Lortie R, André G
Biotechnology Research Institute, National Research Council Canada, Montréal.
Enzyme Microb Technol. 1991 Dec;13(12):960-3. doi: 10.1016/0141-0229(91)90117-s.
The use of a simple rate equation with apparent parameters to describe the kinetic behavior of an immobilized enzyme with uncompetitive [corrected] substrate inhibition was assessed. To do so, the reaction rate was calculated as a function of the interfacial substrate concentration, and the results were used to identify the apparent kinetic parameters by nonlinear regression. This procedure was repeated for different values of the diffusional constraints and of the inhibition constant. The equation using apparent parameters can describe the global kinetic behavior, provided that the diffusional and inhibitory constraints are not too high. When the constraints are high, a Michaelis-Menten equation can be used to model the kinetics for interfacial concentrations lower than the concentration leading to the maximum reaction rate.
评估了使用具有表观参数的简单速率方程来描述具有非竞争性[校正后]底物抑制的固定化酶的动力学行为。为此，将反应速率计算为界面底物浓度的函数，并使用结果通过非线性回归确定表观动力学参数。对扩散限制和抑制常数的不同值重复此过程。使用表观参数的方程可以描述整体动力学行为，前提是扩散和抑制限制不太高。当限制较高时，米氏方程可用于模拟低于导致最大反应速率的浓度的界面浓度的动力学。
