Biomedical Engineering Reference
In-Depth Information
r M 4 E 5 ¼ k 5c ½
M 2 E 5 k 6c ½
M 4 E 5
(11.17i)
r P 1 ¼ k 4c ½
M 3 E 3
(11.17j)
r P 2 ¼ k 6c ½
M 4 E 5
(11.17k)
Assume that P 2 is the intracellular products. Since E 1 ,E 2 ,E 3 ,andE 5 are all part of the
cellular material, we further simplify Eqn (11.15j) and incorporate it into the enzyme
balances lead to:
½
E 1 T ¼½
E 1 0 þ c 1 P 2 ¼½
E 1 þ½
SE 1 þ½
M 1 E 1
(11.18a)
½
E 2 T ¼½
E 2 0 þ c 2 P 2 ¼½
E 2 þ½
M 1 E 2 þ½
M 2 E 2
(11.18b)
½
E 3 T ¼½
E 3 0 þ c 3 P 2 ¼½
E 3 þ½
M 2 E 3 þ½
M 3 E 3
(11.18c)
½
E 5 T ¼½
E 5 0 þ c 5 P 2 ¼½
E 5 þ½
M 2 E 5 þ½
M 4 E 5
(11.18d)
Mass balances in a batch reactor with constant medium volume lead to
dC j
dt ¼ r j
(11.19)
¼
0, C j ¼
¼
At time t
S 0 . The total enzyme concentrations at time 0 are each
assumed to be 2% of the total substrate S 0 , except [E 3 ] T0 ¼
0 for all j except S
0.04 S 0 . Equation (11.19) can be inte-
grated with OdexLims and the solution is shown in Fig. 11.4 .In Fig. 11.4 , we have assumed that
the increase in the amount of each enzyme is 5% of the intercellular product P 2 or
c j ¼
0.05,
except E 3 is increased by 10% of P 2 or
c 3 ¼
0.1. One can observe that the substrate
1.0
S
0.8
P 1
0.6
0.4
S 0 - S - P 1
P 2
0.2
0.0
0.0
0.5
1.0
1.5
2.0
k 1 E 0 t
FIGURE 11.4 A comparison of the full solution and approximate solution (single-step Michaelis e Menten
equation) for the reaction network showing in Fig. 11.3 . The solid lines are based on the full solution, while the
dotted lines are based on the approximated model. The kinetic constants are k j S 0 ¼
k jc ¼
0.01 k j S 0 ; k j ¼
k 1 , for all j
except j
¼
1. Also, k 1 ¼
0.01 k 1 S 0 .
Search WWH ::




Custom Search