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Steady‐state stability of substrate inhibited enzyme catalysis in open reaction systems
Author(s) -
O'Neill S. P.
Publication year - 1971
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260130404
Subject(s) - steady state (chemistry) , substrate (aquarium) , stability (learning theory) , transient (computer programming) , chemistry , steady state theory , thermodynamics , biological system , physics , computer science , biology , ecology , de sitter universe , machine learning , astrophysics , universe , operating system
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.