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Literature summary for 1.1.3.4 extracted from

  • He, C.; Liu, J.; Xie, L.; Zhang, Q.; Li, C.; Gui, D.; Zhang, G.; Wu, C.
    Activity and thermal stability improvements of glucose oxidase upon adsorption on core-shell PMMA-BSA nanoparticles (2009), Langmuir, 25, 13456-13460.
    View publication on PubMed
Search for more literature for 1.1.3.4

General Stability

General Stability Organism
the poly(methyl methacrylate)-bovine serum albumin particle-adsorbed GOx can retain at least 80% of the free enzyme activity Aspergillus niger

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-D-glucose + O2 + H2O
-
 Aspergillus niger D-glucono-1,5-lactone + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
GOX
-
 Aspergillus niger

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 the poly(methyl methacrylate)-bovine serum albumin particle-adsorbed GOx only loses 28% of its activity in comparison with a 64% activity loss of free GOx when it is incubated at 50°C for 35 h Aspergillus niger

pH Stability

pH Stability pH Stability Maximum Comment Organism
4.5 7.4 the poly(methyl methacrylate)-bovine serum albumin particle-adsorbed GOx has a higher catalytic activity at pH 7.4, close to the physiological environment, in comparison with that at pH 4.5 Aspergillus niger