EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
   4.1.2.10 | -999 |
- |
the hydroxynitrile lyase from leaves and that expressed in Pichia pastoris show much better thermostability, pH stability, and organic solvent tolerance than the deglycosylated enzyme expressed in Escherichia coli and the deglycosylated mutant N105Q expressed in Pichia pastoris |
747548 |
| 4.1.2.10 | 0 |
- |
pH 5.0, wild-type, half-life 18 min, surface-modified mutant, half-life 137 min |
727311 |
| 4.1.2.10 | 0 |
20 |
stable |
704762 |
| 4.1.2.10 | 4 |
- |
the enzyme does not show any significant loss of activity at 4°C, hence it has good potential for industrial application |
747465 |
| 4.1.2.10 | 5 |
20 |
free and immobilized enzyme preparations show optimal carboligation activity at 5°C. As the temperature is increased from 5 to 20°C, the yields decrease, however enantiomeric excess values (99%) unchange |
715946 |
| 4.1.2.10 | 10 |
- |
half-life time: more than 96 h |
704762 |
| 4.1.2.10 | 10 |
- |
pH 5.0, wild-type, half-life 23.6 min, surface-modified mutant, half-life 136 min |
727311 |
| 4.1.2.10 | 15 |
40 |
1 h, no loss of activity |
749169 |
| 4.1.2.10 | 20 |
- |
half-life time: 80 h |
704762 |
| 4.1.2.10 | 20 |
- |
pH 5.0, wild-type, half-life 9.6 min, surface-modified mutant, half-life 134 min |
727311 |
