oConclusions
In Part 1 of the lab, 2.2ml of hydrogen peroxide decomposed over a period of seven days without the aid of catalase. This is due to the fact hydrogen peroxide is naturally volatile, meaning it has a rate of natural decomposition without the aid of catalase. However, because it only decomposes at 8.09% its total mass per day, the body must produce catalase to rid itself of the toxic substance at a much quicker rate. Part 1 establishes the need for catalase production in the body. The results of Part 2 establish the fact that catalase aids in the rapid decomposition of Hydrogen Peroxide. This is made apparent with the fact that small bubbles formed in Part 2a during the catalyzation of Hydrogen Peroxide. Part 2b proves the fact that an excessive amount of heat will almost surely denature an enzyme. Prior to the catalyzation of Hydrogen Peroxide, the catalase solution was boiled and allowed cool for a period of five minutes. When added to the Hydrogen Peroxide, the catalase did not react. Evidence of this is provided when the solution of catalase and hydrogen peroxide did not bubble when the catalase was added, this signifies an inactive solution. This occurred because boiling the catalase, the necessary enzyme, prior to adding it to Hydrogen Peroxide denatures it, causing it to be unable to decompose the Hydrogen Peroxide. Denaturation of an enzyme is when the chemical bonds that hold the amino acid groups that make up the enzyme are broken, altering its primary structure and therefore altering the function of the enzyme itself. Because the catalase was boiled, its primary structure was destroyed, and its function, decomposing the Hydrogen Peroxide, was lost. Part 2c of the lab proves that catalase works extremely efficiently in living tissue. Large amounts of Hydrogen Peroxide were decomposed in both the potato and liver tissues. This fact is obvious as large volume of bubbles formed in both the potato and liver tissues after adding the catalase. These...
