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Effect of pH on the activity of potato catalase

Introduction
Catalase is like most enzymes affected like pH changes. Catalase occurs in many plant and animal
tissues, it breaks down hydrogen peroxide into water and oxygen. Hydrogen peroxide is a toxic so the
expected pH level which the catalase can work under would be under pH 7, acidic solutions as hydrogen
peroxide is acidic.
Hypothesis
The rate of enzyme activity (catalase breaks down hydrogen peroxide) would increase closer to the
optimum pH level and then decrease once the optimum pH level is exceeded. The rate of enzyme
activity would be higher at lower pH levels, more gas would be evolved due to the decomposition of
hydrogen peroxide by the enzyme catalase.
At pH levels which are higher or lower than the optimum pH, the enzyme would denature. This is
because the H+ or OH- ions of the solution will interact with the amino acids in the enzyme, breaking
bonds such as the hydrogen bonds between the R groups, the ionic bonds between the charged R
groups and the hydrophilic interactions within the globular protein (enzyme) disrupting the enzymes
tertiary structure causing it to lose the shape of the active site, which is specific to a specific substrate.
Without the specific shape of the active site, the enzyme is non functional (cannot be as a catalyst).
The substrate which the enzyme is catalyzing cannot bind onto the active site and the enzyme-substrate
complex cannot be achieved, which makes the enzyme non functional.

Results

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