacteriostatic agent. The combination of different concentrations of glucose oxidase and glucose could significantly inhibit the growth of Agrobacterium and Escherichia coli in logarithmic phase during the fermentation process
-
diagnostics
-
glucose oxidase can be used in various immunoassays and/or staining procedures as well as removal of excess glucose, in real-time fluorescent microscopy for biological samples, glucose oxidase/catalase is often used for oxygen scavenging to reduce photodamage
diagnostics
-
used in an automatic glucose assay kit in conjunction with catalase and chiefly in biosensors for the detection and estimation of glucose in industrial solutions and in body fluids such as blood and urine
diagnostics
the enzyme is used as a molecular diagnostic and analytical tool in the medical industry for the control of diabetes
diagnostics
the enzyme is used for the manufacture of glucose biosensors and in particular sensor strips used to measure glucose levels in serum
diagnostics
-
glucose biosensor
diagnostics
-
glucose biosensor
diagnostics
-
glucose biosensor
diagnostics
-
glucose biosensor
diagnostics
-
glucose biosensor
diagnostics
a glassy carbon electrode (GCE) is modified with carbon nanochips (CNCs), and glucose oxidase (GOx) is immobilized on the modified electrode surface. Chitosan (CS) is employed to fix the GOx/CNCs tightly to the surface of the GCE. Characterization of the modified electrode shows that glucose oxidase remains in its native structure when immobilized in CNC film. Application in glucose biosensing and biofuel cells
diagnostics
the enzyme is used for a number of applications in biotechnology and clinical diagnostics
diagnostics
-
the enzyme is used for the manufacture of glucose biosensors and in particular sensor strips used to measure glucose levels in serum
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energy production
design of a bioanode that directly utilizes starch as a fuel in an enzymatic biofuel cell. The enzymatic fuel cell is based on three enzymes (alpha-amylase, glucoamylase and glucose oxidase). The carbon paste electrode containing these three enzymes and tetrathiafulvalene can both saccharize and oxidize starchy biomass. In cyclic voltammetry, catalytic currents are successfully observed with both glucose and starchy white rice used as a substrate. A membraneless white rice/O2 biofuel cell is assembled and the electrochemical performance is evaluated. The three enzyme based electrode is used as a bioanode and an immobilized bilirubin oxidase (derived from Myrothecium verrucaria) electrode is used as a biocathode. The biofuel cell deliveres an open circuit voltage of 0.522 V and power density of up to 0.099 mW/cm
energy production
enzyme precipitates coatings of glucose oxidase onto carbon paper for biofuel cell applications. The direct immobilization of enzyme precipitation coatings on hierarchical-structured electrodes with a large surface area can further improve the power density of enzymatic biofuel cells and can make their applications more feasible
energy production
glucose oxidase/cellulose-carbon nanotube composite paper as a biocompatible bioelectrode for biofuel cells. Glucose oxidase, which is a redox enzyme capable of oxidizing glucose as a renewable fuel using oxygen, is immobilized on the CL-CNT composite paper. Cyclic voltammograms reveal that the GOx/CL-CNT paper electrode shows a pair of well-defined peaks, which agreed well with that of FAD/FADH2, the redox center of glucose oxidase. These results clearly show that the direct electron transfer between the glucose oxidase and the composite electrode is achieved. It is found that the glucose oxidase immobilized on the composite electrode retains catalytic activity for the oxidation of glucose
energy production
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. Promising application of enzymes developed by directed evolution tailored for the applications of biosensors and biofuel cells
energy production
triphenylmethane dyes are an alternative for mediated electronic transfer systems in glucose oxidase biofuel cells
food industry
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food and beverage additive, used for low alcohol wine production, used for glucose removal from dried egg, improvement of color, flavor, and shelf life of food materials, oxygen removal from fruit juices, canned beverages, and from mayonnaise to prevent rancidity, used as ingredient of toothpaste, for the production of gluconic acid, and as a food preservative
food industry
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food processing-additive, used for bread making (GOX is an effective oxidant to produce bread with improved texture and increased loaf volume), and in dry egg powder, used as preservative in packaged food and for reduced alcohol wine production
food industry
the enzyme is used as food preservative and color stabilizer
food industry
Horseradish peroxidase, glucose oxidase, and glucose can be applied efficiently to modify several physicochemical properties (especially rheological and emulsifying properties) of soybean protein isolate. Soybean protein products are widely applied in processed foods as important ingredients, due to their higher nutritive values and desirable functional properties. Physical, chemical, and enzymatic modifications can be used to treat food proteins for property improvement
