Final answer:
To measure enzyme activity, one could monitor the consumption of substrate or production of the reaction product. Steady-state kinetics experiments calculate kinetic parameters like Km and Vmax, informing on enzyme saturation and maximum reaction rate.
Step-by-step explanation:
The two ways you could measure enzyme activity are by tracking the rate at which a substrate is consumed or the rate at which a product is formed in an enzymatic reaction. One way to assess these rates is through steady-state kinetics experiments, which can provide numerical measures of an enzyme's capabilities, including its catalysis and binding strength. These experiments involve calculating kinetic parameters such as Km, which indicates how quickly the enzyme becomes saturated with a particular substrate, and Vmax, which describes the maximum rate of the catalyzed reaction.
In practice, substrate concentration in kinetic experiments is typically varied, and enzyme concentrations are adjusted to ensure measurable reaction rates. Measurements might be obtained using techniques like fluorescence in semi-micro cuvettes to reduce inner filter effects, allowing for precise monitoring of enzyme activity under various conditions influenced by pH, temperature, and the concentration of enzyme and substrate.