Enzymes Laboratory Report

ENZYMES LABORATORY REPORT Introduction The utilization of any complex molecule for energy by an organism is dependent on a process called hydrolysis. Hydrolysis publishs complex molecules into simpler molecules using water. Similarly, the process that is the reverse of this is called evaporation synthesis, which removes water from simpler molecules. However, because hydrolysis occurs very slowly, living organisms use biochemicals called enzymes to speed up the reaction.In this research laboratory exercise, we studied the nature of enzyme actions using live yeast cells as our source of sucrose. The enzyme will then break the sucrose into one molecule of glucose and fructose. Because sucrose is a large molecule that cannot enter most cells, yeast will produce sucrase and secrete it into cell membranes. The sucrose will be hydrolyzed into small six-carbon monosaccharoses which can enter into the cell membranes. The sucrose can be obtained from a 0. 5 percentage dissolver of dry bake rs yeast in water.In parts A and B, the experiment will study the optimal temperature under which the yeast cells degrade sucrose using variable pH and temperature of the environment surrounding the yeast cells. Part C will study the beliefs of positive heat on enzyme use and part D will focus on the saturation menstruation for enzymes using varying subst value densitys. Materials and Procedure See pg 79-82 section Enzymes Experiments in Biology from Chemistry to call down Fifth Edition By Linda R. Van Thiel Results In turn up A. ffect of pH, the results we obtained for resistance 1 was a resolving power twist of orange and a color exertion of 3. For 2 was also orange and color performance of 3. For 3 was orange and a color military action of 3, for 4 was green and a color natural process of 1, and finally for 5 was blue and a color act of 0. From our results, it shows the optimum pH is provide 1-3. The chasteness in this experiment was test underpass 3A, with a p H of 7, as this pH was neutral. In test B. set up of temperature, the optimum temperature is shown on our graph to be two different points (either 24 or 60 degrees).For our results we legitimate a dissolving agent color of blue for tube 1, and a color natural action of 0. For tube 2, we legitimate a resultant role color of orange and a color activity of 3. For tube 3, we receive a firmness color of green and a color activity of 1, for tube 4 we genuine a solution color of orange and a color activity of 3. Finally, for test tube 5, we received a solution color of blue, and a color activity of 0. The highest rates of activity were found in test tubes 2 and 4.The control in this experiment was test tube number 2, which was kept in the temperature environment of 24 C room temperature. In test C. Effect of Denaturation, the drudgeed sucrose and sucrase received sparingly demoralizeed color activities than the non-boiled tube. Shown on graph 8. 3, the graph begins with no mov ement in rate of activity followed by a steady add in the color activity. The results show that test tube 1, which was boiled sucrase and sucrose, had a solution color of green and a color activity of 1. rise tube 2, which contained boiled sucrase had a solution color of green and a color activity of 1, test tube 3, which contained boiled sucrose, had a solution color of orange and a color activity of 3, finally test tube 4, which was neither boiled, had a solution color of red, and a color activity of 4. From the results, the neither boiled tube had the highest color activity. The control in this experiment was test tube 4, which was all told untouched. In test D. Effect if substrate concentration, the higher concentrations of sucrose received a higher color activity.The graph is represented by a constant followed by a steady drop as the concentration of sucrose come downs. The results showed that in test tube 1, which contained 100% of sucrose, the solution color was red and th e solution gained a color activity of 4. In test tube 2, the concentration of sucrose of 50%, and the solution color was also red, which a color activity of 4. In test tube 3, which contained 25% sucrose, the solution color was orange, and had a color activity of 3, in test tube 4, which contained 10% concentration the solution color was green and had a color activity of 1.In the last test tube, which had no concentration of sucrose, the solution color was blue, and had no color activity. The control in this experiment was test tube 5 which contained no sucrose at all. Discussion In the get-go test, the test of the effect of pH, the results show the effect of pH increases the rate of reaction as having a slightly acidic pH will increase the actual reaction while supporting a more basic pH will decrease the reaction. In our results, it shows that the pH reaches an optimum pH of 7 before decrease.The results are not completely accurate, as the first three tubes all had a color activi ty of 3. The actual results should have had a slightly higher color activity for the optimum pH (which would have been from a pH of 5-6) and a lower color activity for the starting and ending pH. Experimental error may be caused by earthy test tubes and slightly inaccurate amounts of solution being placed into test tubes. The second test consisted of the effects of Temperature. Temperature (as represented in graph 8. 2) increases rate of reaction in the enzyme until reaching an optimum point, and then decreasing rapidly.However, in our results, we were accurate until we reached the optimum point, (37 degrees). Instead of this being the highest point for rate of reaction, we obtained a color activity of 1. Because 37 degrees was the optimum temperature, this should have been the highest point and the highest rate of activity. However, we had an experimental error in the form of accidently placing the tertiary tube in the wrong temperature environment. The third test consisted of th e effects of Denaturation. In this test, the tube that showed the highest color activity was tube four because it was not exposed to the higher temperatures.Enzymes that are boiled, or exposed to entire temperatures could change the protein component thus destroying the enzyme. However, by boiling the substrate, the enzymes rate of reaction increases. However in our data, the first and second test tube should have contained no color activity as such extreme temperature would have already destroyed the enzyme. There could have been experimental error in the length it took to boil the test tube as it may not have reached its required amount. The last test consisted of the cause of Sucrose Concentration.By increasing the amount of substrate, the rate of reaction will also increase as it is more likely that substrate molecules are closer to an enzyme molecule. However, this is only true to a certain bounce as demonstrated in the chart. Both test tube 1 (which contains 100% of sucros e) and test tube 2 (which contains 50% of sucrose) have the same color activity despite the significant difference in concentration. This is because the concentration of substrates has reached an approximate saturation point, which is seen in this enzymatic reaction to be 50%.