EC Number   |
General Stability |
Reference |
|---|
    3.1.1.1 | 0.1% Triton X-100 exhibits a significant stabilizing effect without leading to a change in activity levels |
726707 |
| 3.1.1.1 | 10% glycerol, increases stability |
171017 |
| 3.1.1.1 | 2 mM dithiothreitol stabilizes |
668446 |
| 3.1.1.1 | 50% loss of activity upon lyophilization |
171002 |
| 3.1.1.1 | dialysis using nitrocellulose membranes causes a significant loss of activity |
170979 |
| 3.1.1.1 | esterase activity diminishes to 50% upon disruption of the protein's disulfide bridges and disappears completely when digested by proteases |
692120 |
| 3.1.1.1 | in absence of 2-mercaptoethanol, purified enzymes are rapidly inactivated at 25°C |
669146 |
| 3.1.1.1 | influence of NaCl on the stability of the enzyme is highly temperature dependent. At 22°C, the enzyme retains its highest activity when incubated at the high salt concentration of 3.4 M NaCl for over 100 hours. In contrast, the enzyme steadily loses its activity without salt, with most of its activity being lost within 50 h. As the incubation temperature is raised to 37°C, the activities under both solution conditions show a clear sign of decline, although the presence of 3.4 M NaCl sustains the activity more effectively. When the incubation temperature reaches 55°C, the rates of activity loss are significantly increased with and without the addition of 3.4 M NaCl. With further increase in temperature to 60°C the trend of acceleration of activity loss continues and salt addition again accelerates the rate of denaturation, confirming that whilst salt addition helps stabilize the enzyme below 50°C, the opposite effect is produced above it |
728547 |
| 3.1.1.1 | resistant to complete denaturation by 8 M urea |
170997 |
| 3.1.1.1 | stable |
652416, 655643 |
