Bio Amylase Lab Manual Answers
195 Effect of Different Temperatures on the Activity of Salivary Amylase on Starch Materials Required Three series of test tubes having iodine solution in each, test tubes, ice cubes, water, 15 ml 1% starch solution + 3 ml 1% NaCl, saliva solution, droppers, thermometer, Bunsen burner and wire gauze. Real Lab Procedure. Take beaker containing 15 ml of 1% starch solution + 3 ml of 1% NaCl solution. Divide and pour this solution into three test tubes and mark them as A, B and C. Maintain the temperature of the beaker containing ice cubes at 5°C. Take beaker containing ice cubes and keep it on the table. Take another two beakers containing water and heat over the Bunsen burner.
Now transfer experimental tube A into a beaker containing ice. Transfer the second experimental tube B into water bath set at 37°C and third experimental tube C into the beaker maintained at 50°C. Using a dropper, take 1 ml saliva solution and transfer the solution into test tube A. Similarly, add 1 ml saliva solution into test tube B and test tube C. Immediately, using a dropper, take few drops from experimental tube A and transfer this into first series of test tubes having iodine solution. Similarly, using fresh droppers, do the same procedure for test tube B and test tube C and transfer the solution into second and third series of test tubes having iodine solution. Note this time as zero minute reading.
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After an interval of 2 minutes, again take a few drops from each tube and add to the iodine tubes and note the change in colour of iodine. Keep on repeating the experiment at an interval of every 2 minutes till colour of iodine does not change. Results It takes less time to reach achromic point at 37°C, as the enzyme is maximum active at this temperature, while at higher and lower temperatures more time is taken to reach the achromic point. Conclusion All enzymes are proteinaceous in nature. At lower temperatures, the enzyme salivary amylase is deactivated and at higher temperatures, the enzyme is denaturated. Therefore, more time will be taken by enzyme to digest the starch at lower and higher temperatures.
At 37° C, the enzyme is most active, hence, takes less time to digest the starch. Effect of Different pH on the Activity of Salivary Amylase on Starch Materials Required Three series of test tubes having iodine solution in each, test tubes, pH tablets of 5, 6.8 and 8, beaker containing water with thermometer, 15 ml 1% starch solution + 3 ml 1% NaCl, saliva solution, droppers, Bunsen burner and wire gauze. Real Lab Procedure.
Take a beaker containing 15 ml of 1% starch solution + 3 ml of 1% NaCl solution. Divide and pour this solution into three test tubes and mark them as A, B and C. Add pH tablet 5 into test tube A, pH tablet 6.8 into test tube B and pH tablet 8 into test tube C. Now transfer experimental tube A, B and C into a beaker containing water and a thermometer for recording temperature.
Temperature of this beaker is to be maintained at 37°C. Using a dropper, take 3 ml saliva solution and add 1 ml of solution to each of the three test tubes. Immediately using a dropper, take few drops from experimental tube A and transfer this into the first series of test tubes having iodine solution. Similarly, do the same procedure for test tube B and test tube C and transfer the solution into second and third series of test tubes having iodine solution. Note this time as zero minute reading. After an interval of 2 minutes, again take a drop from each tube and add to the iodine tubes and note the change in colour of iodine.
Keep on repeating the experiment at an interval of every 2 minutes till colour of iodine does not change. Results pH 5 is acidic and pH 8 is alkaline, therefore salivary amylase did not act in these tubes. Whereas, the enzyme acted in the tube with pH 6.8 (i.e., slightly acidic) and digested the starch. Simulator Procedure (as performed through the Online Labs). You can select the type of test from the ‘Select the test:’ drop down list (Temperature Test and pH Test).
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You can select the temperature from the ‘Select the temperature:’ drop down list or pH from the ‘Select the pH’ drop down list. Click and drag the dropper from the saliva solution bottle and move it into the test tube containing starch solution to drop the saliva solution into it.
Click and drag the dropper from the stand and move into the solution in the test tube containing starch and saliva solution to collect the sample. Still holding the dropper, move it towards test tube that contains iodine solution to drop the mixture into it. Consider time adding as zero minute reading. Reading will show below the test tube.
After an interval of time, again take a drop from the solution and pour into the next test tube containing iodine solution. Note the change in colour of iodine. Keep on repeating the procedure after a regular interval of time till the colour of iodine does not change. You can redo the experiment by clicking on the ‘Reset’ button. Note: If we add saliva on starch, the salivary amylase present in saliva gradually acts on starch and converts it into maltose. Starch keeps on giving blue colour with iodine till it is completely digested into maltose. At this point, no blue colour is formed.
This is the end point or achromic point.
. Tube 1 was the negative control because it contains no enzyme (independent variable). Tube 2 was the positive control because it contains enzyme that has not been altered so it should work as expected. The independent variable was the different conditions to which amylase was exposed. The dependent variable was the disappearance of starch or the presence of an active enzyme. Tube 2 (the control) was the only tube that contained active enzyme. Tubes 3, 4, and 5 must contain denatured enzyme because the enzyme was unable to break down starch.
Bio Amylase Lab Manual Answers
The amylase in tube 3 does not have tertiary structure. When an enzyme is denatured it loses its tertiary structure and no longer functions. You can denature an enzyme by subjecting it to extreme conditions. Extreme heat and high concentrations of H+ ions (low pH) or salt alter the hydrogen bonds that help an enzyme maintain its secondary and tertiary structure.
When an enzyme loses its secondary and tertiary structure it is considered to be denatured and no longer functions.