EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
   3.1.1.74 | -999 |
- |
activity is reduced to less than 10% of the maximum activity by heating for 10 min at 99°C |
710267 |
| 3.1.1.74 | -999 |
- |
ANS binds strongly to native cutinase as a noncompetitive inhibitor with up to 5 ANS per cutinase molecule. The first ANS molecule stabilizes cutinase. The last 4 ANS molecules decrease Tm-value by up to 7°C |
678741 |
| 3.1.1.74 | -999 |
- |
first order rate constants in thermal inactivation, overview |
730129 |
| 3.1.1.74 | -999 |
- |
presence of hexanol and the low water content lead to the enzyme stabilization in the interior of the micelles, increasing its thermostability |
707009 |
| 3.1.1.74 | -999 |
- |
study of thermal unfolding of enzyme as a function of pH-value in different buffers. At pH-optimum of 8.5, enzyme also has high thermal stability |
665756 |
| 3.1.1.74 | -999 |
- |
the enzyme is unstable and functions poorly at high temperatures as well as at acidic pH conditions, differential scanning calorimetry thermograms of cutinase, overview |
713927 |
| 3.1.1.74 | -999 |
- |
thermal denaturation-induced unfolding of LC-cutinase is analyzed at pH 8.0 by circular dichroism spectroscopy, kinetics of transition of the thermal denaturation, overview. The disulfide bond formed by Cys275 and Cys292 contributes not only to the thermodynamic stability but also to the kinetic stability of LC-cutinase |
729249 |
| 3.1.1.74 | -999 |
- |
thermal stability of Humicola insolens cutinase in aqueous SDS. SDS stabilizes noticeably against irreversible aggregation |
681595 |
| 3.1.1.74 | -999 |
- |
trehalose delays thermal unfolding, thus increasing the temperature at the mid-point of unfolding by 7.2°C |
678748 |
| 3.1.1.74 | 4 |
25 |
purified recombinant enzyme, pH 4.5, completely stable at |
729077 |
