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What reaction was catalyzed by salivary amylase?

What reaction was catalyzed by salivary amylase?

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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What reaction was catalyzed by salivary amylase?
Part 1. Effect of pH The pH of an enzyme's environment can affect its activity by interfering with the charge on its amino acids. Small changes in pH can result in enzyme denaturation and subsequent loss of catalytic activity. Each enzyme has a characteristic optimum pH which usually falls within the physiological pH range. Note that for the purpose of this experiment, distilled water has a pH of -7.00. Watch this video and answer the related questions in the questions section of this activity. The experiment in the video follows this procedure: 1. Prepare a water bath maintained at 37°C. 2. Mix the components shown in the table below: Test Tube 1% Starch 0.2M NacI Acid/ Base/ Water Salivary Solution Amylase A 10 mL 0.5 mL 1 mL 0.05 M HCI 2 mL В 10 mL 0.5 mL 1 mL distilled water 2 mL C 10 mL 0.5 mL 1 mL 0.05M NaOH 2 ml 3. Place the test tubes in a water bath. 4. Prepare a spot plate that contains two drops of I, in KI. 5. When the temperature of the test tube contents is 37°C, remove a few drops from the test tubes and place them in the corresponding spot plates. 6. Withdraw another two drops every two minutes until a spot shows no color change. Part 2. Effect of Temperature As the temperature of an enzymatically catalyzed reaction increases, so does the speed of the reaction. However, when the temperature goes beyond a certain point, it causes adverse effects on the enzyme's tertiary structure. As a result, enzyme activity slows down. The temperature that allows peak enzyme activity is known as the optimum temperature for that enzyme. Watch this video and answer the related questions in the questions section of this activity. The experiment in the video follows this procedure: 1. Based on the results from part 1, choose the mixture that showed high amylase activity. 2. Mix the components of this mixture in a different test tube except for the salivary amylase which should be placed in a separate, smaller test tube. 3. Let the two test tubes equilibrate in a water bath maintained at 4°C for 10 minutes. 4. After 10 minutes, mix the salivary amylase with the other components. 5. Prepare a spot plate with 9 of its wells containing two drops of I, in Kl each. 6. Remove a few drops from the test tubes and place them in the corresponding spot plate. 7. Withdraw another two drops every two minutes until all wells with I, in Kl are filled. Repeat the same process but at 37°C and in 70°C.
Transcribed Image Text:Part 1. Effect of pH The pH of an enzyme's environment can affect its activity by interfering with the charge on its amino acids. Small changes in pH can result in enzyme denaturation and subsequent loss of catalytic activity. Each enzyme has a characteristic optimum pH which usually falls within the physiological pH range. Note that for the purpose of this experiment, distilled water has a pH of -7.00. Watch this video and answer the related questions in the questions section of this activity. The experiment in the video follows this procedure: 1. Prepare a water bath maintained at 37°C. 2. Mix the components shown in the table below: Test Tube 1% Starch 0.2M NacI Acid/ Base/ Water Salivary Solution Amylase A 10 mL 0.5 mL 1 mL 0.05 M HCI 2 mL В 10 mL 0.5 mL 1 mL distilled water 2 mL C 10 mL 0.5 mL 1 mL 0.05M NaOH 2 ml 3. Place the test tubes in a water bath. 4. Prepare a spot plate that contains two drops of I, in KI. 5. When the temperature of the test tube contents is 37°C, remove a few drops from the test tubes and place them in the corresponding spot plates. 6. Withdraw another two drops every two minutes until a spot shows no color change. Part 2. Effect of Temperature As the temperature of an enzymatically catalyzed reaction increases, so does the speed of the reaction. However, when the temperature goes beyond a certain point, it causes adverse effects on the enzyme's tertiary structure. As a result, enzyme activity slows down. The temperature that allows peak enzyme activity is known as the optimum temperature for that enzyme. Watch this video and answer the related questions in the questions section of this activity. The experiment in the video follows this procedure: 1. Based on the results from part 1, choose the mixture that showed high amylase activity. 2. Mix the components of this mixture in a different test tube except for the salivary amylase which should be placed in a separate, smaller test tube. 3. Let the two test tubes equilibrate in a water bath maintained at 4°C for 10 minutes. 4. After 10 minutes, mix the salivary amylase with the other components. 5. Prepare a spot plate with 9 of its wells containing two drops of I, in Kl each. 6. Remove a few drops from the test tubes and place them in the corresponding spot plate. 7. Withdraw another two drops every two minutes until all wells with I, in Kl are filled. Repeat the same process but at 37°C and in 70°C.
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