Enzyme Peroxidase Lab Report

Enzymes are important components of life, facilitating reactions that are necessary for an organism to live. Enzymes can be very specific to what environment they function best in1. Numerous environmental impacts were tested for the enzyme peroxidase which catalyzes the decomposition of hydrogen peroxide. The basic decomposition reaction was carried out first without any environmental alterations. The hypothesis for this reaction was supported. The enzyme caused the amount of absorbance increase as time went on at a fairly constant rate (Figure 1). As shown in Figures 2A and 2B, pH has a large effect on the rate to which an enzyme catalyzes a reaction. The optimum pH for the peroxidase was 6. Each varying pH produced a different reaction rate. The pH of 3 and the pH of 9 caused the peroxidase to work at its slowest. The enzyme worked best at pH 6 which was closely followed by pH 7. Peroxidase depends on specific pH’s to be effective, most likely based upon the environment it is usually found in. The hypothesis that the different pH values would have varying effects on the rate to which peroxidase catalyzes the reaction was supported. Altering the enzyme concentration also had a great impact on the rate of the decomposition of hydrogen peroxide. As the concentration of the enzyme increased, so, too, did the rate of the reaction. This is because
The reaction was tested with 0.1 mL of H2O2, 0.2 mL of H2O2, and 0.4 mL of H2O2. All three rates of reactions calculated were within 0.0007 which is a very miniscule difference. The rates of reaction could be very similar since the amount of enzyme was not increased, so there was the same number of enzyme molecules reacting at their optimum pace while more and more substrate molecules were added. The enzyme may have been