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Literature summary for 1.1.3.4 extracted from

  • Ansari, Z.; Karimi, A.; Ebrahimi, S.; Emami, E.
    Improvement in ligninolytic activity of Phanerochaete chrysosporium cultures by glucose oxidase (2016), Biochem. Eng. J., 105, 332-338 .
No PubMed abstract available
Search for more literature for 1.1.3.4

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
-
-

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at 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

General Information

General Information Comment Organism
physiological function glucose oxidase (GOx) addition induces the expression and enzymatic activity of manganese peroxidase (MnP) and lignin peroxidase (LiP) from Phanerochaete chrysosporium strain ATCC 24725 cultures. Daily supplementation with GOx-glucose as compared with control cultures causes a remarkable increase in stability of MnP productivity in fungi cultures. Neither H2O2 nor gluconic acid produced by GOx is responsible for improvement of peroxidase activity in nitrogen-limited cultures. GOx increases MnP and LiP activity in the presence of manganese ions Aspergillus niger