Theoretical analysis of intrinsic reaction kinetics and the behavior of immobilized enzymes system for steady-state conditions

Praveen, T.; Valencia, Pedro; Rajendran, L.

Abstract

Mathematical modeling of immobilized enzymes under different kinetics mechanism viz. simple Michaelis-Menten, uncompetitive substrate inhibition, total competitive product inhibition, total non-competitive product inhibition and reversible Michaelis-Menten reaction are discussed. These five kinetic models are based on reaction diffusion equations containing non-linear terms related to Michaelis-Menten kinetics of the enzymatic reaction. Modified Adomian decomposition method is employed to derive the general analytical expressions of substrate and product concentration for all these five mechanisms for all possible values of the parameters Phi(s) (Thiele modulus for substrate), Phi(p) (Thiele modulus for product) and alpha (dimensionless inhibition degree). Also we have presented the general analytical expressions for the mean integrated effectiveness factor for all values of parameters. Analytical results are compared with the numerical results and also with the limiting case results, which are found to be good in agreement. (C) 2014 Elsevier B.V. All rights reserved.

Más información

Título según WOS: Theoretical analysis of intrinsic reaction kinetics and the behavior of immobilized enzymes system for steady-state conditions
Título según SCOPUS: Theoretical analysis of intrinsic reaction kinetics and the behavior of immobilized enzymes system for steady-state conditions
Título de la Revista: BIOCHEMICAL ENGINEERING JOURNAL
Volumen: 91
Editorial: ELSEVIER SCIENCE BV
Fecha de publicación: 2014
Página de inicio: 129
Página final: 139
Idioma: English
URL: http://linkinghub.elsevier.com/retrieve/pii/S1369703X14002186
DOI:

10.1016/j.bej.2014.08.001

Notas: ISI, SCOPUS