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Literature summary for 1.1.3.4 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

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Sephacryl 200 gel filtration Aspergillus niger

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-D-glucose + O2 + H2O
-
Aspergillus niger D-glucono-1,5-lactone + H2O2
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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

Cofactor Comment Organism Structure
FAD
-
Aspergillus niger