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Literature summary 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)

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.4 Aspergillus niger P13006
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.3.4 commercial preparation
-
 Aspergillus niger
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.3.4 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.4 beta-D-glucose + O2
-
 Aspergillus niger D-glucono-1,5-lactone + H2O2
-
 ?
1.1.3.4 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

EC Number Synonyms Comment Organism
1.1.3.4 GOX
-
 Aspergillus niger