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Effect of varying pH on enzyme activity
Investigating how temperature affects enzyme activities
Conduct an investigation of lactase enzyme activity
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Data table 1 Well plate Contents Glucose concentration A 3 drops 5% sucrose + 3 drops distilled water Negative B 3 drops milk+3 drops distilled water Negative C 3 drops 5% sucrose +3 drops lactase Negative D 3 drops milk +3 drops lactase 15+ E 3 drops 20% glucose +3 drops distilled water 110 ++ Questions B. In this exercise, five reactions were performed. Of those reactions, two were negative controls and one was a positive control. Describe which of the reactions were controls and if they provided the expected results. Use the data in Data Table 1 to support your answer. Answer- In this exercise the positive control was solution E because it contained glucose which would test positive for sugar. The negative controls would be solutions …show more content…
Describe the relationship between temperature and the enzymatic activity of lactase. Of the three temperatures tested, which is the optimal temperature for enzyme activity? Use the results in Data Table 2 to support your answer. Hypothesize how the structure of the lactase relates to the results in Data Table 2. Answer- After conducting this experiment and collecting the data I would have to say that the optimal temperature for enzyme activity would have to be room temperature which in my experiment was thirty-four degrees Celsius. I came to this answer because the glucose test strip showed that at room temperature there was more glucose concentration that at either of the other temperatures. Due to temperature extremes in the boiling water the enzymes could no longer function because the breakdown of lactose stopped. The cold water also hindered the breakdown of the lactose but as the water warmed the enzymes were more active which can be seen in the results for the cold water at 20 minutes B. Describe the relationship between pH and the enzymatic activity of lactase. Of the pH values tested, which is the optimal pH? Use the results in Data Table 3 to support your answer. Hypothesize how the structure of the lactase relates to the results in Data Table
To begin the study, I first calculated how much of each solution I would need. I knew that the final volume of my reaction solution needed to me 30ml, so I calculated how much of starch, amylase, and tris buffer I would need. I used the formula Concentration (initial stock solution) x Volume (initial stock solution)= Concentration (final solution) x Volume (final solution). Using this formula, I found that I would need an initial concentration of 21 ml of starch, 1 ml of amylase, and 8 ml of the tris buffer. After calculating the amounts of substances I would need, I created two different solutions, one with the Carb Cutter and one without. Carb Cutter claims to block starch, however, to find this I needed to test the absorbance level of the control to compare the effect Carb Cutter had on the solution. Below is a graph showing the concentration of the control reaction over one minute intervals through the
We then took 1ml of the 0.1% solution from test tube 2 using the glucose pipette and added it to test tube 3, we then used the H2O pipette and added 9ml of H2O into test tube 3 creating 10ml of 0.01% solution.
For example, substrate concentration, enzyme concentration, and temperature could all be factors that affected the chemical reactions in our experiment. The concentration of substrate, in this case, would not have an affect on how the bovine liver catalase and the yeast would react. The reason why is because in both instances, the substrate (hydrogen peroxide) concentration was 1.5%. Therefore, the hydrogen peroxide would saturate the enzyme and produce the maximum rate of the chemical reaction. The other factor that could affect the rate of reaction is enzyme concentration. Evidently, higher concentrations of catalase in the bovine liver produced faster reactions, and the opposite occurs for lower concentrations of catalase. More enzymes in the catalase solution would collide with the hydrogen peroxide substrate. However, the yeast would react slower than the 400 U/mL solution, but faster than the 40 U/mL. Based on this evidence, I would conclude that the yeast has a higher enzyme concentration than 40 U/mL, but lower than 400
For example, incubating the samples at different temperatures would create more data points to establish an optimal temperature. From the results in the experiment in this study, it is known as temperature increases, enzymatic activity increase, and vise versa. However, what can not be observed is at what point does the increase in temperature begin to denature the enzyme, above 60°C. Furthermore, assays can be preformed to determine optimal pH, as well. From Dutta’s, and his partners, experiment it shows that there is a range where the Heliodiaptomus viduus’s lactase shows the most activity, which is between 5.0 and 6.0
Using a Bunsen burner, tripod and beaker of water 100 degrees could also be tested and 0 degrees was tested by using ice. (I didn’t investigate the 80 degrees temperature). Fair test: Below is a list of things that were kept the same throughout the investigation: Volumes of lipase and milk (by using syringes); volumes of phenolphthalein and sodium carbonate (using pipettes); (best volumes from the preliminary work were used). Each temperature was repeated three times to get a good average. The milk and lipase were equilibrated to the right temperatures before the lipase was added to the milk.
Mader, S. S. (2010). Metabolism: Energy and Enzymes. In K. G. Lyle-Ippolito, & A. T. Storfer (Ed.), Inquiry into life (13th ed., pp. 105-107). Princeton, N.J: McGraw Hill.
