Turnip Peroxidase Lab Report

As pH increases or decreases to get closer to the optimal pH --in this case it is 7 for this particular enzyme-- the rate of reaction peaks and is highest at that point, which is described by the molecular shape and structure of the enzyme at its optimal pH. When turnip peroxidase is at pH 7, the active site is able to fit perfectly with the substrate, therefore explaining why the reaction rate is fastest at this point. Accordingly, if the active site is disrupted, the substrate cannot fit perfectly causing the reaction rate to slow down. This can be supported by the data because the reaction rate gradually increased from pH 3 to pH 7 and reached its maximum at pH 7. Once it did reach the optimal pH, the reaction rate continuously decreased

Because of the fact that reactions are catalyzed by enzymes when they randomly collide with substrate molecules, increasing the temperature would increase the reaction rate. Increasing the temperature further increases the vibrational energy of the enzyme molecules, straining the bonds that keep them together. Furthermore, when the temperature is higher, more bonds will break because of these strains, causing the active site of the enzymes to change too. Similar to pH, a change in the shape of the active site leads to the substrate not being able to fit perfectly, leading to the enzyme not being able to catalyze the reaction. Overall, an increase in temperature will cause the rate of reaction to increase initially due to the increased kinetic energy. Nevertheless, the effects caused by the breakage of bonds will eventually lead to a decrease in the rate of reaction. As seen in the data, the reaction rate increased from 0.088 to 0.101 throughout the interval of -5℃ to 20℃ then decreased to 0.037 throughout the interval 20℃ to 56℃. This can be explained by the fact that 20℃ is the optimal temperature, therefore the active site of the enzyme is complementary to the substrate, causing the rate of reaction to be