Homework #2 (continued) Due 10/18/07

Q1) (Problem 3.5 in Shuler & Kargi) An inhibitor (I) is added to the enzymatic reaction at a level of 1.0 a/l. The
following data were obtained for Km = 9.2 g S/l
v (rate in g/s)
0.909
0.658
0.493
0.400
0.333
0.289
0.227

[S] (in g S/l)

20
10
6.67
5
4
3.33
2.5

a) Is the inhibitor competitive or noncompetitive

b) Find KID (dissociation constant of the inhibitor binding to the enzyme, in g/l)
Q2) (Problem 3.7 in Shuler & Kargi)
Q3) Suppose we have a well-stirred tank containing an aqueous solution. The tank holds 100 liters of fluid and
fluid flows into and out of the tank at a constant rate of 10 l/min (such that the fluid volume remains constant at
100 liters). Suppose that reactant A flows into the tank at a concentration of 1.0 M.
a) If at time 0, the tank contains no A, compute an expression for the concentration of A as a function of
time in the tank. Assume no reaction occurs.
b) Now, assume that an immobilized enzyme (E) binds to A and forms product B. If the reaction is not
diffusion-limited, the Michaelis-Menton constant (Km) is 0.01 M, the total concentration of enzyme
is 0.1M, and the reaction rate constant (k2) is 0.2 min-1, compute the concentration of B in the outlet
at steady state.
Q4) A single enzyme catalyzed reaction S + E <--> SE P occurs at a planar interface between a fluid and a
nonporous solid with immobilized enzyme. The substrate and product concentrations in the bulk fluid are [S]b
and [P]b. and the mass transfer coefficients for the transport of S and P between the bulk fluid and the interface
are kL,s and kL,p. Assuming the Michaelis-Menten constant (Km) is much smaller than the substrate concentration
at the surface, determine the steady-state rate at which P appears in the bulk fluid (in units of moles per time per
unit surface area of the solid).