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Through a set of experiments involving two separate enzymes and  2H₂O₂, we observed the following reactions.

We created a set of observations compiling the amount of gas released by the interaction between Catalase A and 2H₂O₂ over time. In looking at our data in contrast with the data of the class, it was observed that the amount of 2H₂O₂ has an effect on the rate of interaction as well as the end products. The more 2H₂O₂ used in the experiment (.5 mL or 1 mL), the more gas produced by the reaction.

In a second set of observations regarding the effect of pH on the rate of the reaction (the breakdown of 2H₂O₂), we saw that the higher the acidity of the2H₂O₂  solution, the slower the reaction.

In a third set of observations regarding the effect of temperature on the rate of the breakdown of 2H₂O₂, we saw that the lower the temperature, the higher the rate of the reaction.

In a fourth set of observations regarding the effect of enzyme concentration on the rate of breakdown, we saw that the higher the concentration, the faster the reaction.

All in all, it was observed that an enzyme, which obviously engenders the breakdown of 2H₂O₂, has unique properties. Firstly, enzymes speed up the breakdown, without themselves breaking down. Secondly, the higher the concentration of the enzyme and the higher the amount of the 2H₂O₂, the faster the rate of reaction. So, the amount of both enzyme and solution directly affects the speed at which the two interact. Puzzling, though, are the observations which prove that acidity and heat do not speed up the rate of breakdown. We have concluded that the more neutral the pH and the less affected the temperature (closer to room temperature), the faster the reaction. So, it seems that the best conditions for an enzyme to break down 2H₂O₂, are those that are the most natural. Our observations would suggest that enzymes are not alive.