Final answer:
To measure the maximum velocity of an enzymatic reaction, one should conduct experiments where the rate of substrate consumption is measured at varied substrate concentrations shortly after mixing the enzyme and substrate. The resulting plot will indicate Vmax as the point where an increase in substrate concentration no longer increases the reaction rate.
Step-by-step explanation:
To infer the maximum velocity (Vmax) of an enzyme-catalyzed reaction, a series of measurements should be taken on the rate of substrate consumption shortly after mixing the enzyme and substrate, for several substrate concentrations (option d).
When these measurements are plotted on a graph (often referred to as a Michaelis-Menten plot), the reaction rate will increase as the substrate concentration increases, up to a point where it levels off.
This point where the curve plateaus indicates that all enzyme active sites are saturated; thus, any further increase in substrate concentration doesn't increase the reaction rate and the Vmax is reached.
This can also be represented mathematically using the Michaelis-Menten equation or visually using a Lineweaver-Burk plot, which is a double reciprocal plot of 1/v versus 1/[S].
The intercept on the y-axis of this plot gives 1/Vmax, from which Vmax can be directly determined. However, the direct plot of reaction velocity versus substrate concentration is often preferred for its simplicity.