Monitoring How Ph Affects the Rate of Reactions of Barley Amylase Essay Example

the focal point. By testing the enzyme's capability to hydrolyze starch under different pH conditions (pH 4-7) and comparing the results to a control solution lacking the enzyme, the impact of pH on enzyme activity is examined. Our hypothesis, my lab group and I, is that a decrease in pH will concurrently decrease enzyme activity.

According to Klein (2004), the enzyme's highest activity occurs at a pH level that is neither acidic nor basic. This claim is supported by information from the Worthington Biochemical Corporation (Worthington 2008). To investigate how pH affects enzyme activity, we employed a spectrophotometer to measure the absorbance of different enzyme concentrations in solutions with increasing pH levels at specific time intervals. By doing this, we were able to determine the product concentration and calculate the enzyme activity through comparison with a standardized curve. Our experiment started by creating a standard curve using the following procedure:

Prepare six test tubes according to the instructions provided in the table below. Then, cover the tubes with parafilm and shake them vigorously. Prior to inserting a test tube into the spectrophotometer, make sure to remove the parafilm. Utilize the spectrophotometer to measure the absorbance at a wavelength of 580 nm, using the first tube as a reference.

(Do not discard “blank” tube until the experiment is finished). Plot the absorbance at 580 nm on graph paper.

Results

The results indicate that the hydrolysis reaction between starch and amylase enzyme exhibited a higher rate in neutral pH solutions. The reaction between amylase and starch results in the separation of the disaccharide maltose. As the reaction continues, the amount of starch decreases while the amount of maltose (sugar) increases.

(Bernfield 151) The

activity of amylase in the laboratory was observed by using iodine, as iodine reacts with starch to form a purple color. As amylase breaks down starch, less starch is present, causing the solution's color to become lighter. Our group's hypothesis was supported by the experiment's observations. The test tubes with more neutral pH solutions had higher absorbencies, indicating a higher rate of reaction. This supports our hypothesis that decreasing the solution's pH and increasing acidity increases the likelihood of enzyme denaturation (Worthington 2008). Enzymes can easily be denatured by various forces, such as chemical, ionic, and kinetic factors.

The enzyme demonstrates high activity in acidic or nearly neutral conditions, with over 50% of activity occurring between pH 4.6 and 6.8. The enzyme's optimal pH is 6.0, suggesting a preference for a slightly acidic environment (Bernfield 154).
Tables and Figures:
X Axis - Time (minutes)
Y Axis - Absorbance (580nm)
pH = 5
Time (min) 0 2 4
Absorbance (580 nm) 0.

7930.

References

1. Division of Biological Sciences, The University of Georgia, Laboratory Manual For Principles of Biology I, 2007
2. Holum, J. Elements of General and Biological Chemistry, 2nd ed., 377, Wiley, NY (1968).
3. Klein, S. : Barley Amylase, http://www.chem.uwec.edu/Webpapers2005/leee/barley.html, University of Wisconsin, (2004)
4. Kimball, J. : Enzyme Kinetics, http://users.

The following text contains and their contents, which should beand unified:

rcn.com/jkimball.ma.ultranet/BiologyPages/E/EnzymeKinetics.html, Harvard College, (2003)

• Worthington Biochemical Corporation: Effects of pH (Introduction to Enzymes), Lakewood, NJ, 2008
• Bernfeld, P., 1955.
• Amylase a and b.Methods in Enzymology.

1, 149-151.