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Unformatted text preview: LAB 2 NOTE: These labs are known for high failure rates. Therefore, if I show an example using data, a graph, etc yours may be totally different depending upon mine and yours success with the lab. So dont freak if your data is completely different from mine. And therefore the analysis of results sometimes may need to be answered differently since you base your analysis off your data and not mine. DISCLAMIER: DO NOT CHEAT! Introduction Enzymes are proteins produced by living cells that act as catalysts, which affect the rate of a biochemical reaction. They allow these complex biochemical reactions to occur at a relatively low temperature and with less energy usage. In enzyme-catalyzed reactions, a substrate, the substance to be acted upon, binds to the active site on an enzyme to form the desired product. Each active site on the enzyme is unique to the substrate it will bind with causing each to have an individual three- dimensional structure. This reaction is reversible and is shown as following: E + S----ES---- E + P Enzymes are recyclable and unchanged during the reaction. The active site is the only part of the enzyme that reacts with the substrate. However, its unique protein structure under certain circumstances can easily be denatured. Some of the factors that affect enzyme reactions are salt concentration, pH, temperature, substrate and product concentration, and activators and inhibitors. Enzymes require a very specific environment to be affective. Salt concentration must be in an intermediate concentration. If the salt concentration is too low, the enzyme side chains will attract each other and form an inactive precipitate. Likewise, if the salt concentration is too high, the enzyme reaction is blocked by the salt ions. The optimum pH for an enzyme-catalyzed reaction is neutral (7 on the pH scale). If the pH rises and becomes basic, the enzyme begins losing its H+ ions, and if it becomes too acidic, the enzyme gains H+ ions. Both of these conditions denature the enzyme and cause its active site to change shape. Enzymes also have a temperature optimum, which is obtained when the enzyme is working at its fastest, and if raised any further, the enzyme would denature. For substrate and product concentrations, enzymes follow the law of mass action, which says that the direction of a reaction is directly dependent on the concentration. Activators make active sites better fit a substrate causing the reaction rate to increase. Inhibitors bind with the enzymes active site and block the substrate from bonding causing the reaction to subside. The enzyme in this lab is catalase, which produced by living organisms to prevent the accumulation of toxic hydrogen peroxide. Hydrogen peroxide decomposes to form water and oxygen as in the following equation: 2H 2 O 2 2H 2 O + O 2 This reaction occurs spontaneously without catalase, but the enzyme speeds the reaction considerably. This lab's purpose is to prove that catalase does speed the decomposition of considerably....
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- Spring '08