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Literature summary extracted from
- Increased susceptibility of beta-glucosidase from the hyperthermophile Pyrococcus furiosus to thermal inactivation at higher pressures (2009), FEBS J., 276, 109-117.
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 3.2.1.21 | enzyme is highly piezostable and thermostable, with increased enzyme inactivation at 25°C and pressures from 100 to 300 MPa. At a constant pressure of 400 MPa, no enzyme inactivation occurrs. Enzyme has an unfolding pressure of 800 MPa at 85°C. Two-step inactivation process due to pressure, which is most pronounced at low temperatures. An increase in pH from 5.5 to 6.5 has a stabilizing effect | Pyrococcus furiosus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.21 | Pyrococcus furiosus | Q51723 | - |
- |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.21 | 80 | - |
no thermal unfolding at 200 MPa and 400 MPa | Pyrococcus furiosus |
| 3.2.1.21 | 122 | - |
melting point at 50 MPa in Tris buffer, pH 7.5 | Pyrococcus furiosus |
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Release 2023.1 (January 2023)
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