The influence of pH to enzyme potato catalase

In this experiment we are investigating the influence of pH on the activity of an enzyme potato catalase. The aim is to determine how pH can affect the the rate of the reaction catalysed by athis enzyme, and what is the optimal pH in which this enzyme works most effectively.
Our hypothesis states that the optimal pH of potato catalase is approximately 7.0, because according to literature values, catalase is an enzyme which works best at neutral solution. If the solution is too acidic (low pH value) or too basic (high pH value), the catalase is inactive.
In this experiment , potato discs in solutions of known pH act on hydrogen peroxide , and the rate at which oxygen is evolved is measured. This reflects the activity of the catalase in the potato.
With a cork borer we cut cylinders of potato tuber tissue about 1 cm diameter. We cut the cylinder into discs 1mm thick.
K PO 2H O (cm )
Citric acid (cm )
3.0
20.55
79.45
4.0
38.55
61.45
5.0
51.50
48.50
6.0
63.15
36.85
7.0
82.35
17.65
8.0
97.25
2.75
1. Table showing amount of solutions needed to mixture to make buffers of different pH.
When the buffers were prepared we checked their pHs with indicators to be sure the pHs are exact which have to be.
Assembling the apparatus for measuring the rate at which oxygen is evolved. Firstly, we took a test tube with measurements, filled it with water, covered with a finger, turned over and placed into a beaker of water. The test tube was still turned over and filled of water. Then we took a flask linked up with a rubber bung and another end of the bung placed in the test tube.
We added 10 potato discs into the flask, with a syringe placed 5 cm of buffer solution at pH 3 and added 5 cm of hydrogen peroxide. Then we put a stopper on the flask’s neck...

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