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Literature summary for 1.1.3.4 extracted from

  • Burchardt, M.; Wittstock, G.
    Kinetic studies of glucose oxidase in polyelectrolyte multilayer films by means of scanning electrochemical microscopy (SECM) (2008), Bioelectrochemistry, 72, 66-76.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
beta-D-glucose + O2 Aspergillus niger
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D-glucono-1,5-lactone + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Aspergillus niger P13006
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
Aspergillus niger
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
kinetic investigations using Scanning electrochemical microscopy, influence of glucose concentration and of layer number, covering layers and time dependence, kinetic information as a function of layer number, film termination, inert covering layers and enzyme substrate concentration after fitting to numerical models shown, enzymatic conversion by electrochemical measurements at Scanning electrochemical microscopy feedback experiments Aspergillus niger

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-D-glucose + O2
-
Aspergillus niger D-glucono-1,5-lactone + H2O2
-
?
beta-D-glucose + O2 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 Aspergillus niger D-glucono-1,5-lactone + H2O2
-
?

Synonyms

Synonyms Comment Organism
GOX
-
Aspergillus niger