EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
   3.4.22.2 | -999 |
- |
temperature and guanidine hydrochloride induced unfolding transitions of papain at pH 2.0 are biphasic, implying independent and sequential unfolding of its two domains. The N-domain unfolds initially |
653776 |
| 3.4.22.2 | -999 |
- |
the enzyme is stable to heat in the oxidized, inactive form, activity is rapidly lost in presence of 2-mercaptopropionic acid, hippuric acid alters heat stability |
95693 |
| 3.4.22.2 | -999 |
- |
thermal denaturation studies show that the binding of Ca2+ and Mg2+ brings about change in the thermal stability of papain at various concentrations of these metal ions. No significant change in the alpha-helix and beta-sheet structure of the papain upon binding of these metal ions |
653289 |
| 3.4.22.2 | -999 |
- |
thermal unfolding of the prosegment, in acid medium the enzyme unfolds in a globule-like conformation, irreversible without intermediate states, overview |
667324 |
| 3.4.22.2 | 4 |
- |
residual activity after 30 storage: 0% free papain, 80% immobilized papain |
733073 |
| 3.4.22.2 | 22 |
- |
residual activity after 30 storage: 25% free papain, 80% immobilized papain |
733073 |
| 3.4.22.2 | 22 |
- |
room temperature, pH 8.7, 95% loss of activity after 8 days, then the preparation maintains constant activity over an 86-day period, papain included in porous glass |
95674 |
| 3.4.22.2 | 25 |
- |
pH 3.2, 30 min, 5% loss of activity |
752461 |
| 3.4.22.2 | 25 |
- |
pH 7.0, 1 h, 49.8% loss of activity |
95686 |
| 3.4.22.2 | 30 |
- |
residual activity: 70% free papain, 40% immobilized papain |
733073 |
