Amyylase: Lab Experiment: Exploring Enzyme

2004 Words 9 Pages
Exploring Enzymes
Dmitri N. Piquero
Biological Discovery I Laboratory
Section I Abstract
Amylase is an enzyme that speeds up the conversion rate from starch to glucose. Four test tubes were filled with a starch solution and a different concentration of amylase solution ranging from 0 μL to 1000 μL. The test tubes were then left to soak in a 37°C water bath before having 2 mL of 1 M hydrochloric acid added to a test tube of pure amylase solution. Lugol’s iodine was used to test for the existence of starch in the samples, while Benedict’s reagent detected any broken-down glucose. The same procedures were then performed waiting 5, 10, and 15 minutes before deactivating the amylase. Then again repeating the procedures with 4°C and 95°C
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Through experimentation at varying temperatures and pH levels, both were found to have greatly impacted the activity of the enzyme.
When the temperature was too low, at around 0°C, the enzyme did not react at all. At 37°C, the enzyme acted the most strongly, which is consistent with given knowledge that this enzyme acts most optimally at around human body temperature. This is supports the hypothesis that enzymes like amylase have a comfort zone, and upon leaving that range, the enzyme fails to function (Cano 1997).
The pH test showed that the enzyme appeared to function better at lower pH levels. As the pH increased, the reaction gained intensity up until the well with a buffer of pH 8, where the color of the well was a lighter orange than its earlier neighbors. While amylase did function at other levels, the enzyme functioned the most optimally as the pH decreased to around 5 or 6, garnering a darker orange color than its neighboring wells. This further supports the hypothesis, adding that amylase’s optimum pH lies at around 6 (Corporation
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Future experimentation might test different temperature ranges, and deduce at what time amylase’s reaction velocity peaks. Further tests might also reveal what other factors play into amylase or other enzyme’s reactivity. Works Cited
Benedict, S. R. (1909). A reagent for the detection of reducing sugars. Journal of Biological Chemistry, 5(5), 485-487.
Cano, M. P., Hernandez, A., & Ancos, B. (1997). High pressure and temperature effects on enzyme inactivation in strawberry and orange products. Journal of Food Science, 62(1), 85-88.
Corporation, W. B., & Diagnostics, W. (1972). Manual of clinical enzyme measurements Worthington Diagnostics.
Hovenkamp-Hermelink, J. H. M., Jansen, G., & Flamme, W. (2000). Tuber and starch quality of wild and cultivated potato species and cultivars. American Journal of Potato Research, 44(2001),

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