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Implicit Analytic Solution of Michaelis–Menten–Monod Kinetics

[Image: see text] An analytic solution to enzyme kinetics expressed by the Michaelis–Menten–Monod mathematical framework is presented. The analytic solution describes the implicit problem with the independent variable, normally time, substituted with the concentration of the reaction product. The an...

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Detalles Bibliográficos
Autores principales: Maggi, Federico, la Cecilia, Daniele
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2016
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6640786/
https://www.ncbi.nlm.nih.gov/pubmed/31457171
http://dx.doi.org/10.1021/acsomega.6b00174
Descripción
Sumario:[Image: see text] An analytic solution to enzyme kinetics expressed by the Michaelis–Menten–Monod mathematical framework is presented. The analytic solution describes the implicit problem with the independent variable, normally time, substituted with the concentration of the reaction product. The analytic solution provides the substrate, enzyme, and microbial biomass concentration instantaneously and over all time domains without the use of numerical integration schemes or iterative solvers required to overcome transcendental functions. Experiments of NO(2)(–) nitrification by Candidatus Nitrospira defluvii at temperatures ranging between 10 and 32 °C were used for validation tests with the numerical solution by finite differences and the implicit analytic solution presented here. Results showed that both finite differences and analytic solutions matched the experiments particularly well, with a correlation coefficient greater than 0.99 and residuals smaller than 2.75%.