Lab Report Part 1 Essay

Part 1 dilutions participated as a trail run to gather around the “full enzyme” that was used for the other parts of the experiment. Part 2 readings were in the time span of 10 minutes and the final results show a spontaneous increase in the first minutes of the absorbance readings. They then showed a steady reading towards the end of timing. The amount of enzyme is decreasing as the dilution occurred. The activity it catalyzes measures the amount of enzyme present in the reaction (Introduction to Enzymes). Part 3 had the similar steps so the rates must have been in a similar range when dealing with dilutions. In this part, it was displayed with the readings and rates that the substrate amount was decreasing. From the use of the formula, the
Part 4 of the experiment had the addition of the inhibitor to see what sort of inhibition it was known as. After doing the steps of the experiment for Part 4, readings led us to determine the reaction rate with the inhibitor and without the inhibitor. Table shown below displays the results of the rates with the percentage inhibition which is calculated by this formula: ([rate without inhibitor – rate with inhibitor] / rate without inhibitor) times 100. Inhibitors are the substances that lower the rate of enzymatic activity;That occurs usually by binding with the enzyme and by the interference with the formation of the ES (Enzyme Kinetics - Factors Influencing Activity). Determined using the information of the table, data was transferred to make a line graph of percent inhibition versus the substrate concentration. Noncompetitive inhibition would have resulted in a different form of linear graph. It shows a constant substrate concentration because there is no competition at the active site, so everything flows in order unlike competitive inhibition. Active sites are more and more occupied that the substrate doesn’t end up sometimes binding to the active