1.1.3.10: pyranose oxidase
This is an abbreviated version!
For detailed information about pyranose oxidase, go to the full flat file.
Word Map on EC 1.1.3.10
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1.1.3.10
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trametes
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multicolor
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1,4-benzoquinone
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chrysosporium
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phanerochaete
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white-rot
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nivale
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microdochium
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l-sorbose
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aldopyranoses
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synthesis
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1,5-anhydro-d-glucitol
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flavinylated
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ligninolytic
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ochracea
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glucose-methanol-choline
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1,5-anhydroglucitol
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peniophora
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c4a-hydroperoxyflavin
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biotechnology
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food industry
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energy production
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biofuel production
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analysis
- 1.1.3.10
- trametes
- multicolor
- 1,4-benzoquinone
- chrysosporium
- phanerochaete
-
white-rot
- nivale
-
microdochium
- l-sorbose
- aldopyranoses
- synthesis
- 1,5-anhydro-d-glucitol
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flavinylated
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ligninolytic
- ochracea
-
glucose-methanol-choline
- 1,5-anhydroglucitol
- peniophora
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c4a-hydroperoxyflavin
- biotechnology
- food industry
- energy production
- biofuel production
- analysis
Reaction
Synonyms
C-2 specific pyranose-2-oxidase, carbohydrate oxidase, glucose 2-oxidase, glucose-2-oxidase, P2O, P2Ox, POX, PROD, PyOx, pyranose 2-Oxidase, pyranose oxidase, pyranose-2-oxidase, pyranose/oxygen 2-oxidoreductase, pyranose: oxygen 2-oxidoreductase, pyranose:oxygen 2-oxidoreductase, pyranose:oxygen-2-oxidoreductase, TmP2Ox
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Application
Application on EC 1.1.3.10 - pyranose oxidase
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analysis
Coriolus sp.
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immobilization of enzyme on carbon nanotubes for application as enzymatic electrodes for enzyme-based biosensors and biofuel cells. The sensitivities of the covalent attachment, enzyme coating, and enzyme precipitate coating electrodes without 4-benzoquinone are 0.27, 0.76 and 3.7 mA/M/cm2, while covalent attachment, enzyme coating and enzyme precipitate coating electrodes in presence of 4-benzoquinone show 25, 25, and 60mA/M/cm2 of sensitivities, respectively. The maximum power densities of biofuel cells using covalent attachment, enzyme coating and enzyme precipitate coating electrodes without 4-benzoquinone are 41, 47 and 53 microW/cm2, while covalent attachment, enzyme coating and enzyme precipitate coating electrodes with 4-benzoquinone show 260, 330 and 500 microW/cm2, respectively
biofuel production
Coriolus sp.
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pyranose oxidase immobilized on carbon nanotubes via covalent attachment, enzyme coating, and enzyme precipitate coating is used to fabricate enzymatic electrodes for enzyme-based biosensors and biofuel cells
biotechnology
energy production
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enzyme P2O has the potential to be useful for biofuel cell applications
synthesis
biotechnology
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studies on stabilization of enzymatic activity by immobilization
biotechnology
biocatalyst for carbohydrate transformations toward higher-value products
biotechnology
P2Ox is a biocatalyst with high potential for biotransformations of carbohydrates and in synthetic carbohydrate chemistry. P2Ox is useful as bioelement in biofuel cells, replacing glucose oxidase
biotechnology
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enzyme P2O is a useful biocatalyst in several biotechnological applications, including biotransformation of carbohydrates such as D-glucose and D-galactose to generate 2-oxo-sugars that can be further reduced at the C1 position to yield D-fructose and D-tagatose, respectively
Phanerochaete gigantea
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oxidation of 2-keto-aldoses, formation of the methyl pentulose 1-deoxy-D-xylulose, whose phosphorylated form is the precursor of the vitamins thiamine and pyridoxol
synthesis
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the enzyme produces the beta-pyrone antibiotic cortalcerone from D-glucose
synthesis
Polyporus obtusus
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the enzyme produces the beta-pyrone antibiotic cortalcerone from D-glucose
synthesis
Corticium caeruleum
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the enzyme produces the beta-pyrone antibiotic cortalcerone from D-glucose
synthesis
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hydrogenation of 2-keto-aldoses, preparation of D-tagatose, which is used as a building block for the synthesis of bioactive amino sugars and as low-calory sweetener
synthesis
application of the engineered enzyme K312E in bioconversion of L-sorbose to 5-keto-D-fructose
synthesis
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enzyme P2O is a useful biocatalyst in several biotechnological applications, including biotransformation of carbohydrates such as D-glucose and D-galactose to generate 2-oxo-sugars that can be further reduced at the C1 position to yield D-fructose and D-tagatose, respectively
synthesis
immobilization of enzyme to a glass-beaded support with activity yields of 10%-23.3%. after 4,800 measurement cycles carried out over 5 days, 58-62% of activity remains
synthesis
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immobilization of enzyme to a glass-beaded support with activity yields of 10%-23.3%. after 4,800 measurement cycles carried out over 5 days, 58-62% of activity remains
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