The Effect Of Ph On Catalase Activity

We are studying the effect of pH on catalase activity. Catalase by scavenging hydrogen peroxide to water and oxygen is an important enzyme of cell defense mechanisms against oxidative stress in all living organisms (Dat et al., 2003). Cells use catalase because it is the most efficient enzyme as an antioxidative enzyme which lowers hydrogen peroxide or superoxide to accumulate to toxic levels in plant growth (Bowler et al. 1992). The formula that involves catalase as the enzyme is . pH is a measure of the Hydrogen ion concentration of a solution (What is pH). For this experiment, we are using pH to see its effect on enzyme activity in catalase solution.
Researchers conducted a study on the effect of catalase activity for bovine liver at high
We then poured 30 ml of the catalase solution into three 50 ml beakers. We also added 10 ml of water to each of the 50 ml beakers containing the catalase solution. For the catalase activity measuring apparatus kit, we filled the container halfway with water, and we filled the graduated cylinder with water all the way to the 0 ml mark. We also made sure that the hose was under the graduated cylinder in the container of water. Next, the group poured in 40 ml of 1% Hydrogen Peroxide and catalase solution into the gas stopper. Once the reaction started every 5 seconds, we would record how much oxygen was produced for 30 seconds. We repeated that for two trials. We then used a plastic cup to lower the pH of the catalase solution from 6 to 3.5, by adding 1 M of Hydrochloric acid to the solution. To make sure it was a pH that was needed, we used a pH test strip. We added 40 ml of 1% Hydrogen Peroxide and the altered catalase solution into the gas stopper. Once the reaction started every 5 seconds, we would record how much oxygen was produced for 30 seconds. We repeated that process for two trials For the third experimental group we altered the pH of the catalase solution from a pH of 6 to a pH of 8 by adding 1 M of Sodium Hydroxide to the solution. To make sure it was a pH that was needed, we used a pH test strip. We added 40 ml of 1% Hydrogen Peroxide and altered catalase
The results that we got from performing the experiment supports our hypothesis, because when the pH of the catalase was not changed or changed slightly oxygen was produced. Our data suggests that catalase solution that is not changed a lot by an acid and base is the most effective in enzyme activity. However, when the pH of the solution was altered by 3-5 levels of pH there was no enzyme activity. The control catalase without any acid or base added to it at a pH of 6 produced 8-12 ml of oxygen every 5 seconds for thirty seconds (Figure 5). However for trials 2 and 4, they were similar because the pH of the catalase solution was altered enough to change the structure and break the bonds which resulted in no oxygen production. For example, trial 2 had a decent amount of 1 M Hydrochloric acid added to the catalase resulting in a drop of pH from 6 to 3.5. There was no oxygen produced for the 30 seconds given (Figure 5). Similarly, a catalase solution with an addition of Sodium Hydroxide resulting in an increase from a pH of 6 to 12 did not produce any oxygen for the 30 seconds given, so the average final volume was 0 ml (Figure 5). The catalase solution that was changed by the Sodium Hydroxide to