Steady‐state stability of substrate inhibited enzyme catalysis in open reaction systems

Substrate inhibited enzyme reactions occurring in systems open to mass transfer may display multiple steady‐state behavior. For a simple one‐substrate case it is shown theoretically that the unstable steady‐state region always lies within the conversion range of 50–100%. A criterion for the stability of a steady‐state point is given. Numerical solutions of the appropriate transient equation show how the system approaches stable steady state in instances where there are three possible steady‐state points. The consequences of the existence of an unstable region on the systems response to changes in its parameters is discussed.