Influences of Nonuniform Activity Distributions on the Apparent Maximum Reaction Rate and Apparent Michaelis Constant of Immobilized Enzyme Reactions
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概要
- 論文の詳細を見る
The influences of nonuniform activity distribution within a porous solid support on the apparent kinetic parameters, V_m^<app> and K_m^<app>, of immobilized enzme reactions following the Michaelis-Menten kinetics were theoretically investigated. As the enzyme is distributed to the neighborhood of the external surface of the support, V_m^<app> and K_m^<app> 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 V_m^<app> and K_m^<app>. As long as the immobilized enzyme reaction follows Michaelis-Menten kinetics, the nonuniform activity distribution never makes K_m^<app> less than its intrinsic value.
- 公益社団法人日本生物工学会の論文
- 1994-02-25
著者
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Shiraishi Fumihide
Department Of Biochemical Engineering And Science Faculty Of Computer Science Adn Systems Engineerin
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MIYAKAWA HIROMITSU
Department of Chemical and Biological Engineering, Sasebo College of Technology
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Miyakawa Hiromitsu
Department Of Chemical And Biological Engineering Sasebo College Of Technology
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