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Literature summary extracted from

  • Altikatoglu, M.; Basaran, Y.; Arioz, C.; Ogan, A.; Kuzu, H.
    Glucose oxidase-dextran conjugates with enhanced stabilities against temperature and pH (2010), Appl. Biochem. Biotechnol., 160, 2187-2197.
    View publication on PubMed

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.4 Sephadex G-50 gel filtration 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 + H2O
-
Aspergillus niger D-glucono-1,5-lactone + H2O2
-
?

Synonyms

EC Number Synonyms Comment Organism
1.1.3.4 GOD
-
Aspergillus niger

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.3.4 30
-
-
Aspergillus niger

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.3.4 80
-
the pure enzyme is inactive at 80°C, thermal resistance is high only at pH 7.0 Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.3.4 4 5
-
Aspergillus niger

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.4 FAD each subunit of dimeric GOD contains one tightly bound FAD as cofactor Aspergillus niger