The first thing I needed to see was how different concentrations affected the weight and length of the potato. So I needed to see each extreme - highest concentration and lowest concentration. I used 0 molar concentrations (the lowest) and 1 molar (the highest.) I then left each test for 20 minutes, but found after that time a slight reaction had taken place - the potato chips only increased or decreased by a very short amount. I then predicted that now I would have to leave the tests for a longer amount of time and use longer potato chips to ensure that there is enough of a reaction to compare
In this experiment as a whole, there were three individual experiments conducted, each with an individualized hypothesis. For the effect of temperature on enzyme activity, catalase activity will be decreased when catalase is exposed to temperatures greater than or less approximately 23 degrees Celsius. For the effect of enzyme concentration on enzyme activity, a concentration of greater or less than approximately 50% enzymes, the less active catalase will be. Lastly, the more the pH buffer deviates from a basic pH of 7, the less active catalase will be.
Alkaline Phosphatase (APase) is an important enzyme in pre-diagnostic treatments making it an intensely studied enzyme. In order to fully understand the biochemical properties of enzymes, a kinetic explanation is essential. The kinetic assessment allows for a mechanism on how the enzyme functions. The experiment performed outlines the kinetic assessment for the purification of APase, which was purified in latter experiments through the lysis of E.coli’s bacterial cell wall. This kinetic experiment exploits the catalytic process of APase; APase catalyzes a hydrolysis reaction to produce an inorganic phosphate and alcohol via an intermediate complex.1 Using the Michaelis-Menton model for kinetic characteristics, the kinetic values of APase were found by evaluating the enzymatic rate using a paranitrophenyl phosphate (PNPP) substrate. This model uses an equation to describe enzymatic rates, by relating the
We hypothesized that the more heat that we put in or the more heat that we take out, would denature the enzymes and slow down the rate. We set up a plate of depressions the same way as above. We boiled water to 50o C, poured the water onto a tray and did the steps of placing the discs in same as above and timed it until they rose above the surface. We did the same process but instead of using heat, we put ice and cold water on a tray which was about 3.5o C. The control for this experiment was the one that we did before because it was at room temperature. The results for the hot tray showed no rate. The cold tray sped up the rate of reactions making it occur faster than at room temperature starting at 6 for 100% catalase. This lab supported and disproved our hypotheses. It supported our hypothesis for adding more heat because the enzymes were in such hot conditions that the heat denatured the enzyme, making it not possible to create a chemical reaction. So the rate of reaction was zero because the enzymes didn’t split apart hydrogen peroxide. The cold tray disproved our hypothesis. We thought that the cold tray would also denature the the catalase so that there would be little to no rate. Maybe the data came out this way because the catalase was left out in room temperature for a long time that maybe when we took away the heat, it sped up the reaction rate.
Investigating the Effect of Enzyme Concentration on the Hydrolysis of Starch with Amylase Aim: Investigate the effect of enzyme concentration on the rate of an enzyme-controlled reaction. Using amylase and starch as my example. Introduction: I am investigating the effect of the concentration of the enzyme, amylase on the time taken for the enzyme to fully breakdown the substrate, starch to a sugar solution. The varied variable will be the concentration and all other variables are going to be fixed. The different concentrations will be: 0.5% 0.75% 1.0% 1.5% 2% An enzyme is a class of protein, which acts as a biological catalyst to speed up the rate of reaction with its substrates.
Their table had 15 mL glucose, 10 mL RO water, and 10 mL of yeast which they then placed in an incubator at 37 degrees Celsius. In conclusion, I feel that the absence of RO water in the flask made the enzymes work a little harder than when the RO water was in the mixture of the flask. Comparison #4 is between the Controlled Table and Table #5. The mixture for that table’s flask was 15 mL Sucrose, 10 mL of RO water and 10 mL of yeast, which the flask was then placed in an incubator at 37 degrees Celsius.
Dependent Variables Amount of vitamin C in fruit juices. Controlled Variable Same amount of liquid for each fruit juice.... ... middle of paper ... ...
Madar, Sylvia S., & Windelspecht, Michael. (2014). Inquiry into Life, Metabolism: Energy & Enzymes (pp. 104-107). New York: McGraw Hill.
The temperature of the water shows if the temperature in which catalase reacts in has an effect on the amount of oxygen produced. Every enzyme has an optimum amount of pH, which allows it to have a higher reaction velocity (WBC).The higher the reaction velocity the more reactive the enzyme is. Measuring the different amount of pH solutions and their effect on the amount of oxygen produced can show the optimum pH for catalase and the effect pH has on catalase. The data that these three independent variables will yield will allow us to better understand the effects concentration, temperature and pH have on the enzyme catalase. If catalase reacts at full concentration, 37 degrees celsius and a pH of eight the enzyme catalase will produce more oxygen than if it is at room temperature, a lower concentration and a more acidic base because the higher temperature will allow molecules to move faster and have a higher chance to collide and react, a higher concentration will create a higher enzyme to substrate ratio which allows it to react more and finally a more basic pH will allow it catalase to have a higher reaction