EC Number |
General Stability |
Reference |
---|
3.4.21.4 | 0.5 mM CaCl2 stabilizes the activity, especially at acidic pH-values |
667239 |
3.4.21.4 | a fibronectin type III-like peptide from aqueous extract of human placenta, used as a licensed drug for wound healing, tightly complexes the enzyme and protects it against autodigestion. Trypsin retains 40% of activity at constant level between 20 and 26 days in presence of the extract against complete inactivation in its absence. The peptide-trypsin complex is dissociated in presence of high concentration of substrates |
717901 |
3.4.21.4 | aggregated trypsin-containing nanofibers demonstrate excellent enzymatic activity (300 times higher than monolayered nanofibers), long-term stability (i.e. negligible loss of activity over 1 year), and a high resistance to proteolysis by other proteases (such as alpha-chymotrypsin) |
701142 |
3.4.21.4 | autolysis is a contributing factor in the stability of trypsin I |
708223 |
3.4.21.4 | benzamidine minimizes the autolysis of trypsin |
701262 |
3.4.21.4 | Ca2+ stabilizes |
708552, 95427 |
3.4.21.4 | Ca2+ stabilizes the enzyme |
708529 |
3.4.21.4 | Ca2+ stabilizes the purified enzyme |
708835 |
3.4.21.4 | decreasing dielectric constant results from the stabilization of electrostatic energy for the formation of an oxyanion hole, and this stabilization is caused by the increase of electrostricted water around the charged tetrahedral transition state. The control of the solvent dielectric constant can stabilize the tetrahedral transition state, and this lowers the activation energy |
650362 |
3.4.21.4 | denaturation in neutral solution: denaturation of alpha-trypsin is a strict second-order reaction, denaturation of beta-trypsin is not a pure second-order reaction at the same pH. Ca2+ retards the rate of beta-trypsin denaturation to a greater extent than that of alpha-trypsin. Denaturation of immobilized trypsin in alkaline solution is a first-order reaction, Ca2+ does not affect the rate of trypsin denaturation in alkaline solution |
95464 |