Tube 2 Lab Report

Figure 1 shows the average amount of absorbance for each tube, containing different levels of pH. Tube 2 had an acidic pH level, Tube 3 had a neutral pH level, and Tube 4 had a basic pH level. It is indicated that the absorbance rates were the highest for the neutral pH level, with a final absorbance rate of 0.166. This was followed by a basic pH (0.106). The acidic pH level had the least amount of absorbance with a final absorbance rate of 0.069. This reinforces the idea that the ALP enzyme worked best under conditions with a neutral pH and worked the least in an acidic pH environment.

Figure 2 shows the average enzymatic activity for each different pH level. Enzymatic activity was found by taking the range of absorbance divided by the range
of time. It can be indicated that the neutral pH level had the highest rate of enzymatic activity at 1.37 E-04, followed by the basic pH (6.17 E-05). The acidic pH level had the lowest enzymatic activity, with a rate of 5.83 E-06. Thus, it can be said that the ALP enzyme has an optimal pH level at a neutral pH and works the least within an acidic pH level.

Figure 3 shows the average amount of absorbance for the different enzyme concentrations.
As indicated by the figure, the high concentration correlated to having the highest amount of absorbance (1.006 at 300 seconds). This was followed by the medium-high concentration (0.555) and medium concentration (0.540). It can be noted that the medium concentration started off with a higher absorbance than the medium-high concentration, but the medium-high concentration had a faster increase of absorbance over time. Thus, surpassing the absorbance of the medium concentration from 270 and 300 seconds. The low concentration had the lowest amount of absorbance, with a final absorbance rate of 0.204, and did not substantially increase over the period of
time.

Figure 4 shows the average enzymatic activity regarding different enzyme concentrations. It’s indicated that the low concentration had the lowest reaction rate of 2.88 E-04. The high concentration had the highest reaction rate of 2.02 E-03, and this was followed by the medium-high concentration (1.13 E-03), and then the medium concentration (6.43 E-04). It can be implied that as the concentration increases, the rate of the reaction increases as well.

Figure 5 shows the absorption rates for the different temperatures on the enzyme reactions.
Four different temperatures were observed, including 4°C, 20°C, 32°C, and 60°C. It can be indicated that the temperature of 60°C had the highest absorbance rates (0.326 at the final time), followed by 32°C (0.179), and 4°C (0.142). With regard to 32°C and 4°C, it is noted that the tube that was 4°C initially had higher rates than the 32°C tube. Over time, the 32°C tube increased while the 4°C tube decreased, so at the end of 300 seconds, the 32°C tube had the higher absorbance rates. The 20°C tube had the lowest amount of absorbance with an absorbance rate of 0.126. Thus, it can be implied that the optimal temperature was 60°C, since it had the highest levels of
absorbance.

Figure 6 shows the enzymatic activity of the reactions for the varying temperatures. It’s indicated that the optimal temperature for the enzyme was 60°C, since it had the highest reaction rate of 5.07 E-04. This is followed by 32°C (2.18 E-04), and then 20°C (1.18 E-04). The temperature with the lowest rate of reaction was 4°C, with a rate of 3.25 E-05. As implied by the figure, as the temperature increases, the rate of the reaction increases as well.