If an enzyme in solution is saturated with substrate, the most effective way to obtain a faster yield of products is to
a. Add more of the enzyme.
b. Heat the solution to 90°C.
c. Add more substrate.
d. Add a noncompetitive inhibitor.

Verified step by step guidance

Understand the concept of enzyme saturation: When an enzyme is saturated, it means that all active sites of the enzyme molecules are occupied by substrate molecules, and the reaction is proceeding at its maximum rate.

Consider the effect of adding more enzyme: Adding more enzyme can increase the reaction rate because it provides more active sites for the substrate to bind, thus increasing the overall capacity for the reaction to occur.

Evaluate the impact of heating the solution: Heating the solution to 90°C is likely to denature the enzyme, as most enzymes are proteins that can lose their functional shape at high temperatures, leading to a decrease in reaction rate.

Assess the result of adding more substrate: Adding more substrate will not increase the reaction rate if the enzyme is already saturated, as there are no additional active sites available for the substrate to bind.

Consider the effect of adding a noncompetitive inhibitor: A noncompetitive inhibitor binds to a site other than the active site, changing the enzyme's shape and reducing its activity, which would decrease the reaction rate.

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Key Concepts

Here are the essential concepts you must grasp in order to answer the question correctly.

Enzyme Saturation

Enzyme saturation occurs when all active sites of the enzyme molecules are occupied by substrate molecules, meaning the reaction rate has reached its maximum velocity (Vmax). At this point, adding more substrate will not increase the rate of reaction, as there are no free active sites available for additional substrate molecules to bind.

Enzyme Concentration

Increasing enzyme concentration can enhance the reaction rate when the enzyme is saturated with substrate. By adding more enzyme, additional active sites become available, allowing more substrate molecules to be converted into products, thus increasing the overall yield and speed of the reaction.

Noncompetitive Inhibition

Noncompetitive inhibitors bind to an enzyme at a site other than the active site, altering the enzyme's structure and function. This reduces the enzyme's activity regardless of substrate concentration, as it affects the enzyme's ability to catalyze the reaction, making it an ineffective method to increase product yield when the enzyme is saturated.