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Literature summary extracted from

  • Balistreri, N.; Gaboriau, D.; Jolivalt, C.; Launay, F.
    Covalent immobilization of glucose oxidase on mesocellular silica foams Characterization and stability towards temperature and organic solvents (2016), J. Mol. Catal. B, 127, 26-33 .
No PubMed abstract available

Protein Variants

EC Number Protein Variants Comment Organism
1.1.3.4 additional information glucose oxidase is immobilized on mesoporous SBA-15 silica and two mesocellular foams (MCF) characterized by similar surface area and pore volumes but different pore/cell dimensions, covalent grafting of the enzyme through amide bonds, overview. The immobilized protein activity is significantly higher for the mesocellular foam with both cells and windows size larger than the enzyme dimensions. Enzyme GOx exhibits higher thermal stability when immobilized on the mesocellular foam compared to thefree enzyme Aspergillus niger

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.4 additional information
-
 additional information Michaelis-Menten kinetics of immobilized enzyme GOx and free enzyme GOx Aspergillus niger
1.1.3.4 28.8
-
 beta-D-glucose recombinant free enzyme, pH 6.0, 30°C Aspergillus niger
1.1.3.4 29.7
-
 beta-D-glucose recombinant immobilized enzyme, pH 6.0, 30°C Aspergillus niger

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.3.4 extracellular
-
 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
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.1.3.4 immobilized enzyme, 50°C, half of GOx activity is retained in 40% v/v MeOH/acetate buffer Aspergillus niger

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.3.4 commercial preparation
-
 Aspergillus niger
-

Storage Stability

EC Number Storage Stability Organism
1.1.3.4 50°C, purified recombinant immobilized GOx, up to 80% of initial activity is retained after 44 h 50°C, purified recombinant free GOx, loss of 90% of initial activity within 44 h, a further 120 h storage period at 9°C leads to partial denaturation and is not reversible 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
-
 ?
1.1.3.4 beta-D-glucose + O2 enzyme assay using the ABTS/horseradish peroxidase system 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 30
-
 assay at Aspergillus niger

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.3.4 30 50 purified recombinant free enzyme and immobilized enzyme, the enzyme activity remains rather unchanged from 30-45°C and then drops at higher temperatures. The thermal stability of immobilized GOx is only slightly higher than that of the free enzyme Aspergillus niger
1.1.3.4 75
-
 purified recombinant free enzyme, loss of 50% activity Aspergillus niger
1.1.3.4 80
-
 purified recombinant immobilizedenzyme, loss of 50% activity Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.3.4 6
-
 assay at Aspergillus niger

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.4 FAD
-
 Aspergillus niger