Substrate Concentration Dependence of Apparent Maximum Reaction Rate and Michaelis Constant Observed in Immobilized Enzyme Reactions

研究成果: ジャーナルへの寄稿記事

12 引用 (Scopus)

抄録

Expressions for apparent kinetic parameters Vappm ane Kappm observed in immobilized enzyme reactions with diffusional and electrostatic effects are proposed on the basis of the equation of a tangent to the curve of a Sb/υ versus Sb plot. The validity of these expressions is shown by comparing the expression for Kappm with two approximate expressions proposed by other workers for the reaction catalyzed by an enzyme immobilized on the external surface of a nonporous support. Calculation showed that the effect of substrate concentration on Vappm and Kappm is basically different for systems where an enzyme is immobilized on the external and pore surfaces respectively of supports.

元の言語英語
ページ(範囲)123-129
ページ数7
ジャーナルkagaku kogaku ronbunshu
16
発行部数1
DOI
出版物ステータス出版済み - 1 1 1990

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Immobilized Enzymes
Reaction rates
Enzymes
Substrates
Kinetic parameters
Electrostatics

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Chemical Engineering(all)

これを引用

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AB - Expressions for apparent kinetic parameters Vappm ane Kappm observed in immobilized enzyme reactions with diffusional and electrostatic effects are proposed on the basis of the equation of a tangent to the curve of a Sb/υ versus Sb plot. The validity of these expressions is shown by comparing the expression for Kappm with two approximate expressions proposed by other workers for the reaction catalyzed by an enzyme immobilized on the external surface of a nonporous support. Calculation showed that the effect of substrate concentration on Vappm and Kappm is basically different for systems where an enzyme is immobilized on the external and pore surfaces respectively of supports.

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