Abstract In this laboratory exercise, studies of enzyme catalase, which accelerates the breakdown of hydrogen peroxide into water and oxygen. The purpose was to isolate catalase from starch and measure the rate of activity under different conditions. The laboratory was also conducted in association with a second laboratory that measured the effects of an inhibitor on the enzymes.
Changes in temperature and pH along with Substrate Concentration and Enzyme Concentration were the conditions tested in the experiment.
Four AP Biology classes performed this experiment and the data presented in this report will reflect the averages of said classes. In the later discussion sections, it will become very obvious that human error was the deciding factor in the data collection.
Introduction Enzymes are biological catalysts that carry out thousands of chemical reactions that occur in living cells. Generally large proteins, enzymes are made up of several hundred amino acids, and often contain a non-proteinaceuos group essential in the actual catalyst. When an enzyme can on longer function at all, it is said to be denatured. There are several factors that contribute to the denaturing of the enzyme that also determine the enzyme's shape. These factors are very closely regulated in both living organisms and in laboratory environments, so as to achieve optimum enzyme activity. Temperature of the enzymatic reaction or enzyme itself will help in dictating the activity rate of the function. Likewise is true of the enzymatic reaction's pH. The other factors include the Substrate Concentration (a substrate is the substance being acted upon) and Enzyme Concentration. The AP Biology classes performed this study, to examine the effects of changes in the optimum conditions for enzyme activity.
A disc of filter paper was immersed into the enzyme solution for about 15 seconds. Then it was removed from the solution