Final answer:
In an inhibition experiment, the substrate is added after a short delay to allow the enzyme and inhibitor to form a stable interaction, ensuring a proper examination of inhibitor effects on enzyme activity.
Step-by-step explanation:
In an enzyme inhibition experiment, the addition of substrate is delayed to allow the enzyme and inhibitor to interact and reach a state of equilibrium. By waiting for about 1 minute before adding the substrate, it ensures that the inhibitor has sufficient time to bind to the enzyme and either block the active site or alter the enzyme's configuration, which affects its ability to bind with the substrate effectively.
This controlled timing allows for the assessment of the inhibitor's effect on enzyme activity at a steady state, before the enzyme has a chance to start converting substrates into products. The enzyme is added to initiate the reaction, and the inhibitor is added to inhibit the enzyme activity. By waiting 1 minute before adding the substrate, you allow enough time for the inhibitor to bind to the enzyme and inhibit its activity. This way, you can measure the extent of inhibition caused by the inhibitor in the presence of different substrate concentrations.