The Effect of pH on AmylaseIntroductionThe Pearson Laboratory Manual (Carter & Morgan, 2014) has defined enzymes as “biologicalcatalysts, compounds that speed up a chemical reaction without being used up or altered in thereaction.” Research has discovered that pH can denature an enzyme and inhibit it from workingproperly when the pH of the environment is different than the pH of the enzyme. An enzyme’soptimum pH is when the enzyme is most active; therefore, it can perform the reaction thequickest (Carmicheal, 2015). Take a look at your own body. Pepsin is an enzyme found in thestomach, a very acidic environment. Whereas amylase is found in the small intestine, a slightlyalkaline environment. These two enzymes have different optimum pH which allows them towork efficiently in their environment without becoming denatured (Parry, 2012). Thisexperiment will test the effects different pH levels have on enzymes, specifically the enzymeAmylase.In this experiment, the enzyme Amylase (derived from saliva) was mixed with different pHlevels and then starch was added. If the pH levels were higher or lower than the pH of Amylase,then the starch would disappear from the solution slowly. If the pH levels were the same as thepH of Amylase, then the starch would disappear from the solution rapidly and the optimum pHcan be determined.Methods and MaterialsTo start the experiment, six test tubes were labeled 1 through 6 and placed in a test tube rack. Foreach test tube, a different buffer solution was added using a 5-mL graduated pipette (5mL of
