The aim of this study was to test the rate of reactivity of the enzyme catalase on hydrogen peroxide while subject to different concentrations of an inhibitor. The hypothesis was that hydrogen peroxide will be broken down by catalase into hydrogen and oxygen, where a higher concentration of inhibitor will yield less oxygen, resultant of a lower rate of reaction. Crushed potato samples of equal weight were placed in hydrogen peroxide solutions of various temperatures. The results showed that less gas was produced as the concentration of the inhibitor rose. This Is because more enzymes were inhibited, and so less active sites were available for reaction.
Reasearch and rationale
Catalase will break down hydrogen peroxide in water and hydrogen. A higher concentration of inhibitor will yield a slower rate of reaction, thus yielding less oxygen in a given time.
Null hypothesis: Catalase will break down hydrogen peroxide in water and hydrogen. The concentration of the inhibitor will have no effect on the rate of this reaction. Supporting knowledge: Enzymes function as biological catalysts, increasing the rate of reactions that take place within organisms. Catalase is an enzyme found in the vast majority of organisms that are exposed to oxygen, making it very common. It catalyses the decomposition of hydrogen peroxide into water and oxygen. Hydrogen peroxide is a molecule that can attack sulphur atoms and metal ions in protein molecules, and with the aid of iron ions is potentionally mutagenic. Catalase is an extremely effective enzyme, and can break down millions of hydrogen peroxide molecules in a single second. As such, it can be seen how important and effective catalase is to oxygen-exposed organisms. As with the majority of enzymes, it has an optimum pH of approximately 7, though the optimum can vary by species. Haliotis discus discus, a type of shellfish, for example, has catalase which works at an optimum pH of 10.5. There are a