EC Number   |
General Stability |
Reference |
|---|
    1.11.1.7 | a 10% and 74% decrease in activity of native and deglycosylated peroxidase, respectively, is observed after 3 h incubation with trypsin |
660088 |
| 1.11.1.7 | active for several weeks in 1% SDS |
439737 |
| 1.11.1.7 | Ca2+-binding increases the protein conformational stability by raising the melting temperature from 67°C to 82°C |
673542 |
| 1.11.1.7 | cofactor modification(heminD1 in rHRP1 and heminD2 in rHRP2 instead of heme) increases the substrate affinity and catalytic efficiency both in aqueous buffer and some organic solvents, the catalytic efficiency for phenol oxidation is increased by about 55% for rHRP1 in aqueous buffer, and it is also increased by about 70% for rHRP1 in 10% (v/v) acetonitrile. |
696482 |
| 1.11.1.7 | elicitor treatment or mechanical damage causes insolubilization of peroxidase 1 into cell walls, the enzyme binds autocatalytically to lignin in presence of H2O2 |
439742 |
| 1.11.1.7 | immobilization of isoenzyme POX2 was achieved by covalent binding of the enzyme to an epoxy-Sepharose matrix. The immobilized enzyme shows great stability toward heat and storage when compared with soluble enzyme |
671393 |
| 1.11.1.7 | lyophilized peroxidase remains stable and active without any loss of activity for more than 2 years |
671394 |
| 1.11.1.7 | peroxidase activity measured toward o-dianisidine does not alter up to 4 M guanidine, in the case of 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid), 1 M guanidine causes 70% inactivation of the enzyme |
674137 |
| 1.11.1.7 | POD from both cultivars shows higher thermolability compared with PPO, losing more than 90% of relative activity after only 5 min of incubation at 70°C |
687246 |
| 1.11.1.7 | pressure stability of the wild-type enzyme and its active-site Thr213 and Thr214 mutants is investigated. The protein is reversibly inactivated by pressure. At 20°C and pH 6.5, the protein undergoes a reversible P450-to-P420 inactivation with a midpoint at 380 MPa and a reaction volume change of -28 ml/mol. The inactivation transition is retarded, and the absolute reaction volume is decreased by increasing temperature or by mutations that decrease the size of the active site cavity. High pressure affects the tryptophan fluorescence yield, which decreases by about 37% at 480 MPa. The effect is reversible and suggests considerable contraction of the protein. Aerobic decomposition of iron-aryl complexes of the CYP119 T213A mutant under increasing hydrostatic pressure results in variation of the N-arylprotoporphyrin-IX regioisomer (NB:NA:NC:ND) adduct pattern from 39:47:07:07 at 0.1 MPa to 23:36:14:27 at 400 MPa. Preincubation of the protein at 400 MPa followed by complex formation and decomposition give the same regioisomer distribution as untreated protein. |
725185 |
