Method I generally followed most of my plan for the experiments, but to improve accuracy and reliability, I made one change. In my plan, I said that I was going to use 20cm³ of starch for each experiment. However, in my actual experiment I used 40cm³ of starch. This is because I thought I might not have had enough solution if I only used 20cm³ of starch. If this was the case, then I would have to stop the experiment half way through, which would have prevented me from obtaining accurate results. So for this reason, my results would be more accurate and reliable. For everything else, I followed my original plan. To ensure the results were accurate, I made sure I accurately measured out the amylase and starch solutions for each …show more content…
0.2% starch Time (secs) % Transmission 30 1 60 1 90 30 120 45 150 58 180 70 210 76 240 84 270 90 300 99 0.4% starch Time (secs) % Transmission 30 1 60 1 90 1 120 1 150 19 180 30 210 50 240 55 270 58 300 64 0.5% starch Time (secs) % Transmission 30 1 60 1 90 43 120 57 150 71 180 78 210 83 240 87 270 89 300 90 0.6% starch Time (secs) % Transmission 30 1 60 1 90 14 120 42 150 57 180 63 210 70 240 75 270 77 300 79 0.8% starch Time (secs) % Transmission 30 1 60 1 90 16 120 54 150 71 180 77 210 93 240 94 270 97 300 99 1% starch Time (secs) % Transmission 30 1 60 1 90 17 120 55 150 69 180 76 210 93 240 95 270 97 300 99 I will now plot these results on separate graphs. I have plotted the graphs for the average % transmission against time. I did a separate graph for each concentration of starch. I then worked out the gradient of each curve by drawing a tangent. I worked out the gradient by doing the difference in y divided by the difference in x. The gradient represents the rate of reaction. I will now need to draw a final graph to show concentration of starch against rate of reaction. Below is a table to show the rate of reaction for each
In the experiment we used Turnip, Hydrogen Peroxide, Distilled Water, and Guaiacol as my substances. On the first activity, Effect of Enzyme concentration of Reaction Rate for low enzyme concentration, we tested three concentrations of the turnip extract, and hydrogen peroxide. For the Turnip Extract I used 0.5 ml, 1.0 ml, and 2.0 ml. For hydrogen peroxide we used 0.1 ml, 0.2 ml, and 0.4 ml. We used a control to see the standard, and used a control for each enzyme concentration used. The control contains turnip extract and the color reagent, Guaiacol. We prepared my substrate tubes separately from the enzyme tubes. My substrate tube
Used to see if the temperature of the water is at 37oc – 40oc and if
I know that osmosis will occur in the vegetables, but I am not sure of
How concentration affects the rate of reaction between Hydrochloric Acid and Sodium Thiosulphate Chemistry Coursework How Concentration Affects a Reaction Aim: The aim of this experiment is to find out how concentration affects the rate of reaction between Hydrochloric Acid and Sodium Thiosulphate. Introduction: This experiment will be carried out by drawing a cross on a piece of paper and mixing hydrochloric acid and sodium thiosulphate together to see if the cross disappears. The concentration of hydrochloric acid would change every reaction to show that concentration effects a reaction.
My graph shows there is an almost perfect positive correlation between the hydrogen peroxide concentration and the rate of the catalase enzyme reaction, with a correlation coefficient of 0.99. The rate of reaction at 1% concentration was 0.46cm3 oxygen produced per minute and the lowest recorded rate. For 3% was 1.33cm3 per minute, and for 6% was 2.17cm3 per minute and was the highest recorded rate. The
Question: How does changing enzyme concentration or temperature affect the reaction time of enzyme activity?
Human error is easily obtained when working on an experiment with so many different solutions, time measurements, and accuracies of measurements. An easy mistake could have been made while waiting 15-20 minutes for the Carb Cutter to digest. With the time crunch in the Biology Lab, the Carb Cutter may not have been completely digested before rushing to begin the experiment. The results from the experiment showed an increase in absorbance with the Carb Cutter pill, which is not accurate because there is no way that more starch was made in the solution. Given more time for the procedure, this lab experiment may have received more accurate results.
Instead of changing the amount of amylase enzyme added to the test tubes, change the amount of starch added to the test tube. Meaning, the amylase will already be in the test tubes and the starch will added into the test tubes at different amounts. The rest of the experiment would be performed in the same way.
Using the yellow tube, which included everything but starch, as the blank, each group zeroed their spectrophotometer. This was done so that any absorbance observed depends only on the amount of starch present, not on any other reagents (buffer, IKI). To zero the spectrophotometer, the wavelength was first set at 580nm, using knob 3 (45). Next, the groups made sure that the light next to “transmittance” was lit, and the chamber to be tightly closed. Having the chamber empty & closed tightly provides reference for the darkest condition possible. Using knob 1, the transmittance was turned until it read 0.0 (45). Before the groups used their blank test tube to zero the spectrophotometer, each needed to wipe the tube with kimwipes to ensure a clean reading. Turning knob 2, each group was then instructed to zero the absorbance, 0.000. Upon removing the blank, each trial was inserted into the chamber (46). The
We then recorded the initial color. We placed each tube in boiling water for one minute and recorded the color results and gave our conclusion. To test for starch using Lugol’s solution, we reused the test tubes and added a squirt of the solution. We recorded the final color and then our conclusion for each content. To test for lipids using paper towels, we placed a drop of solution and we let it stand for one minute. We then recorded our observation, if it was dry or not dry and wrote our conclusion for each sample. To test for proteins using Biuret’s reagent, we added a squirt of stock solution plus a few drops of Biuret’s solution. We wrote the initial color. We then shook the solution and waited for two minutes before recording the results. After the two minutes, we wrote the final color and conclusion for each content. For the unknowns, we wrote the odor and appearance of each content and then tested the benedict’s, starch, lipid, and protein test and wrote our conclusion.
KM is the substrate concentration that permits for half of vmax to be obtained in the
Data: Effect of Solute Concentration on Osmosis in Potato Cells (for the 6 groups of our class)
reaction rate increases. If the temperature of an enzyme gets to high the reaction rate will slow
The purpose of this lab report is to investigate the effect of substrate concentration on enzyme activity as tested with the enzyme catalase and the substrate hydrogen peroxide at several concentrations to produce oxygen. It was assumed that an increase in hydrogen peroxide concentration would decrease the amount of time the paper circle with the enzyme catalase present on it, sowing an increase in enzyme activity. Therefore it can be hypothesised that there would be an effect on catalase activity from the increase in hydrogen peroxide concentration measured in time for the paper circle to ride to the top of the solution.
In this experiment we wanted to determine the optimal temperatures for fungal, Aspergillus oryzae, and bacterial, Bacillus licheniformis. In order to see if any of the starch was broken down, Iodine was mixed with the starch-amylase substance. In four spot plates, the groups labeled the different temperatures, once the iodine came in contact with the starch, the result would be a reaction that turns the fluid into this dark blue/black color. In a span of 10 minutes, with occasional check ups on the solution every 2 minutes, the amylase-starch solution was placed into five types of temperature, all being Celsius. The five temperatures were 0 degrees, 25 degrees, 55 degrees, and 85 degrees Celsius. The solution would change colors, so in order to measure the changes, a scale was used. Such scale was a 1-5 scale, with colors next to each number. One being the lightest color, or yellow, and 5 being the darkest color, or black. Based on the change of color, we could tell how fast it hydrolyzed the starch in a span of 10 minutes. To keep record of the results, the results were put in Data Tables used from the Lab Manual. The average optimal temperature for Bacteria Amylase was 85 degrees Celsius, while the Fungal was 55 degrees Celsius. You can see this by looking for the