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Literature summary extracted from

  • Halalipour, A.; Duff, M.R.; Howell, E.E.; Reyes-De-Corcuera, J.I.
    Glucose oxidase stabilization against thermal inactivation using high hydrostatic pressure and hydrophobic modification (2017), Biotechnol. Bioeng., 114, 516-525 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.1.3.4 additional information glucose oxidase is chemically modified to increase the stability of GOx using N-(3-dimethylaminopropyl)-N'-ethylcarbodiimide hydrochloride and sodium benzoate or aniline. The modification forms an amide bond between benzoate and lysines or aniline with glutamate and aspartate residues. The labeling of primary amines (lysines and the N-terminus) by benzoate is measured through a trinitrobenzene sulfonic acid (TNBS) assay Aspergillus niger

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.4 17.5
-
 beta-D-glucose pH 5.1, 37°C, unmodified enzyme Aspergillus niger
1.1.3.4 23.2
-
 beta-D-glucose pH 5.1, 37°C, aniline-modified enzyme Aspergillus niger
1.1.3.4 32.4
-
 beta-D-glucose pH 5.1, 37°C, benzoate-modified enzyme Aspergillus niger

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
-

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
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.3.4 GOX
-
 Aspergillus niger
1.1.3.4 More type X-S enzyme Aspergillus niger

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.3.4 35 37 assay at Aspergillus niger

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.3.4 additional information
-
 glucose oxidase stabilization against thermal inactivation using high hydrostatic pressure and hydrophobic modification, method development, evaluation, and kinetics of thermal inactivation, detailed overview. Determination of the effect of temperature on the rate constant of inactivation of GOx at each of the selected pressures, and of the pressure effects on the rate constant of inactivation of GOx Aspergillus niger

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.3.4 434
-
 beta-D-glucose pH 5.1, 37°C, benzoate-modified enzyme Aspergillus niger
1.1.3.4 446
-
 beta-D-glucose pH 5.1, 37°C, unmodified enzyme and aniline-modified enzyme Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.3.4 5.1
-
 assay at Aspergillus niger

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.4 FAD
-
 Aspergillus niger