The concentration of a substrate can affect the rate of an enzyme-catalyzed reaction by influencing the frequency of enzyme-substrate collisions and the saturation of enzyme active sites. At low substrate concentrations, the reaction rate increases linearly with substrate concentration, as more substrate molecules are available to bind to the enzyme's active sites. However, as the substrate concentration increases, the enzyme becomes saturated, and the reaction rate plateaus, reaching its maximum velocity Vmax .To design an experiment to investigate the effect of substrate concentration on the rate of enzyme activity and inhibition, follow these steps:1. Choose an enzyme and its specific substrate: Select an enzyme that has a well-characterized substrate and is readily available. For example, you could use the enzyme catalase, which catalyzes the decomposition of hydrogen peroxide H2O2 into water H2O and oxygen O2 .2. Prepare a range of substrate concentrations: Prepare a series of substrate solutions with varying concentrations, such as 10%, 20%, 30%, 40%, and 50% hydrogen peroxide. This will allow you to observe the effect of substrate concentration on enzyme activity.3. Prepare the enzyme solution: Prepare a stock solution of the enzyme e.g., catalase at a known concentration. You may need to dilute the enzyme to an appropriate working concentration for the experiment.4. Set up a control: Prepare a control reaction without the enzyme to account for any spontaneous breakdown of the substrate.5. Measure enzyme activity: Add a fixed volume of enzyme solution to each substrate solution and mix well. Monitor the reaction by measuring the rate of product formation or substrate disappearance. For the catalase example, you could measure the rate of oxygen production using a gas pressure sensor or the decrease in hydrogen peroxide concentration using a spectrophotometer.6. Plot the results: Plot the reaction rate y-axis against the substrate concentration x-axis . The resulting graph should show an initial linear increase in reaction rate with increasing substrate concentration, followed by a plateau as the enzyme becomes saturated.7. Investigate enzyme inhibition: To study the effect of enzyme inhibition, select a known inhibitor for your chosen enzyme. Prepare a series of inhibitor solutions with varying concentrations. Repeat steps 5 and 6 with the enzyme, substrate, and inhibitor solutions. Compare the resulting graphs to determine the effect of the inhibitor on enzyme activity at different substrate concentrations.By analyzing the data obtained from this experiment, you can determine the relationship between substrate concentration and enzyme activity, as well as the effect of enzyme inhibition on this relationship.