Butovich I A, Tertykh V A
Ukr Biokhim Zh (1978). 1984 Sep-Oct;56(5):527-32.
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.
在邻苯二酚氧化过程中，对从马铃薯块茎中分离出的邻二酚氧化酶的失活动力学进行了研究。当酶被底物饱和时，其失活速率常数kin = 0.5 - 1.0 min⁻¹；kin取决于邻苯二酚的初始浓度。酶促反应产物的最终产量随酶的初始浓度呈线性增加。引入与邻醌缩合的乙二胺硫酸盐不会提高邻二酚氧化酶的操作稳定性。所获得的数据证明邻二酚氧化酶在酶 - 底物复合物水平失活，或因与底物的双分子反应而失活。
