EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
   1.11.1.18 | -999 |
- |
heat stable enzyme |
675819 |
| 1.11.1.18 | -999 |
- |
the enzyme is extremely thermostable |
671929 |
| 1.11.1.18 | -999 |
- |
vanadate increases the thermostability. Ag+ and Al3+ lower the thermostability of the enzyme when compared with the control. Mn2+, Fe2+, Co2+, Ni2+, and Ba2+ have slightly positive effects, whereas Li+, Na+, K+, and Rb+ have no effect and Zn2+ lowers the thermostability |
674916 |
| 1.11.1.18 | 10 |
80 |
reaction activity in the presence of recombinant BPO-A1 peaks at 60°C whereas peak in the non-enzymatic activity of H2O2 is not observed in temperature range of 10-70°C. The increase in the activity of the enzyme with propanoic acid around 10-50°C is due to the peroxidation step because high activity in the nonenzymatic oxidative bromination step is maintained at low temperature, which suppresses the decomposition of the active species generated by the reaction between peracid and Br-. The active species is heat-labile. The significant decrease in activity around 65-70°C is attributed to decomposition of the active species. The native BPO-A1 possesses high stability up to 80°C. Recombinant BPO-A1 possesses high peroxidating activity at high temperatures |
764075 |
| 1.11.1.18 | 50 |
- |
activity remains constant for at least 4 h |
672433 |
| 1.11.1.18 | 57 |
- |
20 min, 50% loss of activity, enzyme preincubated without metal ion |
674916 |
| 1.11.1.18 | 60 |
- |
1 h, about 50% loss of activity |
676980 |
| 1.11.1.18 | 60 |
- |
50 min, complete inactivation, nonhaem-type bromoperoxidase BPO 1a |
675171 |
| 1.11.1.18 | 60 |
- |
50 min, no loss of activity, nonhaem-type bromoperoxidase BPO 1b |
675171 |
| 1.11.1.18 | 60 |
- |
50 min, no loss of activity, nonhaem-type bromoperoxidase BPO 3 |
675171 |
