Robust numerical method for a singularly perturbed problem arising in the modelling of enzyme kinetics

A system of two coupled nonlinear initial value equations, arising in the mathematical modelling of enzyme kinetics, is examined. The system is singularly perturbed and one of the components will contain steep gradients. A priori parameter explicit bounds on the two components are established. A num...

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Main Authors: John J. H. Miller, Eugene O'Riordan
Format: Article
Language:English
Published: Bulgarian Academy of Sciences, Institute of Mathematics and Informatics 2020-09-01
Series:Biomath
Subjects:
Online Access:http://www.biomathforum.org/biomath/index.php/biomath/article/view/1366
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author John J. H. Miller
Eugene O'Riordan
author_facet John J. H. Miller
Eugene O'Riordan
author_sort John J. H. Miller
collection DOAJ
description A system of two coupled nonlinear initial value equations, arising in the mathematical modelling of enzyme kinetics, is examined. The system is singularly perturbed and one of the components will contain steep gradients. A priori parameter explicit bounds on the two components are established. A numerical method incorporating a specially constructed piecewise-uniform mesh is used to generate numerical approximations, which are shown to converge pointwise to the continuous solution irrespective of the size of the singular perturbation parameter. Numerical results are presented to illustrate the computational performance of the numerical method. The numerical method is also remarkably simple to implement. ?
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spelling doaj.art-721ff393b03543ab8ca3716a93bd49012023-09-02T10:36:14ZengBulgarian Academy of Sciences, Institute of Mathematics and InformaticsBiomath1314-684X1314-72182020-09-019210.11145/j.biomath.2020.08.227858Robust numerical method for a singularly perturbed problem arising in the modelling of enzyme kineticsJohn J. H. MillerEugene O'RiordanA system of two coupled nonlinear initial value equations, arising in the mathematical modelling of enzyme kinetics, is examined. The system is singularly perturbed and one of the components will contain steep gradients. A priori parameter explicit bounds on the two components are established. A numerical method incorporating a specially constructed piecewise-uniform mesh is used to generate numerical approximations, which are shown to converge pointwise to the continuous solution irrespective of the size of the singular perturbation parameter. Numerical results are presented to illustrate the computational performance of the numerical method. The numerical method is also remarkably simple to implement. ?http://www.biomathforum.org/biomath/index.php/biomath/article/view/1366enzyme-substrate dynamics, nonlinear system, shishkin mesh, parameter-uniform convergence
spellingShingle John J. H. Miller
Eugene O'Riordan
Robust numerical method for a singularly perturbed problem arising in the modelling of enzyme kinetics
Biomath
enzyme-substrate dynamics, nonlinear system, shishkin mesh, parameter-uniform convergence
title Robust numerical method for a singularly perturbed problem arising in the modelling of enzyme kinetics
title_full Robust numerical method for a singularly perturbed problem arising in the modelling of enzyme kinetics
title_fullStr Robust numerical method for a singularly perturbed problem arising in the modelling of enzyme kinetics
title_full_unstemmed Robust numerical method for a singularly perturbed problem arising in the modelling of enzyme kinetics
title_short Robust numerical method for a singularly perturbed problem arising in the modelling of enzyme kinetics
title_sort robust numerical method for a singularly perturbed problem arising in the modelling of enzyme kinetics
topic enzyme-substrate dynamics, nonlinear system, shishkin mesh, parameter-uniform convergence
url http://www.biomathforum.org/biomath/index.php/biomath/article/view/1366
work_keys_str_mv AT johnjhmiller robustnumericalmethodforasingularlyperturbedproblemarisinginthemodellingofenzymekinetics
AT eugeneoriordan robustnumericalmethodforasingularlyperturbedproblemarisinginthemodellingofenzymekinetics