Influences of nonuniform activity distributions on the apparent maximum reaction rate and apparent Michaelis constant of immobilized enzyme reactions

Fumihide Shiraishi, Hiromitsu Miyakawa

Research output: Contribution to journalArticle

14 Citations (Scopus)

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 languageEnglish
Pages (from-to)224-228
Number of pages5
JournalJournal of Fermentation and Bioengineering
Volume77
Issue number2
DOIs
Publication statusPublished - Jan 1 1994
Externally publishedYes

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Immobilized Enzymes
Reaction rates
Enzyme kinetics
Enzymes
Kinetics
Kinetic parameters
Substrates

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Applied Microbiology and Biotechnology

Cite this

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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.",
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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.

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