Typical approaches to kinetic analyses (from a chemistry point-of-view) reduce mechanisms to simple Michaelis-Menten type first-order kinetics to avoid mathematical complexity. This case study considers a two-stage enzymatic reaction modelled in four different ways of increasing complexity. The simplest (Michaelis-Menten type) model proved to be a good fit for the batch experimental data in regions of high reagent concentration but failed elsewhere. A more complex system of differential equations which closely follows the true reaction mechanism was able to fit the full range of experimental data, find constant reaction rate constants and was successfully used to predict the results of the same reaction run continuously in a packed bed reactor. This work may serve as an example for more rigorous reaction modelling in future which has the potential to greatly aid reactor design.

Az előadás a Formális reakciókinetikai szeminárium előadása.