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Literature summary for 1.1.3.4 extracted from
- Recombinant glucose oxidase from Penicillium amagasakiense for efficient bioelectrochemical applications in physiological conditions (2011), J. Biotechnol., 151, 122-129.
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | GOX is the most widely used enzyme for the development of electrochemical glucose biosensors and biofuel cell in physiological conditions | Aspergillus niger |
| biotechnology | GOX is the most widely used enzyme for the development of electrochemical glucose biosensors and biofuel cell in physiological conditions | Penicillium amagasakiense |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Pichia pastoris strain GS115 | Aspergillus niger |
| expressed in Pichia pastoris strain GS115 | Penicillium amagasakiense |
General Stability
| General Stability | Organism |
|---|---|
| the enzyme stability is not influenced by physiological concentration of sodium chloride (140 mM) | Aspergillus niger |
| the enzyme stability is not influenced by physiological concentration of sodium chloride (140 mM) | Penicillium amagasakiense |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| oxygen | - |
Aspergillus niger |  |
| oxygen | - |
Penicillium amagasakiense | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0638 | - |
ferrocinium-methanol | recombinant enzyme yGOXpenag, pH 6.0, 50°C | Penicillium amagasakiense | |
| 0.1107 | - |
ferrocinium-methanol | native enzyme, pH 6.5, 70°C | Aspergillus niger | |
| 11.7 | - |
beta-D-glucose | recombinant enzyme yGOXpenag, using O2 as cosubstrate, pH 6.0, 50°C | Penicillium amagasakiense | |
| 18.2 | - |
beta-D-glucose | recombinant enzyme yGOXpenag, using ferrocinium-methanol as cosubstrate, pH 6.0, 50°C | Penicillium amagasakiense | |
| 50.3 | - |
beta-D-glucose | native enzyme, using O2 as cosubstrate, pH 6.5, 70°C | Aspergillus niger | |
| 71.2 | - |
beta-D-glucose | native enzyme, using ferrocinium-methanol as cosubstrate, pH 6.5, 70°C | Aspergillus niger | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 72000 | - |
2 * 72000, recombinant enzyme, SDS-PAGE | Penicillium amagasakiense |
| 77000 | - |
2 * 77000, native enzyme, SDS-PAGE | Aspergillus niger |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus niger | - |
- |
- |
| Penicillium amagasakiense | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | - |
Aspergillus niger |
| glycoprotein | - |
Penicillium amagasakiense |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| phenyl Sepharose column chromatography and Q Sepharose column chromatography | Penicillium amagasakiense |
| phenyl Sepharose column chromatography, Q Sepharose column chromatography, gel filtration | Aspergillus niger |
Storage Stability
| Storage Stability | Organism |
|---|---|
| 4°C, purified recombinant enzyme in 100 mM sodium phosphate, pH 5.1, several months, no loss of activity | Aspergillus niger |
| 4°C, purified recombinant enzyme in 100 mM sodium phosphate, pH 5.1, several months, no loss of activity | Penicillium amagasakiense |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-D-glucose + ferrocinium-methanol | - |
Aspergillus niger | ? | - |
? | |
| beta-D-glucose + ferrocinium-methanol | - |
Penicillium amagasakiense | ? | - |
? | |
| beta-D-glucose + O2 + H2O | - |
Aspergillus niger | D-glucono-1,5-lactone + H2O2 | - |
? | |
| beta-D-glucose + O2 + H2O | - |
Penicillium amagasakiense | D-glucono-1,5-lactone + H2O2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 72000, recombinant enzyme, SDS-PAGE | Penicillium amagasakiense |
| homodimer | 2 * 77000, native enzyme, SDS-PAGE | Aspergillus niger |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| beta-D-glucose:oxygen 1-oxidoreductase | - |
Aspergillus niger |
| beta-D-glucose:oxygen 1-oxidoreductase | - |
Penicillium amagasakiense |
| GOX | - |
Aspergillus niger |
| GOX | - |
Penicillium amagasakiense |
| yGOXpenag | recombinant enzyme | Penicillium amagasakiense |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
recombinant enzyme | Penicillium amagasakiense |
| 70 | - |
- |
Aspergillus niger |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
at 37°C and in pH 7.5 buffer, the half life of the native enzyme is 48 h | Aspergillus niger |
| 37 | - |
at 37°C and in pH 7.5 buffer, the half life of the recombinant enzyme yGOXpenag is 6 h | Penicillium amagasakiense |
| 50 | - |
at pH 6.0 and at 50°C, the half life of the enzyme is about 20 h, thermal denaturation is observed above 50°C | Penicillium amagasakiense |
| 50 | 60 | at pH 6.0 and at 50°C, the half life of the enzyme is about 20 h, thermal denaturation is observed above 60°C | Aspergillus niger |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1695 | - |
beta-D-glucose | recombinant enzyme yGOXpenag, using ferrocinium-methanol as cosubstrate, pH 6.0, 50°C | Penicillium amagasakiense | |
| 1808 | - |
beta-D-glucose | recombinant enzyme yGOXpenag, using O2 as cosubstrate, pH 6.0, 50°C | Penicillium amagasakiense | |
| 1890 | - |
beta-D-glucose | native enzyme, using O2 as cosubstrate, pH 6.5, 70°C | Aspergillus niger | |
| 1938 | - |
beta-D-glucose | native enzyme, using ferrocinium-methanol as cosubstrate, pH 6.5, 70°C | Aspergillus niger | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
under O2 and Ar at 37°C, recombinant enzyme yGOXpenag | Penicillium amagasakiense |
| 6.5 | - |
native enzyme | Aspergillus niger |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 7.5 | under O2 and Ar at 37°C, recombinant enzyme yGOXpenag | Penicillium amagasakiense |
| 5.5 | 9 | 80% of the maximal activity is observed in the pH 5.5-9.0 range | Aspergillus niger |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
at pH 6.0 and at 50°C, the half life of the enzyme is about 20 h | Aspergillus niger |
| 6 | - |
at pH 6.0 and at 50°C, the half life of the enzyme is about 20 h | Penicillium amagasakiense |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Aspergillus niger | |
| FAD | - |
Penicillium amagasakiense | |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.017 | - |
ferrocinium-methanol | native enzyme, pH 6.5, 70°C | Aspergillus niger | |
| 0.027 | - |
ferrocinium-methanol | recombinant enzyme yGOXpenag, pH 6.0, 50°C | Penicillium amagasakiense | |
| 27 | - |
beta-D-glucose | native enzyme, using ferrocinium-methanol as cosubstrate, pH 6.5, 70°C | Aspergillus niger | |
| 38 | - |
beta-D-glucose | native enzyme, using O2 as cosubstrate, pH 6.5, 70°C | Aspergillus niger | |
| 93 | - |
beta-D-glucose | recombinant enzyme yGOXpenag, using ferrocinium-methanol as cosubstrate, pH 6.0, 50°C | Penicillium amagasakiense | |
| 155 | - |
beta-D-glucose | recombinant enzyme yGOXpenag, using O2 as cosubstrate, pH 6.0, 50°C | Penicillium amagasakiense | |
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