EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
   3.4.19.3 | 40 |
- |
pH 7.0, 30 min, about 30% loss of activity of wild-type enzyme, about 5% loss of activity of mutant enzyme S185C and mutant enzyme C68S/S185C |
650352 |
| 3.4.19.3 | 45 |
- |
stable for at least 1 h |
95299 |
| 3.4.19.3 | 47 |
- |
thermodynamics of heat denaturation of the monomeric enzyme form of mutant enzyme C142S/C188S at pH 2.3. The mechanism of refolding is a two-state process. The equilibrium establishes with a relaxation time of 5080 s at Tm = 46.5°C |
652880 |
| 3.4.19.3 | 50 |
- |
90 min, enzyme is completely stable in crude preparation |
653759 |
| 3.4.19.3 | 50 |
- |
pH 7.0, 30 min, about 95% loss of activity of wild-type enzyme, about 10% loss of activity of mutant enzyme S185C and mutant enzyme C68S/S185C |
650352 |
| 3.4.19.3 | 50 |
- |
pH 7.8, 15 min, stable |
95283 |
| 3.4.19.3 | 55 |
- |
partial inactivation |
95299 |
| 3.4.19.3 | 59 |
- |
peak temperature on the differential scanning calorimetry is 59.3°C, pH 2.15, cysteine-free mutant enzyme C142S/C188S |
667733 |
| 3.4.19.3 | 60 |
- |
2 min, total inactivation |
95299 |
| 3.4.19.3 | 60 |
- |
30 min, activity is almost completely lost |
653759 |
