EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
   1.1.3.4 | -999 |
- |
analysis of thermal inactivation kinetics of enzyme GOD |
743857 |
| 1.1.3.4 | -999 |
- |
comparison of stability of enzyme from different sources |
389815 |
| 1.1.3.4 | -999 |
- |
enzyme denaturing process at different temperatures, localization of breaking points, analysis by molecular dynamics simulations, overview. Identification of the transition state of protein folding/unfolding, overview |
743759 |
| 1.1.3.4 | -999 |
- |
glucose oxidase stabilization against thermal inactivation using high hydrostatic pressure and hydrophobic modification, method development, evaluation, and kinetics of thermal inactivation, detailed overview. Determination of the effect of temperature on the rate constant of inactivation of GOx at each of the selected pressures, and of the pressure effects on the rate constant of inactivation of GOx |
742144 |
| 1.1.3.4 | -999 |
- |
glucose stabilizes against heat inactivation |
389814 |
| 1.1.3.4 | -999 |
- |
inactivation of the free enzyme within 10 min. Microencapsulation improves the thermal stability of GOx at temperatures up to 60°C due to stabilization of its active conformation but reduces the thermal stability of laccase because of the increased coordination between poly(ethyleneimine) and copper atoms in the enzyme's active site, 70% remaining activity after 60 min |
726413 |
| 1.1.3.4 | -999 |
- |
native and carbohydrate-depleted enzyme, no decrease of activity after 100 freeze-thaw cycles |
389788 |
| 1.1.3.4 | -999 |
- |
the enzyme is very stable at cold temperatures |
389805 |
| 1.1.3.4 | -999 |
- |
the irreversible nature of thermal inactivation is caused by a change in the state of association of apoenzyme. The dissociation of FAD results in the loss of secondary and tertiary structure, leading the unfolding and nonspecific aggregation of the enzyme molecule because of hydrophobic interactions of side chains |
656139 |
| 1.1.3.4 | -999 |
- |
thermal denaturation of glucose oxidase is an irreversible transition to the compact denatured form with a defined oligomeric structure that is significantly different from the chemically denatured state of the enzyme, unfolded monomer |
656254 |