food industry
mutant enzyme Y169C/A211C is a good candidate for the bread baking industry. It has a significant effect on bread volume. Its improved thermostability, pH stability, and catalytic activity, its resistance to SDS, maximal enzymatic activity at low temperatures, and high activity under alkaline conditions are valuable properties that in addition to the bread baking industry
food industry
potentially useful in food biopreservation, application for the preservation of aquatic products at low-temperatures, good antimicrobial effect against common fish pathogenic bacteria (Listeria monocytogenes and Vibrio parahaemolyticus), excellent freshness preserving agent in the context of the grass carp
food industry
the enzyme is used in clinical, pharmaceutical, food and chemical industries
food industry
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the enzyme is used in clinical, pharmaceutical, food and chemical industries
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food industry
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mutant enzyme Y169C/A211C is a good candidate for the bread baking industry. It has a significant effect on bread volume. Its improved thermostability, pH stability, and catalytic activity, its resistance to SDS, maximal enzymatic activity at low temperatures, and high activity under alkaline conditions are valuable properties that in addition to the bread baking industry
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industry
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oxygen scavenger, chemical bleaching, used for gluconic acid production and in glucose sensor/assays
industry
in the textile industry, enzyme GOX is used for bio-bleaching and in oral care products as antimicrobial agent
industry
the enzyme is used in clinical, pharmaceutical, food and chemical industries
industry
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in the textile industry, enzyme GOX is used for bio-bleaching and in oral care products as antimicrobial agent
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industry
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the enzyme is used in clinical, pharmaceutical, food and chemical industries
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synthesis
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preparative production of hydroquinone using a column packed with the enzyme immobilized onto alumina, O2 is replaced with benzoquinone
synthesis
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enzymatic biotransformation of (4R)-limonene to carvone involves addition of glucose oxidase and peroxidase to the biotransformation medium
synthesis
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AldO is an enantioselective biocatalyst for the kinetic resolution of racemic 1,2-diols
synthesis
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GOD is used as a commercial source of gluconic acid, which can be produced by the hydrolysis of delta-glucono-1, 5-lactone, the endproduct of GOD catalysis
synthesis
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utilization of recombinant enzyme expressed in the periplasm or on the cell surface of Escherichia coli as biocatalyst in a non-laborious and non-costly whole-cell application for reacting on towards different polyols such as xylitol and sorbitol
synthesis
recombinant Aga2-GOx fusion proteins in the Saccharomyces cerevisiae cell wall can be used as immobilized catalysts for the production of gluconic acid
synthesis
the enzyme is used in the production of gluconic acid
synthesis
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. Poly(N-vinyl)caprolactam (PVCL) microgels are synthesized by precipitation polymerization initiated by the enzyme and a conventional azo-initiator 2,2'-azobis(N-(2-carboxyethyl)-2-methylpropionamidine) tetrahydrate. The use of enzymes in precipitation polymerization leads to the encapsulation of enzymes in formed microgels. After the GOx-induced polymerization and purification of the microgels, high enzyme activity could be determined in the microgels, enabling facile synthesis of core-shell microgels. The glucose oxidase-based initiator system is a powerful and promising alternative to azo- or peroxide-initiated polymerization, leading to the formation of polymers at low synthesis temperatures
synthesis
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utilization of recombinant enzyme expressed in the periplasm or on the cell surface of Escherichia coli as biocatalyst in a non-laborious and non-costly whole-cell application for reacting on towards different polyols such as xylitol and sorbitol
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synthesis
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AldO is an enantioselective biocatalyst for the kinetic resolution of racemic 1,2-diols
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additional information
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GOx bioactive paper is fabricated, which can potentially be used as food packaging paper
additional information
despite the broad range of applications for glucose oxidase, the effectiveness of glucose oxidase is restricted by the narrow substrate range of this enzyme and susceptibility to H2O2 inactivation