EC Number   |
General Stability |
Reference |
|---|
   3.4.21.1 | 1,8-bis(tributylammonium)octane dibromide provokes stabilization effects in a way similar to cetyltributytetrabutylammonium bromide, but at lower concentration |
755380 |
| 3.4.21.1 | alpha-chymotrypsin immobilized on mesoporous silica is stable for at least 1 week, i.e. 20 recycles per day, at room temperature, activity decreases gradually to 15% during next 10 days |
650704 |
| 3.4.21.1 | autolysis of alpha-chymotrypsin is impeded when the enzyme is adsorbed on silica particles |
753018 |
| 3.4.21.1 | Ca2+ stabilizes the enzyme near pH 7, at low pH the enzyme is more stable in absence of Ca2+ |
171864 |
| 3.4.21.1 | enzyme stability is analyzed in 0.05 M Tris-HCl buffer pH 8.20 in the presence or the absence of methylamine, urea or methylamine + urea mixture of various concentrations at 25°C for 4 h to attain complete equilibrium. Indication that methylamines suppress the aggregation of a thermal denatured protein and that methylamines have comparable effects on counteracting the temperature-perturbing actions on alpha-chymotrypsin. |
693843 |
| 3.4.21.1 | immobilization of the enzyme on selenium nanoparticles increases the stability |
752535 |
| 3.4.21.1 | in the presence of putrescine and spermidine a clear stabilizing effect against thermal unfolding is achieved |
680206 |
| 3.4.21.1 | lanthanide ions, e.g. terbium accelerates the inactivation process |
171878 |
| 3.4.21.1 | protects the enzyme from inactivation process, probably of autolytic nature |
171878 |
| 3.4.21.1 | stability of the enzyme is increased in the presence of spermine |
754197 |
