EC Number   |
General Stability |
Reference |
|---|
    1.14.18.1 | half-life depends on O2 pressure, 46 h under 21 kPa O2, 7.7 h under 100 kPa O2 |
636432 |
| 1.14.18.1 | highly resistant to SDS and proteinase K |
636340 |
| 1.14.18.1 | inactivation by freezing/thawing |
636352 |
| 1.14.18.1 | maximal stability in Tween 20, 0.25 mg/ml melanosomal lipids stabilize |
636428 |
| 1.14.18.1 | maximal stabilization in the presence of 0.6 mM sodium dodecylsulfate |
636367 |
| 1.14.18.1 | monophenolase and diphenolase activities of tyrosinase are relatively stable across a broad range of pH values with maximum stability at pH 5.0 and 4.0. |
686437 |
| 1.14.18.1 | PPOextracted from plum shows stability at high pressure, with enzyme activation at 500 MPa |
746341 |
| 1.14.18.1 | The stability of the enzyme is determined by measuring activity in the various buffers (0.1 M citrate/0.2 M phosphate for pH 3.5-5.0, 0.2 M phosphate for pH 5.5-7.5) every 3 days using catechol as substrate under optimum conditions (pH, temperature and ionic strength). |
688046 |
| 1.14.18.1 | trypsin causes no inactivation |
636407 |
| 1.14.18.1 | tyrosine hydroxylation activity is inactivated faster than catecholase activity |
636375 |
