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Enzyme Lab Report

1150 Words5 Pages

The data received in the experiment only somewhat supported my hypothesis. My group tested how changing the pH of the hydrogen peroxide substrate would affect enzyme activity and the rate of reaction. Our hypothesis was that the solution with a pH closest to the pH of hydrogen peroxide, which is fairly acidic, would have the fastest rate of reaction. After conducting the experiment, we found that an acidic pH of 2 resulted in the reaction having a reaction rate of 0 sec-, while when conducted with a substrate pH of 7, the reaction proceeded at the fastest rate of 0.051 sec-. These results show that a pH of 7—a more neutral solution—actually caused the enzyme to work the best, as opposed to the predicted acidic substrate. While the data didn’t …show more content…

Since enzymes are extremely specific, the hydrogen peroxide can only bind to catalase because of the specific shape of catalase’s active site. If the shape of catalase is changed, then the binding of the hydrogen peroxide will be decreased, or nonexistent in the case that the catalase shape is changed so much that the tertiary structure unravels, and the enzyme becomes denatured. One factor that can cause the enzyme to change shape is pH. A acidic pH means that there are excess H+ ions in the solution, while a basic pH means that the solution contains excess OH- ions. These ions can interact with the R-groups in the enzyme and cause the shape to change. In the experiment, the optimal pH of 7 means that since its neutral there are very little ions in the solution, and the ions that are in the solution reacts with the R-groups in the catalase to actually cause the hydrogen peroxide to fit in catalase’s active site better. When the pH was decreased or increased past 7, then the excess ions changed the shape of the active site too much and the hydrogen peroxide couldn’t bind as well. Furthermore, when the pH was way too acidic or basic, like with the pH of 2, the excess ions caused the enzyme to denature, thus resulting in the reaction rate of 0

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