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
.
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