An enzyme is a globular protein produced by a living organism which acts as a catalyst to bring about

a specific biochemical reaction. These changes would most likely denature protein and kill the
organism. Enzymes are important because in their absence reactions in the cell would be too slow to
sustain life. An enzyme works by providing an alternate pathway of lower activation energy ( the
minimum energy required to start a chemical reaction)for a reaction to occur. Factors affecting
enzyme activity include temperature, pH, enzyme concentration, substrate concentration, and the
presence of an inhibitor.

An enzyme has an active site to which a substrate bonds in order to form a short lived enzyme/
substrate complex which can then decompose into the an enzyme/product complex, at this stage
the product is released from the enzyme. This results in the enzyme being unchanged while products
are formed. An enzyme is very specific and has an active site which is adapted for a specifically
shaped molecule. A suggested hypothesis on how this mechanism works is by a postulate of Emil
Fischer called the ‘lock and key’ hypothesis and its adaptation by Daniel Koshland called the
‘induced fit’ hypothesis. The lock and key hypothesis uses the analogy that the lock is the enzyme
and the key is the substrate. Only the correctly shaped key(substrate) fits into the key hole (active
site) of the lock (enzyme).The induced-fit hypothesis proposed the mechanism of interaction
between an enzyme and a substrate. It states that exposure of an enzyme to a substrate causes the
active site of the enzyme to change shape in order to allow the enzyme and substrate to bind and in
some rarer cases the substrate may change slightly in shape to fit into the enzyme.

In the case of this experiment the factor affecting enzyme activity observed was that of substrate
concentration. Increasing substrate concentration increases the frequency with which the enzyme
and substrate collide. As a result enzyme-substrate complexes form more quickly and the rate of
reaction increases. Eventually, as substrate concentration increases there is a point when any
further increase in substrate concentration produces no significant change in reaction rate.This is
because of high substrate concentrations the active site of the enzyme molecules at any given
moment are virtually saturated with substrate. Thus any extra substrate has to wait until the
enzyme/substrate complex has released the products before it may itself enter the active site of the
enzyme.It is important to note that the reaction observed was for the respiration of yeast:

2H202 2H2O + O2

The enzyme catalase is found in potato. The experiments were all carried out over a 5 minute
period. From the table we can see as the solution contained 20 vol. Of H202 the maximum number
of bubbles was obtained (30 bubbles). As the volume of H202 decreased to 10 there was a decrease
in the number of bubbles (16 bubbles). This was also seen when the vol. Of H202 was decrease to 5
there was a decrease in the number of bubbles produced (10 bubbles). These observations can be
explained by the decrease in concentration of substrate (H2O2) from 20 to 10 or 5 as there is a
decrease in the frequency of collisions between substrate and catalyst (catalase) resulting in a lower
rate of reaction.Finally when there was no H202 in the solution there was no reaction occurring
denoted by the fact that there was 0 bubbles produced. This is because without a substrate there is
nothing for the catalase to act on to form products and so no reaction would occur, this is, rate of
reaction would be 0. Upon plotting the graph of vol. Of H202 against number of bubbles produced it
was noticed by extrapolating the graph we can obtain the number of bubbles produced for any vol.
Of H202. By calculating the gradient of the graph we can obtain the change in vol. Of H202 with
respect to the number of bubbles produced. This value (0.75) was positive and so as vol. of H202
increased so does the number of bubbles produced indicating proportionality of between the two
variables.
This experiment can be improved by collecting and measuring the volume of gas evolved using an
inverted measuring cylinder in a trough both filled with water while attempting to keep all other
factors affecting enzyme activity constant. In this way the volume of gas evolved can be obtained
which can be used to more accurately observed the trend between substrate concentration and
enzyme activity.