Biomedical Engineering Reference
In-Depth Information
This approach was used for the study of the kinetic properties of invertase
immobilized on the cellulose bead surface [27,30,33].In the following example
the kinetic model described for invertase was used [34]
V
m
c
S
W
v(c
Sb
,c
Pb
,
P
) =
(25)
948 42
c
S
W
0
K
m
+ c
S
+
K
i
where W/W
0
expresses the effect of the decrease in the activity of water on the
reaction rate at high sucrose concentrations [34].Introducing the kinetic model
in Eqs.(1),(3) and (14) we obtain
dc
Sb
(1-
e)
V
m
c
Sb
W
=-
(26)
7
729484 42
dz w c
Sb
W
0
K
m
+ c
Sb
+
41
K
i
dT (1-
e)(
-
D
H
r
)
V
m
c
Sb
W
=-
.
(27)
33
7294425946
dz w
Ç
C
P
c
Sb
W
0
K
m
+ c
Sb
+
41
K
i
Depending on the overall activity of the enzyme immobilized in the column two
characteristic cases were studied:
1. The activity was so low that the change in substrate concentration along the
column had no influence on the enzyme reaction rate and the column was
regarded as a differential reactor.
2. The activity was so high that the change in substrate concentration along the
column could not be neglected.
5.1.2.1
Low Enzyme Activity
In this case,which had been investigated in previous work [27],the results were
identical to those of kinetic measurements using an independent analyti-
cal method. Introducing the kinetic model [Eq. (25)] into Eq. (14) and com-
bining with Eq. (19),the following expression is obtained:
a
(1-
e)
V
m
c
Sb
W
D
T
r
=
.
(28)
7292 4259441
e
c
Sb
W
0
K
m
+ c
Sb
+
41
K
i
The significance of Eq. (28) is that the thermometric data can be used for
evaluation of the kinetic parameters K
m
and K
i
, and, thus, for rapid determina-
tion of the kinetic properties of IMB preparations. This had been performed in
the previous work by investigating the kinetic properties of immobilized inver-
tase [27]. Typical kinetic data from this study are presented in Fig. 7. In this
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