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Literature summary for 1.1.3.4 extracted from

  • Cho, Y.K.; Bailey, J.E.
    Immobilization of enzymes on activated carbon: Properties of immobilized glucoamylase, glucose oxidase, and gluconolactone (1978), Biotechnol. Bioeng., 20, 1651-1665.
No PubMed abstract available

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.51 3.4 beta-D-glucose depending on O2-concentration, comparison of values with enzyme immobilized on various materials Aspergillus niger

Natural Substrates/ Products (Substrates)

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

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
-
?
beta-D-glucose + O2 + H2O native enzyme and enzyme immobilized on activated carbon Aspergillus niger D-glucono-1,5-lactone + H2O2
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
free enzyme Aspergillus niger
6.3
-
immobilized on activated carbon Aspergillus niger

pH Range

pH Minimum pH Maximum Comment Organism
2.5 9 immobilized on activated carbon Aspergillus niger
3.4 7.5 soluble enzyme Aspergillus niger