Enzymes function as highly efficient biocatalysts which lowers the amount of energy needed for

a reaction to occur. However, there are only specific conditions where enzymes can work best and above
or below this optimum condition, the activity of the enzyme would reduce or would even result to
denaturation, leaving the enzyme unfunctional. To observe the activity of the enzymes when exposed to
different conditions, this experiment is conducted. Specifically, this experiment aimed to investigate the
presence of catalase in potato and observe the action of this particular enzyme when exposed to varying
temperature and pH conditions. Catalase is a key enzyme which uses hydrogen peroxide as its substrate
and is responsible for neutralization through decomposition of hydrogen peroxide. The reaction of
catalase with the hydrogen peroxide is indicated by the formation of bubbles minutes after the H2O2 is
applied. As reflected in the results of the study, the amount of bubbles formed vary between each
container. On the first set-up which investigates the effect of temperature to the action of catalase, it was
demonstrated that heating the potato pulp ceases the action of the catalase as no bubbles were observed to
form in the glass container. Heating the enzyme at high temperature causes the protein composing it to be
denatured and leaving the enzyme unfunctional. At very low temperature, the enzyme was also observed
to reduce its activity because only few bubbles were observed to form in the glass container, indicating
that exposing the enzyme at very low temperature causes its activity to slow down. On one hand, the glass
container exposed at room temperature had the highest amount of bubbles to form, indicating that the
enzyme catalase works best in this condition. On the second set-up which investigates the effect of pH
condition in the action of catalase, it was shown that catalase works best at neutral pH, and least, in acidic
environment. Very few bubbles were formed in the glass container treated with muriatic acid indicating
that type of environment is not favorable to the activity of the enzyme. On one hand, the container treated
with bleach formed few bubbles after the application of hydrogen peroxide, indicating that strongly basic
environment also slows down the activity of the enzyme. The container treated with water had the
highest amount of bubbles to form which indicates that the enzyme works best at neutral pH. Based on
the results of the study, the hypotheses formulated prior the conduct of the experiment were accepted.
However, it was also important to consider that certain limitations were observed during the conduct of
the activity based on the fact that the potato pulp is vulnerable to oxidation especially when transferring it
to the glass containers. Overall, the experiment especially the results are significant in adding to the
existing body of knowledge about the activities of enzyme catalase and different agents or conditions that
can cause the reduction and acceleration of enzymes’ activities. The methods and experimental design of
the experiment are repeatable to allow further studies and discussion about the topic.