Substrate-concentration dependences of the apparent, maximum-reaction rate and Michaelis-Menten constant in immobilized enzyme reactions

研究成果: ジャーナルへの寄稿記事

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抄録

Expressions are proposed for the apparent-rate parameters Vmapp and Kmapp of an immobilized-enzyme reaction with diffusional and electrostatic effects, based on the equation for the tangent of the Sb/v-Sb curve. The validities of the expressions are demonstrated by comparing the expression for the apparent Michaelis constant Kmapp with two approximate expressions proposed elsewhere for an enzyme-catalyzed reaction with the enzyme immobilized on the surface of a nonporous support. Calculations showed that the effect of the substrate concentration of Vmapp and Kmapp was, fundamentally, different in a system where the catalyst was immobilized on the exterior surface of support, and in a system where it was immobilized on the surface of the pores.

元の言語英語
ページ(範囲)140-147
ページ数8
ジャーナルInternational chemical engineering
32
発行部数1
出版物ステータス出版済み - 1 1 1992

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Reaction rates
Enzymes
Catalyst supports
Substrates
Electrostatics
Catalysts

All Science Journal Classification (ASJC) codes

  • Engineering(all)

これを引用

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N2 - Expressions are proposed for the apparent-rate parameters Vmapp and Kmapp of an immobilized-enzyme reaction with diffusional and electrostatic effects, based on the equation for the tangent of the Sb/v-Sb curve. The validities of the expressions are demonstrated by comparing the expression for the apparent Michaelis constant Kmapp with two approximate expressions proposed elsewhere for an enzyme-catalyzed reaction with the enzyme immobilized on the surface of a nonporous support. Calculations showed that the effect of the substrate concentration of Vmapp and Kmapp was, fundamentally, different in a system where the catalyst was immobilized on the exterior surface of support, and in a system where it was immobilized on the surface of the pores.

AB - Expressions are proposed for the apparent-rate parameters Vmapp and Kmapp of an immobilized-enzyme reaction with diffusional and electrostatic effects, based on the equation for the tangent of the Sb/v-Sb curve. The validities of the expressions are demonstrated by comparing the expression for the apparent Michaelis constant Kmapp with two approximate expressions proposed elsewhere for an enzyme-catalyzed reaction with the enzyme immobilized on the surface of a nonporous support. Calculations showed that the effect of the substrate concentration of Vmapp and Kmapp was, fundamentally, different in a system where the catalyst was immobilized on the exterior surface of support, and in a system where it was immobilized on the surface of the pores.

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