Abstract
The inactivation kinetics of o-diphenoloxidase isolated from potato tubers was studied in the process of pyrocatechol oxidation. The enzyme when saturated with the substrate is inactivated with the inactivation rate constant kin = 0.5-1.0 min-1; kin depends on the initial concentration of pyrocatechol. The ultimate yield of the enzymic reaction product increases linearly with the initial concentration of the enzyme. Introduction of ethylene-diaminosulphate, a substance which condenses with o-quinones, does not increase the operation stability of o-diphenoloxidase. The data obtained evidence for inactivation of o-diphenoloxidase either at the level of the enzyme-substrate complex or due to bimolecular reaction with the substrate.
| Translated title of the contribution | Inactivation of o-diphenoloxidase in the pyrocatechol oxidation reaction |
|---|---|
| Original language | Russian |
| Pages (from-to) | 527-532 |
| Number of pages | 6 |
| Journal | Ukrainskii biokhimicheskii zhurnal |
| Volume | 56 |
| Issue number | 5 |
| State | Published - Sep 1984 |
ASJC Scopus subject areas
- Biochemistry