EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
   3.2.1.B26 | 90 |
- |
half-life: 1.7 h |
724582 |
| 3.2.1.B26 | 90 |
- |
low concentrations of the detergent (up to 0.02%) induce slight changes in the enzyme secondary structure, whereas high concentrations cause the alpha-helix content to increase at high temperatures and prevent protein aggregation |
718769 |
| 3.2.1.B26 | 90 |
- |
low concentrations of the SDS (up to 0.02%) induce slight changes in the enzyme secondary structure, whereas high concentrations cause the alpha-helix content to increase at high temperatures and prevent protein aggregation |
718769 |
| 3.2.1.B26 | 90 |
- |
t1/2: 0.7 d |
724623 |
| 3.2.1.B26 | 92 |
- |
half-life: less than 3 min |
724212 |
| 3.2.1.B26 | 97 |
98 |
Tm-value for recombinant enzyme |
725356 |
| 3.2.1.B26 | 98 |
99 |
Tm-value for native enzyme |
725356 |
| 3.2.1.B26 | 100 |
- |
investigation of the activity and conformational dynamics above 100°C. The data indicate a strong correlation between enzyme activity and protein flexibility. In particular, the time-resolved fluorescence data point out that some regions of the protein structure are very sensitive to the temperature increases, gaining a high flexibility degree with temperature. On the other hand, it is also possible to identify local environments of the enzyme structure that still possess a relatively high rigidity at 125°C |
719097 |
