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

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)123-129
Number of pages7
Journalkagaku kogaku ronbunshu
Volume16
Issue number1
DOIs
Publication statusPublished - Jan 1 1990

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Chemical Engineering(all)

Fingerprint Dive into the research topics of 'Substrate Concentration Dependence of Apparent Maximum Reaction Rate and Michaelis Constant Observed in Immobilized Enzyme Reactions'. Together they form a unique fingerprint.

  • Cite this