Each group labels three test tubes with SS and our group names, which ours was 5 dots, and were told to put 4ml of stock starch in each test tub with a pipette. The next step was to get each beaker of 1, 5, and 10 percent concentration of amylase and put 4ml in three other beakers labeled with their respected concentrations. After that was completed our group put all 6 beakers in a water bath that was at 37 degrees Celsius, room temperature, for five minutes. We did that in order for both the substrate and the enzyme to be at its highest effectiveness. While that was going on one of our group members put one drop of IKI, a die that changes the color of starch to a black blue color, in each depression of the spot plate. The reason for that is according to the lab manual, IKI does not stain maltose, so it can determine the effectiveness of the enzyme on starch. after the five minutes had elapsed, one of my group members grabbed one test tube with SS and 1 percent amylase and brought it back to the table. When she returned she poured the amylase 1% in the SS test tube and mixed it for 10 second. She then drew up some of the mixture into a plastic pipette and prepared to continue the …show more content…
Some groups were doing an increase in temp. to try to see at what temp the catalyst would denature, proteins denature after they reach the optima temp in the environment which can in turn affect the shape and structure of an enzyme. (Campbell bio, 11th edition, Pg. 158) Then others were given other types of inhibitors. Those inhibitors were sodium dodecyl sulfate, a form of detergent, an amylase inhibitor, a nutrition competitive inhibiter, and what we were using was EDTA, a chelating agent (an agent that binds Ca2 and Mg2 to each other within the center of metal or bacterial enzymes in order to keep the enzyme from carrying out its job. (Dictionary of Medicine , 7th