EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
   3.4.21.64 | -999 |
- |
Ca2+ contributes to the overal stability of the surface regions and improves the thermal stability |
29501 |
| 3.4.21.64 | -999 |
- |
depletion of Ca2+ increases the rate of autolysis after about 48 h, it reduces the thermal stability |
29510 |
| 3.4.21.64 | 16.2 |
80 |
the denaturation temperature of proteinase K derivatized with praseodymium (Pr) ions is 16.2°C, which is 5.9°C higher than those of metal-free and Ca2+-bound proteinase K, respectively. Isothermal titration calorimetry (ITC) measurements demonstrate that Pr-ion binding to proteinase K shows endothermic peaks, whereas Ca2+-ion binding shows exothermic peaks, indicating that the binding mode of Pr ions is different from that of Ca2+ ions, even though the crystal structures of proteinase K with Pr and Ca2+ ions are identical. Hydrolytic activity of Pr-derivatized proteinase K shows that the hydrolytic activity is 46fold higher at 70°C using synthetic nitroanilide substrate and 9 and 76fold higher at 70°C and 80°C using fluorescein isothiocyanate-labeled casein, respectively, in comparison with the native proteinase K. Furthermore, based on the yield of chemoenzymatic peptide syntheses, the aminolysis activity of Pr-derivatized proteinase K is 3.5 and 9.5fold higher than that of the native proteinase K at 50°C and 60°C, respectively |
752347 |
| 3.4.21.64 | 37 |
- |
30 min, about 90% residual activity even in presence of 1% sodium dodecylsulfate |
668577 |
| 3.4.21.64 | 46 |
- |
15 min, 50% loss of activity of Ca2+-free enzyme |
29510 |
| 3.4.21.64 | 50 |
- |
30 min, 19% residual activity in presence of 1% sodium dodecylsulfate |
668577 |
| 3.4.21.64 | 50 |
- |
30 min, 90% residual activity even in presence of 1% sodium dodecylsulfate |
668577 |
| 3.4.21.64 | 60 |
- |
retains 83% activity after 2 h |
649326 |
| 3.4.21.64 | 65 |
- |
15 min, 50% loss of activity of Ca2+-saturated enzyme |
29510 |
| 3.4.21.64 | 66 |
- |
thermal unfolding is cooperative at pH 7.0 with transition midpoint of 66°C |
707588 |
