Biochemical engineering by James M. Lee
By James M. Lee
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2. 57) k = A0 e− E / RT Consequently, when ln k is plotted versus 1/T, a straight line with slope -E/R is obtained. The temperature dependence of many enzyme-catalyzed reactions can be described by the Arrhenius equation. An increase in the temperature increases the rate of reaction, since the atoms in the enzyme molecule have greater energies and a greater tendency to move. However, the temperature is limited to the usual biological range. As the temperature rises, denaturation processes progressively destroy the activity of enzyme molecules.
5) Eq. 15) − S = k1CS CE − k2CES dt Assume that the change of CES with time, dCES/dt, is negligible compared to that of CP or CS. 16) = k1CS CE − k2CES − k3CES ≅ 0 dt Substitution of Eq. 16) into Eq. 9) Substituting Eq. 9) into Eq. 17) CES = k 2 + k3 + CS k1 Substitution of Eq. 17) into Eq. 18) r= P =− S = k2 + k3 + dt dt K C M S + CS k1 which is the same as the Michaelis-Menten equation, Eq. 11), except that the meaning of KM is different. In the Michaelis-Menten approach, KM is Enzyme Kinetics 2-11 equal to the dissociation constant k2/k1, while in the Briggs-Haldane approach, it is equal to (k2 + k3)/k1.
Is the two-reactor system more efficient than one reactor whose volume is equal to the sum of the two reactors? 11 Suppose that the following sequence describes an enzyme-substrate reaction with product inhibition: k1 """ # ES E + S $"" k2 " k3 """ # EP E + P $"" k4 " k5 """ # ESP ES + P $"" k6 " k7 """ # EPS EP + S $"" k8 " k 9 →E + P ES 2-40 Enzyme Kinetics a. Derive the rate equation by making the Michaelis-Menten assumption. b. How can the rate equation derived in part (a) be simplified if ESP and EPS are the same?