RP 1 Enzyme
RP 1 Enzyme
Enzymes are biological catalysts that speed up reactions by lowering the activation energy
required for reactions to proceed. Trypsin is a protease enzyme that breaks down proteins into
smaller peptides. The rate of enzyme-catalysed reactions is influenced by several factors,
including temperature. This experiment investigates how temperature affects the activity of
trypsin by monitoring the break down the substrate under different temperature conditions.
By measuring the time taken for the solution to become transparent (indicating the
breakdown of protein), we can assess how temperature influences enzyme activity. Trypsin
hydrolyses the casein protein (found in milk).
Method
Important Considerations
Maintaining accurate temperature control in water baths is crucial to ensure reliable results.
Timing should start as soon as trypsin is added to casein and stop when the solution turns
clear, so consistency in timing is critical.
Analysis
The graph shows an initial increase in the rate of reaction as temperature rises from 20°C to
around 40°C, indicating that the enzyme activity increases with temperature due to increased
molecular collisions, due to more kinetic energy. At around 40°C, the rate of reaction peaks,
suggesting this is the optimum temperature for trypsin activity. Beyond 40°C, the rate of
reaction decreases, indicating enzyme denaturation at higher temperatures, where the
enzyme loses its functional shape due to the breaking of bonds in its tertiary structure.
Validity of Results
The results generally follow the expected trend, but a few data points, particularly at extreme
temperatures, could be improved with more precise temperature regulation and timing.
Repeating the experiment multiple times would provide more reliable averages and reduce the
impact of outliers/anomalies.
A pH buffered milk solution was used to ensure results were unaffected by the pH and that
temperature was the only independent variable in the experiment.
The solution was also left in a water bath for 5 minutes to equilibrate, ensure temperature was
equal throughout.
However, the validity of results could have been improved by maintaining a constant water
bath temperature by wrapping the beaker in an insulator, so heat is not dissipated to the
surroundings.
By extending the range of conditions tested, you could gather more comprehensive data to
deepen your understanding of how enzymes function under varying conditions.