Abstract
In the case of enzymatic reactions, the catalytic activity during the mixing time is always neglected. Using the fast acetaldehyde reduction activity of horse liver alcohol dehydrogenase (HL-ADH) (alcohol: NAD + oxidoreductase; EC 1.1.1.1) has allowed to measure the influence of the mixing time constant on the catalytic activity and to propose a theoretical model which takes into account the characteristics of the used mixing device. This theoretical model could be used as a decision tool which must be related to the kinetic of the reaction. According to the kinetics of the studied enzyme, this model will give the maximum tolerated mixing time in order not to modify the reaction kinetic analysis and so will allow to select the most adapted mixing device.
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