Discussion: The cells of living organisms are the site of metabolic reactions.

These reactions do
not occur by spontaneous means. They occur by catalysis. Catalysis is defined as the acceleration
of a chemical reaction by some substance which itself undergoes no permanent chemical change.
The catalysts of biochemical reactions are enzymes and are responsible for bringing about almost
all of the chemical reactions in living organisms. Without enzymes, these reactions take place at
a rate far too slow for the pace of metabolism. Enzymes are able to catalyze reactions by binding
to substrates, forming enzyme-substrate complexes, after which it converts them into products.
There are several factors that affect enzyme activity. These include enzyme concentration,
substrate concentration, temperature and pH. The pH is the factor of interest in this experiment.
Enzymes are very specific. They have a pH at which maximum rate is achieved, this is referred
to as the optimum pH. Extremely high or low pH values generally result in complete loss of
activity for most enzymes. pH is also a factor in the stability of enzymes. As with activity, for
each enzyme there is also a region of pH optimal stability. In addition to these factors there are
other factors, such as ionic strength, which can affect the enzymatic reaction. Each of these
physical and chemical parameters must be considered and optimized in order for an enzymatic
reaction to be accurate and reproducible. In this experiment the effect of pH on catalase activity
in potato was assessed using hydrogen peroxide, under neutral, very acidic and very basic
conditions. The foam height was used as an indication of enzyme activity.

The results obtained in the experiment showed that the sample in the distilled water gave the
highest average foam height of 72.5mm whereas, the sample in the lime water gave the lowest
foam height of 42.5mm, and those in the vinegar was in the middle with an average foam height
of 50mm. Potatoes have a pH of about 6.1, this means that the optimum pH is about 6.1. Based
on this knowledge it was expected that the sample placed in distilled water would have the
highest foam height. This is because the pH of distilled water is 7; this is relatively close to the
optimum pH of the enzyme. Therefore the active site would not be affected much by this slight
change in pH. However, the pH of the vinegar used was 2; this pH is very far below the optimum
pH and as a result the foam height was very low. At the optimum pH the enzyme is in its most
stable form. This means that the enzyme was almost completely denatured at pH 2. The fact that
enzymes are protein and proteins are made up of amino acids; these amino acids are known
Zwitterions- they have an acidic group (carboxyl group COOH) and a basic group (amino group-
NH2) attached to the alpha-carbon. This means that depending on the pH of the solution, H+ ions
would either be lost or gained. In acidic conditions the NH2 group ionizes to NH3+ and in basic
conditions the COOH group ionizes to COO-. This loss and gain of H+ ions interrupts the
hydrogen bonds and weak ionic interactions that keeps the tertiary structure of amino acid
together and the specific shape of the active site. The more acidic or basic the solution is the
greater the degree of disruption. Since enzymes are specific, these changes will distort the active
site of the enzyme. Eventually the active site will be completely changed and substrate will no
longer be able to bind to the active site. At this point the enzyme will be completely denatured.
For this reason the foam height in the distilled water was the highest and those in the very acidic
and basic conditions were low as the enzyme was almost completely denatured.
Conclusion: Above and below the optimum pH there was a decline in the rate of the enzyme
catalyzed reaction. The highest enzyme activity was obtained under neutral conditions. Under
very acidic and very basic conditions little enzyme activity was observed.