EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
   3.4.17.B1 | -999 |
- |
hydrophobic interactions between Leu7 and Leu376 increase protein thermostability |
695033 |
| 3.4.17.B1 | 0 |
25 |
instable at, glycerol stabilizes |
651034 |
| 3.4.17.B1 | 20 |
- |
stable for several days at room temperature in buffer containing 10 mM imidazole-HCl, 10 mM potassium acetate and 23 mM Tris-HCl, pH 7.2, in the presence of 2 mM 2-mercaptoethanol and 50% (v/v) glycerol |
721897 |
| 3.4.17.B1 | 25 |
- |
the enzyme gradually loses its activity resulting in a complete inactivation after 96 h. The nanobioconjugate of the enzyme immobilized on silica-coated magnetic nanoparticles leads to a substantial increase in stability, up to 85% of initial activity being retained after 96 h |
729491 |
| 3.4.17.B1 | 40 |
- |
in the presence of ethanol at 40°C and various concentrations the inactivation profiles shows that the enzyme has a residual activity of 50% after 6 h, which decreases to 20% after 24 h incubation. The nanobioconjugate of the enzyme immobilized on silica-coated magnetic nanoparticles reveales a significantly improved stability in ethanol at the different tested concentrations compared with free enzyme, up to 80-90% of residual activity after 6 h, and 70% after 24 h incubation in 80% ethanol being retained |
729491 |
| 3.4.17.B1 | 50 |
- |
after 1 h of incubation at 50°C and 1 MPa in the absence of substrate, the activity is decreased by 30%. This effect is abolished when the enzyme is incubated at 200 MPa. Activity loss at atmospheric pressure is about 7% in 10 min, the activity can be stabilized completely at 300 MPa |
721897 |
| 3.4.17.B1 | 50 |
- |
in the absence of glycerol and 2-mercaptoethanol, at 50°C, the enzyme undergoes a slow thermal inactivation upon dilution in an aqueous buffer at pH 6.5. This loss of activity can be inhibited when the enzyme is maintained at high pressure. At higher temperatures, higher pressures (up to 400 MPa) are required to maintain the enzyme in its active state |
721897 |
| 3.4.17.B1 | 70 |
- |
inactivation rate constants of both holo- and apo-enzyme is determined at 70°C over a broad pH range. At pH values below 5.7, the metal-depleted enzyme is substantially more stable than the native form, a probable consequence of a reduction in electrostatic repulsion. In contrast, at any pH value above 5.7 loss of Zn2+ severely impairs enzyme stability. Below pH 5 the apoenzyme is also significantly destabilized |
649646 |
| 3.4.17.B1 | 80 |
- |
first-order irreversible thermal inactivation of the metal-depleted enzyme shows an activation energy value of 205.6 kJ/mol, which is considerably lower than that of the holoenzyme (494.4 kJ/mol). The values of activation free energies, enthalpies and entropies also dropp with metal removal. Thermal inactivation of the apoenzyme is very quick at 80°C, whereas the holoenzyme is stable at the same temperature. The bivalent cation exhibits a major stabilizing role. Chaotropic salts strongly destabilize the holoenzyme, showing that hydrophobic interactions are involved in maintaining the native conformation of the enzyme. The inactivation rate is also increased by sodium sulfate, acetate and chloride, which are not chaotropes, indicating that one or more salt bridges concur in stabilizing the active enzyme |
649646 |
| 3.4.17.B1 | 80 |
- |
holoenzyme is stable at 80°C, while the apoenzyme is rapidly inactivated |
649646 |
