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Literature summary for 1.1.3.4 extracted from

  • Seehuber, A.; Dahint, R.
    Conformation and activity of glucose oxidase on homogeneously coated and nanostructured surfaces (2013), J. Phys. Chem. B, 117, 6980-6989.
    View publication on PubMed

Application

Application Comment Organism
analysis the enzyme is useful as biosensor for glucose detection Aspergillus niger

Protein Variants

Protein Variants Comment Organism
additional information enzyme adsorption on different particles with homogeneous or nanostructured surfaces and coated with different compounds, i.e. 11-amino-1-undecanethiol, 12-mercaptododecanoic acid, 1-dodecanethiol, and 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol), only 9% of the activity of the native protein is preserved on 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol), but the substrate affinity of the adsorbed GOx is best on 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol) where its catalytic activity is worst, secondary structure of thhe enzyme is altered compared to enzyme in solution, overview Aspergillus niger

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics Aspergillus niger
0.019
-
beta-D-glucose native enzyme in solution, pH 5.5, temperature not specified in the publication Aspergillus niger
8
-
beta-D-glucose enzyme adsorbed on 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol) coated matrix, high enzyme concentration, pH 5.5, temperature not specified in the publication Aspergillus niger
12
-
beta-D-glucose enzyme adsorbed on 11-amino-1-undecanethiol coated matrix, pH 5.5, temperature not specified in the publication Aspergillus niger
22
-
beta-D-glucose enzyme adsorbed on 11-(1H-pyrol-11-(1H-pyrol-1-yl)undecane-1-thiol) coated matrix, low enzyme concentration, pH 5.5, temperature not specified in the publication Aspergillus niger

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
Aspergillus niger
-
-

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
-
-

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
100
-
immobilized enzyme, pH 5.5, temperature not specified in the publication, high enzyme concentration Aspergillus niger
216
-
immobilized enzyme, pH 5.5, temperature not specified in the publication, low enzyme concentration 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
-
?

Synonyms

Synonyms Comment Organism
GOX
-
Aspergillus niger

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
assay at Aspergillus niger