Title: The Effect of pH on Catalase Enzyme Activity
Objective: To determine how varying pH levels affect the rate of catalase-catalyzed hydrogen peroxide decomposition.
Hypothesis: Catalase activity will be optimal at neutral pH (pH 7.0) and decrease in acidic (pH 3.0) and basic (pH 11.0) conditions due to enzyme denaturation.
Methods: Catalase solution was mixed with hydrogen peroxide at pH levels 3, 5, 7, 9, and 11. Reaction rate was measured by oxygen production volume over 60 seconds. Each condition was tested in triplicate.
Results: Maximum reaction rate occurred at pH 7.0 (mean 8.2 mL O₂/min, SD ±0.3). Rates decreased to 2.1 mL/min at pH 3.0 and 1.8 mL/min at pH 11.0. ANOVA showed significant pH effect (F=124.6, p<0.001).
Conclusion: Results support the hypothesis that catalase has optimal activity at neutral pH. Acidic and basic conditions significantly reduce activity, likely through denaturation of the enzyme's active site. Future experiments should test temperature effects and use purified enzyme preparations.
