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
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
These labels indicated the lactose solution that was be placed into the mini-microfuge tubes. The varying lactose ph solutions were obtained. The four miniature pipets were then used, (one per solution,) to add 1mL of the solution to the corresponding mini-microfuge tubes. When this step is completed there were two mini-microfuge tubes that matched the paper towel. Then, once all of the solutions contained their respective lactose solutions, 0.5mL of the lactase enzyme suspension was added to the first mini-microfuge tube labeled LPH4 on the paper towel, and 4 on the microfuge tube. As soon as the lactase enzyme suspension was added to the mini-microfuge tube, the timer was started in stopwatch mode (increasing.) When the timer reached 7 minutes and 30 seconds, the glucose test strip was dipped into the created solution in the mini-microfuge tube for 2 seconds (keep timer going, as the timer is also needed for the glucose strip. Once the two seconds had elapsed, the test strip was immediately removed, and the excess solution was wiped gently on the side of the mini-microfuge tube. The timer was continued for 30 addition seconds. Once the timer reached 7:32 (the extra two seconds accounting for the glucose dip), the test strip was then compared the glucose test strip color chart that is found on the side of the glucose test strip
· I predict that the enzyme will work at its best at 37c because that
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.
However, the decrease varied depending on the temperature. The lowest temperature, 4 degrees Celsius, experienced a very low decrease of amylose percentage. Temperature at 22 degrees Celsius and 37 degrees Celsius, both had a drastic decrease in amylose percentage. While the highest temperature, 70 degrees Celsius, experienced an increase of amylose percentage. In conclusion, as the temperature increases the percentage of amylose decreases; however, if the temperature gets too high the percentage of amylose will begin to increase. The percentage of amylose increases at high temperatures because there is less enzyme activity at high temperatures. However, when the temperature is lower, more enzyme activity will be present, which results in the decrease of amylose percentage. This is why there is a decrease of amylose percentage in 4, 22, and 37 degrees Celsius. In this experiment the optimal temperature is 37 degrees Celsius, this is because this is the average human body temperature. Therefore, amylase works better at temperatures it is familiar
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.
I used Cheerios, distilled water, and a pestle and mortar. I ground the Cheerios until they had a fine, sand-like texture and consistency. I then added distilled water and mixed until I was left with a thin, runny solution, that was beige in color. Once I had the stock solution made, I was able to perform my first experiment, beginning with Benedict’s reagent. For this experiment I used a hot plate, beaker, and three test tubes, one labeled + (positive control), - (negative control), and Cheerios. Two milliliters of each solution was then added to the tubes they were labeled to go into. In this experiment, the positive control was a glucose solution. I then added two milliliters of Benedict’s reagent to each tube. Once a boiling bath had been made using water, the beaker, and the hot plate, each of the three test tubes were places, sitting upwards, into the boiling bath. A timer was set for three minutes, and I recorded the color
Dependent Variable ------------------ Rate at which the bubbles of oxygen rise, which will be calculated by observing how many bubbles of oxygen rise to the surface of a measuring cylinder (by means of downward displacement) in one minute. This will be measured in bubbles per ten seconds. Control variables: ¨ Volume of substrate used: 100ml ¨ Temperature: taken place at room temperature 21 degrees centigrade ¨ Type of substrate used: Hydrogen peroxide ¨ Mass of meat used: 5g ¨ Amount of water in the test tube in which the oxygen bubbles downward displaces in the water. This is so the time taken for each individual bubble to effectively rise to the bottom of the test tube will take the same amount of time.
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 conclusion, the method seems flawed in accurately measuring the glucose concentration of solutions. To make the experiment a "fair test," three main variables needed to be kept constant. Firstly, the volumes, including all measurements, i.e., the amount of Benedict's solution used and the amount of glucose water solution in each test tube. Secondly, the time that all the test tubes were kept in the water bath had to be the same for all test tubes, including solution X.
Researchers experimented with enzyme activity with potato extract. Researchers will test enzyme activity by increasing and decreasing pH levels, lowering and increasing temperature, and substrate concentration effects. In the first experiment, researchers hypothesized that different pH levels would change how much Benzoquinone is created and how the enzymes function at neutral pH levels rather than higher and lower levels. Researchers used potato extract and different levels of pH to test their hypothesis. In addition, researchers questioned at what temperature does the greatest amount of potato extract enzyme activity take place in?
Enzyme concentration is directly proportional to the rate of reaction provided the substrate concentration is maintained at a high level and the pH and temperature are kept constant. We know that the substrate concentration is maintained at the same level in all samples, this done by ensuring that all samples are of equal mass and we know that all the samples were placed in an incubator at 40°C thus ensuring that the temperature effects the rate of reaction in all samples in the same way. Graph: - From 0% ¬> 0.25% concentration we can see the greatest rate of reaction as there is an abundance of substrate molecules available to combine with the active site of the enzymes producing a large gradient on the graph. As concentration increases from 0.25% ¬> 0.