Hannah Choi #7907 Per.

5, AP Biology 10 October 2011 Enzyme Catalysis Lab: Lab #2 Materials: Plastic cups Syringes Ring stand Burette clamp Burette Catalase Hydrogen Peroxide Sulfuric acid Distilled water Timer KMnO4 Margin of Error: When putting together the hydrogen peroxide and the catalase together, we might not have mixed well enough, causing an uneven distribution of the hydrogen peroxide on the bottom and the catalase on the top. In the beginning of our titration process, since it was the first time for many of us, some of the KMnO4 got on the sides of the flask, making the margin of error plus or minus one or two drops. Because of the drops on the side the amount of KMnO4 may have been larger than it should have been, thus affecting the baseline control value, which was used to calculate the amount of hydrogen peroxide that was consumed. There's a plus or minus one mL for the buret, not only because it naturally has a margin of error like all other instruments but because in our buret, we weren't able to get all the bubbles out, thus causing another error. Since we did all of our measuring of the chemicals through a syringe, there is a plus or minus one mL on most of our chemical measurements like hydrogen peroxide and the sulfuric acid. There is a plus or minus one or two seconds for when we added the catalase and the sulfuric acid for one person was looking at the timer while the other added. Because people have different methods of starting and counting (some people would start adding the catalase/ sulfuric acid after hearing the three one, two, three while others might have waited a second after hearing the three then added the catalase/sulfuric acid. Conclusion: After reading the lab and actually doing it, my understanding of what enzymes do is a lot better. An enzyme is a protein that is produced by a living cell and is a catalyst in biochemical reactions. Since it is a catalyst, this means that it can change the rate of a chemical reaction; for example, enzymes can speed up reactions. Enzymes, as a result, can do complex chemical activities at low temperatures. Each enzyme is different however, due to their different and unique amino acid sequences (since enzymes are proteins). These diverse sequences cause the enzymes to take on unique 3-D figures, thus, different

substances will affect the enzymes that have different active sites, affecting the activity of the enzyme. One thing enzymes have in common, however, are their -COOH and -NH2 groups that are ready to lose or gain H+ ions, making them prone to factors such as pH to affect their initial reaction rates. With their amino acid chains and even with their stable -S-S- bonds, enzymes are prone to different factors that can affect the initial reaction rates of enzyme catalyzed reactions. First of all, an initial reaction rate is dependent on the characteristics of a particular enzyme. It will always be the same for any enzyme and its substrate at a given temperature and pH. Temperature is one factor that can affect the initial reaction rate. When temperature is raised, reactions are usually sped up. With a higher temperature, there's more kinetic energy for more reacting molecules to undergo the reaction; so, the more free energy there is, the faster the reaction will go. With the speeding up of the molecules in the reaction, the enzymes are also sped up as well. However, if the temperature optimum is reached, the kinetic energy of the enzyme and water molecules is so great that the enzyme molecules are disrupted. Another factor is the pH. Like earlier stated, the -COOH and-NH2 groups in the enzymes make it so that they're ready to gain or lose H+ ions. So, if the pH is lowered, enzymes tend to gain H+ ions, making it so that eventually, their amino acid chains are disrupted, upsetting the enzyme's shape. The enzyme's shape is also disrupted when the pH is raised, and the enzyme loses the H+ ions. This affects the amino acid chains, and eventually makes the enzyme lose shape. The concentration of the enzyme and substrate can affect the initial reaction rate as well, for if the concentration is too high or too low, the reaction will not take place until that substrate or enzymes is removed or added into the system. I thought that this lab was a good experience. First, I learned many new concepts about enzymes and new lab techniques such as titration. My group worked very well together and even got to meet new people. We also each contributed to the lab. Though only half our group understood titration, we were all very patient with each other and worked hard to help each other out.