EC Number   |
pH Stability |
pH Stability Maximum |
Reference |
|---|
  1.1.1.431 | -999 |
- |
alteration in both secondary and tertiary structures cause enzyme deactivation in acidic pH, while increased deactivation rates at alkaline pH are attributed to the variation of tertiary structure over time. The secondary structure of enzyme DnXR is completely affected at pH 5.0 and is retained at pH 5.5 with altered signature. Negative ellipticity values are reduced at pH 6.0 and 10.0 without alteration in secondary signatures. Overlapping spectra are obtained at pH 7.0, pH 8.0, and pH 9.0 with the highest signals. Effect of pH on thermodynamic parameters, overview |
761017 |
| 1.1.1.431 | 3.5 |
- |
purified recombinant wild-type and engineered enzymes have a half-life of 1.2 h |
761007 |
| 1.1.1.431 | 5 |
- |
purified recombinant wild-type enzyme has a half-life of 10 h, engineered enzyme Pir-XR of 30 h, and engineered enzyme XR-GPI of 30 h |
761007 |
| 1.1.1.431 | 5 |
9 |
the purified recombinant enzyme exhibits remarkable stability at pH 6 and pH 7. It retains 58.7%, 73.76%, and 45.95% activity after 30 min at pH 5.0, pH 8.0, and pH 9.0, respectively. The activity at pH 5.0 and pH 8.0 declines to 27% and 54%, respectively, after an incubation of 60 min |
760720 |
| 1.1.1.431 | 6 |
- |
purified recombinant wild-type enzyme has a half-life of 5 h, engineered enzyme Pir-XR of 20 h, and engineered enzyme XR-GPI of 20 h |
761007 |
| 1.1.1.431 | 7 |
- |
purified recombinant wild-type enzyme has a half-life of 4 h, engineered enzyme Pir-XR of 7.5 h, and engineered enzyme XR-GPI of 12.5 h |
761007 |
| 1.1.1.431 | 7 |
- |
the purified recombinant enzyme is catalytically and structurally stable at pH 7.0 with half-life of 250 min |
761017 |
