Biomedical Engineering Reference
In-Depth Information
The experimental data shown in Fig. 9 were used for the determination of the
kinetic parameters.The kinetic model of substrate inhibition was in the form:
V
m
c
Sb
v(c
S
,c
P
,
P
) =
(35)
42594
c
Sb
K
m
+ c
Sb
+
41
K
i
1-
e
V
m
c
Sb
v
obs
=
h
6 42594
.
(36)
e
c
Sb
K
m
+ c
Sb
+
41
K
i
The thermometric data in Fig. 9 were transformed via parameter
,which was
determined by calibration [29] and used to determine the kinetic parameters
V
m
,K
m
and K
i
in Eq. (36) by nonlinear regression. The effectiveness factor
values were calculated by solving Eq. (7) using the orthogonal collocation pro-
cedure [37]. As can be seen in Fig. 9, the kinetic behavior corresponds to a
reaction slightly inhibited by substrate. When the bulk concentration of the
substrate exceeds the maximum on the kinetic curve, the resistance to mass
transfer can increase the reaction rate by decreasing the actual substrate con-
centration in the enzyme site. Generally, this situation is expressed by effec-
tiveness factor values being greater than 1. Values of the effectiveness factor
calculated on the basis of kinetic parameters obtained for penicillin acylase
are represented in Fig. 10.
a
Fig. 10.
Effectiveness factor values for immobilized penicillin acylase calculated by Eq. (6).
Kinetic parameter values (K
m
=1.5 mM, K
i
=570 mM) were calculated from results in Fig. 11.
Parameter of lines is input penicillin G concentration in mM [29]
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