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How P H Affects An Enzyme's Ability To Catalyze Honors Biology I Lab Report

943 words - 4 pages

How pH Affects an Enzyme’s Ability to Catalyze
How pH Affects an Enzyme’s Ability to Catalyze
Kayah Takei and Annelise Kofod
Durham Museum of Life and Science
Honors Biology I
The purpose of our lab was to demonstrate how pH affects the productivity of enzymes. In our lab, we tested how changing the pH of our enzyme, lactase, affected its ability to catalyze its substrate, lactose. We tested the enzyme’s ability to function by using glucose test strips to determine if glucose was present. Our results showed no sign of glucose, thus, supporting our hypothesis. These results are important because it shows the environmental sensitivity of the enzyme lactase.
Every enzyme has an active site, the area where a substrate will bind to the enzyme to conduct the chemical reaction. When conditions are ideal, the enzyme should catalyze, or speed up, the reaction. Enzymes are very specific as to what reactions they will catalyze. The active site of every type of enzyme is different, allowing the enzyme to catalyze only one type of substrate. This, in turn, makes the enzyme very specific.
In earlier research, after using several potential substrates and lactase as our enzyme, we measured presence of glucose by using glucose test strips. We found no presence of glucose in anything except for lactose, demonstrating the specificity of enzymes.
In this report, we extend our earlier work by changing the pH to test how changing the environment surrounding the enzyme affected it. Our hypothesis was that changing the pH of the substance would make the lactase unable to catalyze the lactose. The goal of this experiment was to determine if lactase would denature in response to a basic pH. A denatured enzyme would be unable to catalyze its substrate.
We conducted our experiment using sodium hydroxide (NaOH), lactase, and milk. The purpose of the NaOH was to change the pH of the solution. NaOH has a pH of 13, extremely alkalotic, or basic.
We started our control group by adding 1mL of lactase (Lactase Drops, Seeking Health, Bellview, WA) to 2mL of milk (for lactose). We tested our solution for glucose by using a glucose strip (Precision Laboratories, Cottonwood, AZ), then set it aside for five minutes. By adding 1mL of NaOH to 9mL of lactase, we created our experimental group. We took 1mL of the solution and added it to 2mL of milk. Next, we used a glucose strip, as we did with the control group, dipped it into the solution and let it sit for five minutes. After the five minutes was up, we found our results to be negative, with 0mg of glucose present in the solution.
The results from our control group and experimental group were completely different, as we predicted in our hypothesis. Our results from our control group came back positive, indicating that there was glucose...

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