Abstract
The effect of electrostatic field on apparent kinetic parameters in a packed-bed immobilized enzyme reactor was investigated using a mathematical model. The relationship between the dimensionless concentration of substrate consumed in the reactor and the logarithm of the unconverted fraction of substrate at the reactor outlet was nonlinear and changed remarkably according to the magnitude of electrostatic potential and the sign of charges that carry the support and substrate. For the opposite sign of these charges, the apparent Michaelis constant was less than its intrinsic value in the region of high substrate concentration, which reflects a promoting effect on the enzyme reaction by the electrostatic attraction.
| Original language | English |
|---|---|
| Pages (from-to) | 589-590 |
| Number of pages | 2 |
| Journal | Kagaku Kogaku Ronbunshu |
| Volume | 23 |
| Issue number | 4 |
| Publication status | Published - 1997 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Chemistry(all)
- Chemical Engineering(all)
Cite this
Electrostatic effect on apparent kinetic parameters in a packed-bed immobilized enzyme reactor. / Miyakawa, Hiromitsu; Shiraishi, Fumihide.
In: Kagaku Kogaku Ronbunshu, Vol. 23, No. 4, 1997, p. 589-590.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Electrostatic effect on apparent kinetic parameters in a packed-bed immobilized enzyme reactor
AU - Miyakawa, Hiromitsu
AU - Shiraishi, Fumihide
PY - 1997
Y1 - 1997
N2 - The effect of electrostatic field on apparent kinetic parameters in a packed-bed immobilized enzyme reactor was investigated using a mathematical model. The relationship between the dimensionless concentration of substrate consumed in the reactor and the logarithm of the unconverted fraction of substrate at the reactor outlet was nonlinear and changed remarkably according to the magnitude of electrostatic potential and the sign of charges that carry the support and substrate. For the opposite sign of these charges, the apparent Michaelis constant was less than its intrinsic value in the region of high substrate concentration, which reflects a promoting effect on the enzyme reaction by the electrostatic attraction.
AB - The effect of electrostatic field on apparent kinetic parameters in a packed-bed immobilized enzyme reactor was investigated using a mathematical model. The relationship between the dimensionless concentration of substrate consumed in the reactor and the logarithm of the unconverted fraction of substrate at the reactor outlet was nonlinear and changed remarkably according to the magnitude of electrostatic potential and the sign of charges that carry the support and substrate. For the opposite sign of these charges, the apparent Michaelis constant was less than its intrinsic value in the region of high substrate concentration, which reflects a promoting effect on the enzyme reaction by the electrostatic attraction.
UR - http://www.scopus.com/inward/record.url?scp=33751180177&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33751180177&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:33751180177
VL - 23
SP - 589
EP - 590
JO - Kagaku Kogaku Ronbunshu
JF - Kagaku Kogaku Ronbunshu
SN - 0386-216X
IS - 4
ER -