Investigating the Effect of pH on the Activity of an Enzyme
For this investigation, I will be finding out the effect of pH on the activity of the enzyme potato catalase. Catalase is found in all living organisms. It has one of the highest turnover rates of all enzymes; one molecule of catalase can convert millions of molecules of hydrogen peroxide to water and oxygen per second. Catalase occurs in many plant and animal tissues. It breaks down toxic hydrogen peroxide, a by-product of many bio-chemical reactions, into water and oxygen.
Variables
The variables that I will ensure remain constant through the experiment will be:
- Substrate concentration and enzyme concentration
- Temperature
- Volume of substrate and volume of enzyme.
- Volume of buffer solution used.
The independent variable (what I am changing) for my experiment, is the pH level.
I will use all 14 values of pH: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, and 14. To make sure the solution is at the right pH I will use pH buffer solutions (solutions that maintain a constant pH). This is an easy and effective way of changing the independent variable.