State the purpose of running the peroxidase reaction at different pH levels
Different pH creates different environments for the experiment to take place. The pH creates a reaction rate that is unique from the other pH level used (Ai, Li, Zhang, Fu, & Jiang, 2013). The rate of the enzymes catalyzing the reaction will differ as per pH level.
Bar graph showing the effect of pH on the reaction rate of peroxidase from the data obtained in the laboratory
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Absorbance rate multiplied by 1,000
Ph3 = 4.39
pH 5 = 7.64
pH 5 = 5.66
pH 5 = 0.1
Effect of pH on peroxidase’s ability to catalyze the reaction as evidenced by the results obtained in the lab.
The discussion shall include a quantitative analysis of the data and address these questions:
| Time in (Sec) | pH 3 | pH5 | pH7 | pH10 |
| 0 | 0.0035 | 0.05 | 0.049 | 0.0195 |
| 15 | 0.004 | 0.168 | 0.063 | 0.008 |
| 30 | 0.0035 | 0.2685 | 0.144 | 0.009 |
| 45 | 0.003 | 0.3835 | 0.24 | 0.0085 |
| 60 | 0.003 | 0.4955 | 0.349 | 0.0085 |
| 75 | 0.004 | 0.6595 | 0.4335 | 0.009 |
| 90 | 0.0025 | 0.7205 | 0.498 | 0.009 |
| 105 | 0.003 | 0.8625 | 0.595 | 0.01 |
| 120 | 0.0025 | 0.9355 | 0.706 | 0.0095 |
| 135 | 0.003 | 1.0415 | 0.7685 | 0.0095 |
| 150 | 0.0025 | 1.145 | 0.8685 | 0.0095 |
| 165 | 0.004 | 1.2525 | 0.939 | 0.0095 |
What assumptions did you make when analyzing and interpreting the linear plots obtained?
Using the report from the lab, I assumed that the increase in Peroxidase concentration increases the rate of reaction (Ai, Li, Zhang, Fu, & Jiang, 2013) . The temperature and pH test showed the optimum condition, which is the best for the enzymes to react.
Were the results consistent with what is known about how pH affects protein structure and why peroxidase structure is essential to its function?
The results were mostly consistent only on a few occasions, whereby the test tubes are assumed to be contaminated. The data was uniform all over the experiment; however, the difference only recorded when there was a difference in the temperature. Peroxidase structure is a beneficial enzyme for the test because they are more like pulleys, which makes work more comfortable in a cell during the reaction process (Jiang, et al., 2013) . They cause different specific changes in their chemical structure equally when they are mixed with other chemicals. Precisely, Peroxidase, as a result of the metabolic reaction, they can remove the Hydrogen peroxide from the cells. Therefore, the unique nature of Peroxidase makes it the best for the experiment conducted.
Was your hypothesis regarding the effect of pH falsified or supported?
The results collected from the lab supported the hypothesis that was stated at the beginning of the experiment. Peroxidase worked best at a pH of 7 and below (Ai, Li, Zhang, Fu, & Jiang, 2013) . The consistency in the results recorded confirmed how the test was practical and proved the hypothesis.
Given the results you obtained, what do you think the results would look like if
More pH levels were tested (rather than just four)
The rate of the reaction will continue to increase when the pH level kept rising.
Peroxidase was extracted from potatoes instead of turnips
Potatoes have a live cell that has different concentration. The Peroxidase from potatoes will increase the rate of reaction compared to that of turnips (Ai, Li, Zhang, Fu, & Jiang, 2013) .
Given the results you obtained, how can you improve this experiment to obtain additional relevant data?
As I was experimenting, I realize that there are ways that we could experiment with making the results more reliable and authentic. First, we could have used a different inhibitor rather than guaiacol. Guaiacol is good for testing the acid in a cell (Ai, Li, Zhang, Fu, & Jiang, 2013) . The inhibitor is the real pH that the enzyme has. We could have also used potatoes, which are more natural and have a live cell.
Reference
Ai, L., Li, L., Zhang, C., Fu, J., & Jiang, J. (2013). MIL ‐ 53 (Fe): A Metal-Organic Framework with Intrinsic Peroxidase ‐ Like Catalytic Activity for Colorimetric Biosensing. Chemistry–A European Journal, 19 (45), 15105-15108.
