The Effect of Ph on Beef Liver Catalase Activity Measured by the Change in Temperature

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Katrinka Strickland Lab Partners: Fatima Asad , Sara Merz SL Biology Internal Assessment P.d. 2 12/12/13 The effect of pH on beef liver catalase activity measured by the change in temperature Background Information: This experiment will examine how the effect of pH on enzyme activity is measured by the difference in temperature. After doing research on beef liver, it was discovered that the optimum of the pH is 6.5 and the enzyme present is catalase. Catalase catalyzes the breakdown of hydrogen peroxide to water and oxygen. The pH affects the amino acids in the enzyme. This can alter the shape of an enzyme because the ionization of the amino acids is altered (Danson, 2010). In some cases, when the pH becomes very low or high, this shape change becomes irreversible; this is called denaturation. Changes in the pH or acidity of the environment can take place. This change in the pH will affect the polar and non-polar intramolcular attractive forces (Nishiur, 2012). If the environment is too basic the acid groups would be deprotonated. There are two established thermal properties of enzymes that affect the catalytic rate. Those two are activation energy and their thermal stability. Problem: What is the effect of pH on beef liver catalase activity when it is measured by the change in temperature? The pH will be measured using a pH probe; and the temperatures will be measured using four temperature probes. Hypothesis: It is hypothesized that if the pH of the beef liver catalase solution is adjusted from its initial pH with the use of an acid or base, then a temperature difference will occur within the beef liver catalase solution. This is predicted because pervious experiments have shown that an increase in temperature may also lead to an increase in the number of ions in solution due to the dissociation of molecules. Since pH is a measure of the hydrogen ion
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