The Effects of Ph on Peroxidas Activity

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The Effects of Temperature and Acidity on Peroxidase Activity Yohannes Eshete 14 November 2014 Peroxidase is a type of enzyme that has a large protein containing an iron ion in its active site, acting as a cofactor. Peroxidase is an appropriate enzyme for experimentation because it is easily prepared and assayed. The goal of our experiments was to find out the effects of temperature and acidity on this crucial process by taking note of its reaction rate at varying temperatures and pH levels. The results of peroxidase were observed by aggregating guaiacol which is a substance that binds to the enzyme and is oxidized when hydrogen peroxide is turned into water. A spectrophotometer was used to annotate the change in color resulting from that oxidation, which directly correlates to the amount of hydrogen peroxide converted. It has been noted that in these experiments, temperature was a more important factor than acidity. This is because the reactions were found to be most effective at temperatures between 23° to 40° Celsius, and at pH between 5 and 9. Therefore, these effects suggest that peroxidase is at its peak level of performance when it is at or a little above room temperature, and when it is at a water-like pH level. The effects of temperature and of pH were tested in this experiment. An enzyme is a type of catalyst that speeds up a chemical reaction without being consumed by the reaction. The reactant that an enzyme acts on is referred to as a substrate. To achieve a reaction, the substrate enters a pocket of the enzyme called the active site, joining to form an enzyme-substrate complex. The enzyme then facilitates the reaction by one of the following methods: 1) Acting as template for substrate orientation; 2) Stressing the substrates and stabilizing the transition state; 3) Providing a favorable microenvironment; or 4) Participating directly in

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