Effects of pH and Concentration
on Amylase Digestion of Starch
Amylase is an enzyme that breaks down starch to maltose. In an effort to understand how this enzyme works, it is essential that various experiments be carried out. We were testing the Hydrolysis of starch and use of the reaction vials. The solutions needed are: amylose, dilute amylase, iodine-potassium iodide, and ph 7 buffer. We obtain a reaction vial with dropper top. We mix in the vial 2 ml of amylose solution with 2 ml of ph 7 buffers, add 1 ml of dilute amylase, note the time, cap the vial and shake it for a minute to mix the contents. After the minute we place 3 drops one of top of each other in a glass plate. Then add 1 drop of iodine-potassium to the plate as well. Hold the plate on top of a white surface and observe the color of the sample. Dark blue-black indicates the presence of starch which we did not see. We were supposed to continue testing samples at one minute intervals until a dark brown color results. But that wasn’t done because the first one did not work either. We were supposed to work as teams and try different buffers until the solution of starch was being able to be seen. Prior to the experiment, it was hypothesized that a greater acidity would increase the rate of starch digestion. It was also supposed to predict that a greater concentration of amylase would increase the rate of starch digestion. The lab was supposed to be that the sample with the highest concentration of amylase produced the most efficient digestion of starch, while digestion took the longest with a lower concentration of amylase. Yet in the experiment that was done in class it did not show neither. It would just look like an error. Probably messing around with the amounts would get us to where we needed but yet there was not much time. While the results were supposed to appear reasonable, the potential for error in this experiment must be taken into consideration and could’ve been made better. Maybe we...
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