EC Number   |
General Stability |
Reference |
|---|
    1.11.1.11 | dialysis of crude enzyme preparations for 24 h against a buffer depleted of ascorbate or sorbitol results in 90% and 20% loss in enzyme activity, respectively. In air saturated solutions, salting-out results in a significant loss in enzyme activity, therefore exchange to N2 gas is performed prior to salting-out of the root enzyme |
439868 |
| 1.11.1.11 | enzyme retains 35% activity after chymotrypsin digestion at pH 8 and 37°C for 40 min |
724680 |
| 1.11.1.11 | loss of activity after incubation of crude extracts from pea shoots with either pronase or chymotrypsin |
439856 |
| 1.11.1.11 | the enzyme is completely inactivated within 30 s in ascorbate-depleted medium under anaerobic conditions |
439875 |
| 1.11.1.11 | the enzyme is relatively stable in ascorbate-depleted medium |
439874 |
| 1.11.1.11 | the enzyme is very unstable in the absence of ascorbate and looses its activity within min particularly in the case of chloroplastic and mitochondrial isoforms |
699802 |
| 1.11.1.11 | the half-inactivation time is estimated to be 15 min, when the enzyme is diluted with ascorbate-depleted medium |
439871 |
| 1.11.1.11 | the recombinant enzyme-B remains active for at least 180 min after depletion of ascorbate |
439881 |
| 1.11.1.11 | when the enzyme is diluted with the ascorbate-deleted medium, the half inactivation time is approximately 15 min |
713299 |
