Abstract
The influences of nonuniform activity distribution within a porous solid support on the apparent kinetic parameters, Vmapp and Kmapp, of immobilized enzyme reactions following the Michaelis-Menten kinetics were theoretically investigated. As the enzyme is distributed to the neighborhood of the external surface of the support, Vmapp and Kmapp approach their respective intrinsic values over a wide range of substrate concentration. There is a close relationship between the nonuniform distribution and internal diffusional resistance. Changes in these two factors provide similar effects on Vmapp and Kmapp. As long as the immobilized enzyme reaction follows Michaelis-Menten kinetics, the nonuniform activity distribution never makes Kmapp less than its intrinsic value.
| Original language | English |
|---|---|
| Pages (from-to) | 224-228 |
| Number of pages | 5 |
| Journal | Journal of Fermentation and Bioengineering |
| Volume | 77 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Jan 1 1994 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Biotechnology
- Applied Microbiology and Biotechnology
Cite this
Influences of nonuniform activity distributions on the apparent maximum reaction rate and apparent Michaelis constant of immobilized enzyme reactions. / Shiraishi, Fumihide; Miyakawa, Hiromitsu.
In: Journal of Fermentation and Bioengineering, Vol. 77, No. 2, 01.01.1994, p. 224-228.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Influences of nonuniform activity distributions on the apparent maximum reaction rate and apparent Michaelis constant of immobilized enzyme reactions
AU - Shiraishi, Fumihide
AU - Miyakawa, Hiromitsu
PY - 1994/1/1
Y1 - 1994/1/1
N2 - The influences of nonuniform activity distribution within a porous solid support on the apparent kinetic parameters, Vmapp and Kmapp, of immobilized enzyme reactions following the Michaelis-Menten kinetics were theoretically investigated. As the enzyme is distributed to the neighborhood of the external surface of the support, Vmapp and Kmapp approach their respective intrinsic values over a wide range of substrate concentration. There is a close relationship between the nonuniform distribution and internal diffusional resistance. Changes in these two factors provide similar effects on Vmapp and Kmapp. As long as the immobilized enzyme reaction follows Michaelis-Menten kinetics, the nonuniform activity distribution never makes Kmapp less than its intrinsic value.
AB - The influences of nonuniform activity distribution within a porous solid support on the apparent kinetic parameters, Vmapp and Kmapp, of immobilized enzyme reactions following the Michaelis-Menten kinetics were theoretically investigated. As the enzyme is distributed to the neighborhood of the external surface of the support, Vmapp and Kmapp approach their respective intrinsic values over a wide range of substrate concentration. There is a close relationship between the nonuniform distribution and internal diffusional resistance. Changes in these two factors provide similar effects on Vmapp and Kmapp. As long as the immobilized enzyme reaction follows Michaelis-Menten kinetics, the nonuniform activity distribution never makes Kmapp less than its intrinsic value.
UR - http://www.scopus.com/inward/record.url?scp=0028278944&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028278944&partnerID=8YFLogxK
U2 - 10.1016/0922-338X(94)90332-8
DO - 10.1016/0922-338X(94)90332-8
M3 - Article
AN - SCOPUS:0028278944
VL - 77
SP - 224
EP - 228
JO - Journal of Bioscience and Bioengineering
JF - Journal of Bioscience and Bioengineering
SN - 1389-1723
IS - 2
ER -