Literature DB >> 18595055

Parametric analysis of the errors associated with the Michaelis-Menten equation.

R F Brown1, M T Holtzapple.   

Abstract

Based on the well-known mechanism describing Michaelis-Menten kinetics, three rate expressions may be developed: the exact solution (Model 1), a rate equation resulting from the pseudo-steady-state assumption (Model 2), and Model 2 with the additional assumption that the amount of free substrate is approximately equal to the total amount of substrate (Model 3). Although Model 1 is the most precise, it must be integrated numerically and it requires three experimentally determined parameters. Models 2 and 3, however, are simpler and require only two parameters. Using dimensionless forms of the three models, we have evaluated the errors in the two simplified models relative to the exact solution using a wide range of parameter values. The choice of model for reactor design depends on the initial substrate to enzyme ratio (alpha(0)), and on the ratio of the Michaelis-Menten constant to the enzyme concentration (sigma). Based on a 2% model error criteria, when alpha(0) > 15 or sigma >or= 100, Model 3 is adequate; if 5 < alpha(0) < 15, or if sigma >or= 10, then Model 2 may be used; and if alpha(0) < 5 and sigma < 10, then the exact solution (Model 1) is required.

Year:  1990        PMID: 18595055     DOI: 10.1002/bit.260361109

Source DB:  PubMed          Journal:  Biotechnol Bioeng        ISSN: 0006-3592            Impact factor:   4.530


  1 in total

1.  Development of modified HCH-1 kinetic model for long-term enzymatic cellulose hydrolysis and comparison with literature models.

Authors:  Chao Liang; Chao Gu; Jonathan Raftery; M Nazmul Karim; Mark Holtzapple
Journal:  Biotechnol Biofuels       Date:  2019-02-18       Impact factor: 6.040

  1 in total

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