If any of the liquid in the Epp tubes were brown after the addition of the solutions, the appropriate response was to start over, as well as if the amount of fluid in each tube varied. However, this experiment did not experience either of these results, so the next step was to let the tubes set for five minutes, as the enzyme had to have time to be reduced by the hydrogen peroxide (Doebel, p. 64, 2015).
Transferring the liquid from the B Epp tube and the A Epp tube into a cuvette came next, and had to be done using clean plastic pipetes each time. The fluid had to mixed well, so the process was to hold the opening of the cuvette closed and shake the tube up and down a few times. Then, the sides of the cuvette were wiped with the tissue and inserted into the spectrophotometer. This was done first using the Blank cuvette to set the standard between runs. Timing was critical for the remaining tubes, as once the Tubes A and …show more content…
These were then taken out, mixed into individual cuvettes after five minutes, and recorded for absorbance every twenty seconds in the spectrophotometer.

Results:
The data measured in Experiment One was interpreted to form a Michaelis-Menten plot and a Lineweaver Burk Plot. These plots were collected by first finding the velocities of the enzyme reaction of each tube, which is the slope of each tube’s equation. As seen in Figure 1 below, each Tube has it’s own equation, and it shows the relative absorbance of each substrate concentration related to the time of the experiment. Figure 1. The Effect of Time on Absorbance. The velocity of each stock solution was found to measure the rate of the enzyme reaction. It is shown that there is a positive relationship between the time of the experiment and the rate of