Kinetics of Fermentation by Enzymes: A Mathematical Approach

Authors

  • Semiu Adebayo Kareem Department of Chemical Engineering, Federal University of Technology Yola, Adamawa State, Nigeria
  • Haruna Mavakumba Kefas Department of Chemical Engineering, Federal University of Technology, Yola, Adamawa State, Nigeria.
  • Ternenge Joseph Chior Department of Chemical Engineering, Federal University of Technology, Yola, Adamawa State, Nigeria.
  • Ganiyu Kayode Latinwo Department of Chemical Engineering, Ladoke Akintola University of Technology, Ogbomosho, Oyo State, Nigeria.

Keywords:

fermentation, rate-determining step, steady state approximation and quasi-equilibrium

Abstract

To explain the kinetics of enzyme-substrate reactions, Michaelis and Menten (1913) came up with a mechanism, which uses an equilibrium assumption. Briggs and Haldane (1925), on the other hand, employed a steady-state assumption in place of the equilibrium assumption and came up with their own mechanism. In this work, the method outlined by Boudart (1968) for surface reaction was applied to mechanism of enzyme-substrate reactions. The Cramer’s rule was applied to solve the sets of algebraic equations obtained from the method. The results obtained are similar to those of Michaelis and Menten as well as those of Briggs and Haldane. This work shows the power of applied Mathematics to explain natural phenomena and attestation to the fact that enzyme-catayzed reactions are another form of surface reaction.

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Issue

Vol. 15 No. 2 (2011): October 2011

Section

Articles