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Literature summary extracted from

  • Paz-Alfaro, K.J.; Ruiz-Granados, Y.G.; Uribe-Carvajal, S.; Sampedro, J.G.
    Trehalose-mediated thermal stabilization of glucose oxidase from Aspergillus niger (2009), J. Biotechnol., 141, 130-136.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.3.4 trehalose trehalose does not affect Vmax but instead decreases Km and as a result enzyme efficiency is increased Aspergillus niger

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.4 12.42
-
 beta-D-glucose in the presence of 0.6 M trehalose, at 25°C Aspergillus niger
1.1.3.4 18.76
-
 beta-D-glucose in the absence of trehalose, at 25°C Aspergillus niger

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.4 Sephacryl 200 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
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.3.4 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 Aspergillus niger

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.4 FAD
-
 Aspergillus niger