Question

A scientist determined the rate of an enzyme-catalyzed reaction by measuring the amount of product formed over time. The following curve was generated from the data collected. The rate of the reaction could also be determined by measuring the change in the amount of enzyme Answer A: measuring the change in the amount of enzyme A measuring the change in the amount of substrate Answer B: measuring the change in the amount of substrate B measuring the change in salt concentration Answer C: measuring the change in salt concentration C adding more substrate Answer D: adding more substrate D adding more enzyme

Answer 1

To determine the rate of an enzyme-catalyzed reaction, one can measure the change in substrate amount or product over time; increasing substrate concentration leads to a higher reaction rate until enzyme saturation and increasing enzyme concentration increases the rate linearly with excess substrate available.

Step-by-step explanation:

The rate of an enzyme-catalyzed reaction can be determined by monitoring the change in product concentration over time. However, this rate can also be measured by observing the change in the amount of substrate. When substrate concentration is low and enzyme concentration is held constant, increasing the substrate concentration will increase the reaction rate until the enzyme becomes saturated with substrate, which is depicted as a hyperbolic curve on a graph. On the other hand, increasing the enzyme concentration in the presence of an excess of substrate will linearly increase the reaction rate, assuming all other factors are constant and the substrate is not limiting. Monitoring changes in properties such as gas volume, pressure, light absorption, and conductivity can also give insights into reaction rates for different types of reactions.

Answer 2

To determine the rate of an enzyme-catalyzed reaction, monitoring the change in substrate concentration or enzyme concentration are viable methods. The reaction rate increases with substrate concentration up to the point of enzyme saturation, whereas an increase in enzyme concentration can raise the rate if substrate is available.

Step-by-step explanation:

The rate of an enzyme-catalyzed reaction can be measured by several methods. One of these methods is to monitor the change in the amount of product formed over time. In experiments where the enzyme concentration ([E]) is held constant, the rate of product formation can vary with changes in substrate concentration ([S]). As the substrate concentration increases, the reaction rate will also increase until a point is reached where the enzyme is saturated with the substrate, and no further increase in rate can be observed.

Alternatively, the reaction rate can be affected by the amount of active enzyme present. If more enzyme molecules are available to catalyze the reaction and sufficient substrate is present, the rate of reaction will increase. This relationship typically produces a linear curve when graphed, indicating a direct proportion between enzyme concentration and reaction rate, up to the point of substrate saturation.

Thus, the reaction rate of an enzymatic process can be determined by measuring either changes in substrate concentration (if enzyme is constant) or by changes in enzyme concentration (if substrate is constant), but not by measuring changes in salt concentration or simply by adding more substrate once saturation is achieved.