Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.3.4 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
Search for more literature for 1.1.3.4

Protein Variants

Protein Variants Comment Organism
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
17.5
-
 beta-D-glucose pH 5.1, 37°C, unmodified enzyme Aspergillus niger
23.2
-
 beta-D-glucose pH 5.1, 37°C, aniline-modified enzyme Aspergillus niger
32.4
-
 beta-D-glucose pH 5.1, 37°C, benzoate-modified enzyme 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 P13006
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 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
More type X-S enzyme Aspergillus niger

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Aspergillus niger