EC Number   |
General Stability |
Reference |
|---|
    3.1.1.3 | 2 mM ammonium sulfate, bovine serum albumin at 2 mg/ml, or 40% v/v glycerol stabilize the cold-labile purified enzyme |
677702 |
| 3.1.1.3 | Ca2+ ions stabilize the tertiary structure of the enzyme |
650618 |
| 3.1.1.3 | Ca2+ is important for structural stability of the enzyme |
666821 |
| 3.1.1.3 | Ca2+ stabilizes the enzyme |
651022 |
| 3.1.1.3 | Ca2+ stabilizes the enzyme at concentration of 1-10 mM with decreasing effect at higher concentration, 100% activity at 1 mM, 4% activity at 10 mM |
653692 |
| 3.1.1.3 | Ca2+ stabilizes the enzyme, no loss of activity after 30 h at 30°C in presence of Ca2+, 70% loss after 30 h at 30°C of activity in absence of Ca2+ |
651141 |
| 3.1.1.3 | colipase and bile salts stabilize the enzyme against inactivation at its water/substrate interface: colipase and bile salts above their critical micellar concentration offer better protection than either of them alone |
80814 |
| 3.1.1.3 | denaturation of the pure SDL at the tributyrin/water interface due to the high interfacial energy |
679311 |
| 3.1.1.3 | following immobilization by covalent attachment on hydrous niobium oxide, the enzyme exhibits improved storage stability and performs better at higher incubation temperatures. In addition, the enzyme retains most of its catalytic efficiency after successive operational cycles. For the esterification reaction of butanol with butyric acid (24 h, 37°C), a slow decrease in the esterification activity is verified (25%) after ten recycles (240 h), which corresponds to a half-life of 406 h |
714870 |
| 3.1.1.3 | half-life of the enzyme is enhanced by glycine, sorbitol, glycerol, glucose, and ammonium chloride |
653693 |
