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Literature summary extracted from
- Improvement in ligninolytic activity of Phanerochaete chrysosporium cultures by glucose oxidase (2016), Biochem. Eng. J., 105, 332-338 .
No PubMed abstract available
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 | - |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.1.3.4 | commercial preparation | - |
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 | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.3.4 | GOX | - |
Aspergillus niger |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.1.3.4 | 25 | - |
assay at | 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 | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.1.3.4 | 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 |
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Release 2023.1 (January 2023)
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