EC Number   |
pH Stability |
pH Stability Maximum |
Reference |
|---|
   3.4.22.32 | 0.8 |
2 |
stem bromelain at pH 2.0 is maximally unfolded and characterized by significant loss of secondary structure (about 80%) and almost complete loss of tertiary contacts, at pH 0.8 a molten globule state is observed with secondary structure content similar to that of native protein but no tertiary structure |
680545 |
| 3.4.22.32 | 2 |
- |
almost complete loss of native tertiary contacts, acid unfolded state |
664339 |
| 3.4.22.32 | 3 |
9 |
4°C, 24 h, stable |
30285 |
| 3.4.22.32 | 3.2 |
7 |
stem bromelain solubilized at pH 7.0 and at pH 3.2 retains, after 16 h at 256°C, 10 and 40% of the initial activity, respectively |
731526 |
| 3.4.22.32 | 4 |
10 |
5°C, 24 h, stable |
30273 |
| 3.4.22.32 | 5 |
- |
50°C, 60 min, stable |
30285 |
| 3.4.22.32 | 5.5 |
10 |
stem bromelain is fully resistant against urea around neutral pH (5.5 to 10.0) and unfolds only below pH 5.0 |
707537 |
| 3.4.22.32 | 5.6 |
9 |
stable |
30297 |
| 3.4.22.32 | 7 |
10 |
from pH 7.0 to 10.0, the protein's secondary structure remains the same, although a slight loss of tertiary structure is observed. Above pH 10.0, there is a significant and irreversible loss of secondary and tertiary structure. At pH 10.0, SBM shows a significant increase in 8-anilino-1-naphthalene-sulfonate binding relative to the native state. No significant loss of activity is observed up to pH 10.0, beyond which there is an irreversible loss of activity |
707283 |
