Join thousands of students who trust us to help them ace their exams!Watch the first video
Multiple Choice
Which of the following approaches is most appropriate to test the specificity of catalase in an enzyme inhibition experiment?
A
Measure the activity of catalase in the absence of any substrate.
B
Use a substrate structurally similar to hydrogen peroxide and observe if catalase catalyzes its breakdown.
C
Increase the temperature to denature catalase and observe the reaction rate.
D
Add a non-specific inhibitor and measure the change in pH.
Verified step by step guidance
1
Understand the role of catalase: Catalase is an enzyme that specifically catalyzes the breakdown of hydrogen peroxide (H₂O₂) into water (H₂O) and oxygen (O₂). Its specificity means it works primarily with hydrogen peroxide as its substrate.
Define enzyme specificity testing: To test the specificity of catalase, you need to determine whether it can catalyze the breakdown of a substrate other than hydrogen peroxide. This involves using a structurally similar substrate to hydrogen peroxide and observing whether catalase can act on it.
Select a structurally similar substrate: Identify a compound that resembles hydrogen peroxide in structure, such as organic peroxides or other molecules with similar functional groups. This ensures the test focuses on structural similarity and enzyme-substrate interaction.
Design the experiment: Introduce the structurally similar substrate to the reaction system containing catalase. Measure the reaction rate or observe whether the substrate is broken down into products. Compare this to the reaction rate with hydrogen peroxide to assess specificity.
Analyze the results: If catalase catalyzes the breakdown of the structurally similar substrate, it may indicate broader specificity. If no reaction occurs, it confirms the enzyme's high specificity for hydrogen peroxide.