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Literature summary for 1.1.3.13 extracted from
- Increased activity of alcohol oxidase at high hydrostatic pressure (2021), Enzyme Microb. Technol., 145, 109751 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Komagataella phaffii | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| commercial preparation | - |
Komagataella phaffii | - |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
there are two fractions of AOx with different thermal stability. High hydrostatic pressure increases the activity of the heat labile (L) + resistant (R) combined fractions but not of the R fraction alone. The activity of the L + R fractions increases 2.4fold at 160 MPa and 30°C compared to the activity at 0.1 MPa. At higher temperatures, the increase in activity with pressure is greater due to the combined stabilization and activation effects. The reaction rate of the R fraction at 50 °C is 17.9 or 17.7 microM min-1 at 80 or 160 MPa, respectively, and is not significantly different from the activity of the L + R fractions under the same conditions (18.4 micro min-1) | Komagataella phaffii |
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Release 2023.1 (January 2023)
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