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 enzyme
concentration. For a given enzyme concentration, the rate of an enzyme reaction increases with
increasing substrate concentration. Increasing the amount of enzyme also increases the frequency of
with which the enzyme and substrate collide. As a result enzyme-substrate complexes form more
quickly and the rate of reaction increases. However, there is a limit as eventually there will be more
enzyme molecules that substrate. Some enzymes become virtually useless at that point as they
won't have any substrate to bind. Any further increase in enzyme concentration has no further
effect on the reaction rate.It is important to note that the reaction observed was for the respiration
of yeast:

Starch Maltose

Starch + Iodine Starch/Iodine complex

Trend:

I didn’t include a trend yet because I don’t have the results on me at the moment. So can you just
check the rest. Thank you

This experiment can be improved by using a wider range of concentrations, larger amounts of
enzyme and substrate measured with more accurate instruments such as a pipette and attempt to
hold all other factors affecting enzyme activity constant. In this way we can more accurately
observed the trend between enzyme concentration and enzyme activity.