Optimal designs in enzymatic reactions with high-substrate inhibition

Abstract

Abstract The Michaelis-Menten (MM) model is extensively used in biochemistry to describe reaction kinetics. However, deviations from MM kinetics can occur, usually due to an inhibition effect on the amount of substrate. Two different models, describing the kinetic reaction when this type of inhibition occurs, are introduced. Optimal experimental designs methods are used in order to find the best estimation of the parameters in these models. An application to the semicarbazide-sensitive amine oxidase (SSAO) activity towards benzylamine is presented.