effect of pH on amylase activity
Biology Lab Report
Research Question:
Effects of pH on amylase activity
Introduction:
Amylase is an enzyme that is in human’s saliva as well as the pancreas. Enzymes are biological catalysts that speed up a chemical reaction. They break down complex molecules into simple ones. In this case, amylase converts starches (complex molecule) into simple sugars. That is why foods like potatoes for example, may taste sweet to us, because they contain starch. The optimum pH for pancreatic amylase is the pH of 7. In the experiment I have used buffer solutions with the pHs of 2.8, 4 and 6.5. I have also used iodine and starch. Normally, iodine is orange-yellow, however when you add starch to it, the solution will turn blue-black.
Aim:
The aim for this experiment is to investigate how the different buffer solutions work on the enzyme amylase. This will be investigated by using iodine and by timing the experiment using the colorimeter and the program Loggerlite.
Hypothesis:
The pH denatures enzymes, and since amylase is an enzyme, my hypothesis is that the pH will change the shape of the active site of the enzyme, so the substrate will not be able to fit in anymore. Therefore if the pH is either too low or too high, it may stop the enzyme from working.
I believe that the solution containing iodine, starch and amylase will turn blue-black when the enzyme will be denatured. However, when I will use the buffer solution which has the pH of 6.5 (which is the closest to amylase’s optimum temperature) the solution will slowly turn back to its original colour (yellow-orange), as I believe the enzyme will start digesting the starch.
Apparatus:
buffer solutions of pH 2.8, 4 and 6.5 starch solution amylase solution iodine solution colorimeter Loggerlite program pipette test-tubes test-tube rack marker (Sharpie – to label which buffer solution is in which test-tube) stopwatch (on iPhone) laptop (MacBook Pro)
Research Question:
Effects of pH on amylase activity
Introduction:
Amylase is an enzyme that is in human’s saliva as well as the pancreas. Enzymes are biological catalysts that speed up a chemical reaction. They break down complex molecules into simple ones. In this case, amylase converts starches (complex molecule) into simple sugars. That is why foods like potatoes for example, may taste sweet to us, because they contain starch. The optimum pH for pancreatic amylase is the pH of 7. In the experiment I have used buffer solutions with the pHs of 2.8, 4 and 6.5. I have also used iodine and starch. Normally, iodine is orange-yellow, however when you add starch to it, the solution will turn blue-black.
Aim:
The aim for this experiment is to investigate how the different buffer solutions work on the enzyme amylase. This will be investigated by using iodine and by timing the experiment using the colorimeter and the program Loggerlite.
Hypothesis:
The pH denatures enzymes, and since amylase is an enzyme, my hypothesis is that the pH will change the shape of the active site of the enzyme, so the substrate will not be able to fit in anymore. Therefore if the pH is either too low or too high, it may stop the enzyme from working.
I believe that the solution containing iodine, starch and amylase will turn blue-black when the enzyme will be denatured. However, when I will use the buffer solution which has the pH of 6.5 (which is the closest to amylase’s optimum temperature) the solution will slowly turn back to its original colour (yellow-orange), as I believe the enzyme will start digesting the starch.
Apparatus:
buffer solutions of pH 2.8, 4 and 6.5 starch solution amylase solution iodine solution colorimeter Loggerlite program pipette test-tubes test-tube rack marker (Sharpie – to label which buffer solution is in which test-tube) stopwatch (on iPhone) laptop (MacBook Pro)