In this experiment, you will try to figure out the rate at which the enzyme catalase converts the substrate. You will allow catalase to react with hydrogen peroxide for different amounts of time. Enzymes catalyze reactions by lowers the activation energy for a reaction to appear. The substrate is the substance acted upon by an enzyme. Substrate molecules are changed, and product is formed. The enzyme molecule is unchanged after the reaction, and it can continue to catalyze. Each enzyme is specific for the reaction it will catalyze. Once you add a small amount of catalase to hydrogen peroxide, you will see bubbles forming. Enzymes are globular proteins. As temperature is increased the chemical reaction also increases. Catalysis will increase at higher temperatures. Every single enzyme has a temperature optimum, and if it pasts their optimum point the enzyme's functional shape is lost. Boiling temperatures will denature most enzymes. Then in order to determine the amount of hydrogen peroxide that remains, you will do a titration with KMnO4. The point of this titration is to examine how much substrate has been broken down by catalase at varying times. As we slowly added KMnO4 into each of our 5 mL samples from the varying times 30, 60, 90, 120, 180, 360 seconds. You will know when the titrade is done when your sample turns light brown. Our results were pretty accurate, but there were two points that were inaccurate, which was the 90 and 120 seconds. The results