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Evaluation of true kinetic parameters for reversible immobilized enzyme reactions
Author(s) -
Ishikawa Haruo,
Tanaka Takenori,
Kurose Katsuo,
Hikita Haruo
Publication year - 1987
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260290803
Subject(s) - fumarase , thiele modulus , thermodynamics , kinetic energy , chemistry , reaction rate , substrate (aquarium) , reaction rate constant , diffusion , kinetics , enzyme , reversible reaction , computational chemistry , organic chemistry , catalysis , physics , biology , ecology , quantum mechanics
For a reversible one‐substrate reaction system that follows the Haldane reaction mechanism, a new and effective method has been proposed to extract true or intrinsic kinetic parameters of immobilized enzymes from diffusion limited rate data. The method utilizes the effectiveness factors correlated in terms of the general modulus defined by Aris and Bischoff, and a new modulus defined in the present study. It requires a trial‐and‐error calculation, but only a few data points. Furthermore, it provides a saving of materials such as substrates and enzymes, and takes less time for experiments compared to the initial rate methods. The usefulness of the method is demonstrated by determining the kinetic parameters for membrane bound fumarase which catalyzes the reaction of the conversion of fumarate to L ‐malate, for which the equilibrium constant is ca. 4.