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Literature summary for 1.1.3.4 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
Search for more literature for 1.1.3.4

Protein Variants

Protein Variants Comment Organism
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]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 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
-
-

Oxidation Stability

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

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Aspergillus niger
-

Storage Stability

Storage Stability Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-D-glucose + O2
-
 Aspergillus niger D-glucono-1,5-lactone + H2O2
-
 ?
beta-D-glucose + O2 enzyme assay using the ABTS/horseradish peroxidase system 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
30
-
 assay at Aspergillus niger

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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
75
-
 purified recombinant free enzyme, loss of 50% activity Aspergillus niger
80
-
 purified recombinant immobilizedenzyme, loss of 50% activity Aspergillus niger

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Aspergillus niger