Introduction An enzyme is a protein that functions as a catalyst, it speeds up chemical reactions (Freeman et al. 2017 p. 90). Enzymes are often large globular proteins and are able to hold substrates in specific orientations so they are able to react, the location where the substrate binds with the enzyme and reacts is called the active site and is the location where the catalysis occurs (Freeman et al. 2017). Enzymes activity is often related to the optimal environment for them in respect to temperature and pH, meaning that each enzyme will have an optimal temperature/pH where it will preform at its peak relating to the environment it is from (Freeman et al. 2017). Enzymes that break down α-glycosidic linkages in starch are called amylases
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First, we labeled 5 test tubes with .5%, .25%, .125%, .063% and .031% amylase and then added 5 ml of distilled water to each test tube. Second, we added 5 ml of the 1% amylase from our flip top bottle to the first test tube, .5%, thus reducing the percentage of amylase in the tube to .5%. Third, we removed 5 ml of solution from our .5% tube, and added it to our second test tube, reducing the amount of amylase in test tube 2 to .25%. Fourth, we repeated this process for the remaining test tubes, removing 1 ml of solution from the previous concentration and adding it to the next test tube to reduce the percentage further, creating a .125% tube, a .063% tube, and a .031% tube. Fifth we added 2 ml of 6.8 buffer to each of our 5 tubes. Sixth, we filled each chamber of a 95 well spot plate with one drop of iodine reagent. Seventh, doing each tube separately, one at a time, starting with the .5% tube, we added .5 mL of potato starch to the test tube, thus starting the reaction, and we started our second/minute timer and rolling the tube between our hands to mix well. Eighth, using a Pasteur pipet, we transferred one drop of our .5% solution tube to one of the chambers in the 95 well spot plate, putting a drop in a new chamber every 15 seconds. We were looking for when there was no longer a color change, signifying the digestion of the starch was complete. We then repeated steps 7-8 with the remaining concentrations of, .25%, .125%, .063%, and .031% amylase one at a time (Crawley and Pendarvis
First, we labeled 5 test tubes with .5%, .25%, .125%, .063% and .031% amylase and then added 5 ml of distilled water to each test tube. Second, we added 5 ml of the 1% amylase from our flip top bottle to the first test tube, .5%, thus reducing the percentage of amylase in the tube to .5%. Third, we removed 5 ml of solution from our .5% tube, and added it to our second test tube, reducing the amount of amylase in test tube 2 to .25%. Fourth, we repeated this process for the remaining test tubes, removing 1 ml of solution from the previous concentration and adding it to the next test tube to reduce the percentage further, creating a .125% tube, a .063% tube, and a .031% tube. Fifth we added 2 ml of 6.8 buffer to each of our 5 tubes. Sixth, we filled each chamber of a 95 well spot plate with one drop of iodine reagent. Seventh, doing each tube separately, one at a time, starting with the .5% tube, we added .5 mL of potato starch to the test tube, thus starting the reaction, and we started our second/minute timer and rolling the tube between our hands to mix well. Eighth, using a Pasteur pipet, we transferred one drop of our .5% solution tube to one of the chambers in the 95 well spot plate, putting a drop in a new chamber every 15 seconds. We were looking for when there was no longer a color change, signifying the digestion of the starch was complete. We then repeated steps 7-8 with the remaining concentrations of, .25%, .125%, .063%, and .031% amylase one at a time (Crawley and Pendarvis