Steady-state behavior systemic analysis

Segel, I.H., Enzyme Kinetics Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems . John Wiley Sons, New York, 1975. 

In this section, the analysis of the data reconciliation problem is restricted to quasi-steady-state process operations. That is, those processes where the dominant time constant of the dynamic response of the system is much smaller than the period with which disturbances enter the system. Under this assumption the system displays quasi-steady-state behavior. The disturbances that cause the change in the operating conditions may be due to a slow variation in the heat transfer coefficients, catalytic... 

Segel IH. 1993. Enzyme kinetics. Behavior and analysis of rapid equilibrium and steady-state enzyme systems. New York Wiley. 

Kinetic Considerations. The reaction kinetics are masked by a desorption process as shown below and are further complicated by rate deactivation. The independence of the 400-sec rate on reactant mole ratio is not indicative of zero-order kinetics but results because of the nature of the particular kinetic, desorption, and rate decay relationships under these conditions. It would not be expected to be more generally observed under widely varying conditions. The initial rate behavior is considered more indicative of the intrinsic kinetics of the system and is consistent with a model involving competitive adsorption between the two reactants with the olefin being more strongly adsorbed. Such kinetic behavior is consistent with that reported by Venuto (16). Kinetic analysis depends on the assumption that quasi-steady state behavior holds for the rate during rate decay and that the exponential decay extrapolation is valid as time approaches zero. Detailed quantification of the intrinsic kinetics was not attempted in this work. 

Schuster, R. and Schuster, S. (1991) Relationships between modal-analysis and rapid-equilibrium approximation in the modeling of biochemical networks. Syst. Anal. Model. Simul. 8, 623-633. Segel, I.H. (1993) Enzyme kinetics Behavior andAnalysis of Rapid Equilibrium and Steady-state Enzyme Systems. (New York John Wiley Sons, Inc.). 

Segal IH. Enzyme kinetics behavior and analysis of rapid equihb-rium and steady state enzyme systems. 1975. John Wiley Sons, New York, p. 106. 

Hexokinase does not yield parallel reciprocal plots, so the Ping Pong mechanism can be discarded. However, initial velocity studies alone will noi discriminate between the rapid equilibrium random and steady-state ordered mechanisms. Both yield ihe same velocity equation and families of intersecting reciprocal plots. Other diagnostic procedures must be used (e.g., product inhibition, dead-end inhibition, equilibrium substrate binding, and isotope exchange studies). These procedures are described in detail in the author s Enzyme Kinetics behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems, Wiley-Interscience (1975),... 

Stability analysis could prove to be useful for the identification of stable and unstable steady-state solutions. Obviously, the system will gravitate toward a stable steady-state operating point if there is a choice between stable and unstable steady states. If both steady-state solutions are stable, the actual path followed by the double-pipe reactor depends on the transient response prior to the achievement of steady state. Hill (1977, p. 509) and Churchill (1979a, p. 479 1979b, p. 915 1984 1985) describe multiple steady-state behavior in nonisothermal plug-flow tubular reactors. Hence, the classic phenomenon of multiple stationary (steady) states in perfect backmix CSTRs should be extended to differential reactors (i.e., PFRs). 

Should one use the Hill plot in practice to examine the initial velocity behavior of enzymes Because infinite cooperativity is assumed to be the basis of the Hill treatment, only rapidly equilibrating systems are suitable for the Hill analysis. However, enzyme systems displaying steady-state kinetic behavior will not satisfy this requirement for this reason, one must avoid the use of kinetic data in any application of the Hill equation to steady-state enzyme systems. 

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