2. Which enzyme concentration produced the greatest concentration of mono and disaccharides after 10 minutes? Explain how your Benedict's test results support your answer.
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See attached, you have a table that is perhaps required for some of the questions.
Answer question number 2 in your own words. Do not copy and paste from google.
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- Help me answer question 3 4. Seliwanoff’s test – prepare 4 test tubes and place 5 drops of glucose, fructose, sucrose and xylose in separate test tubes. Add 1 ml of seliwanoff’s reagent in each of the 4 test tubes. Immerse in a boiling water bath. Observe the color change in each tube after 3 minutes of boiling. If no color change is observed, continue heating for another 2 minutes and observe.Will UPVOTE Answer the following: 1. What is the effect of boiling in the test tube with starch solution and saliva? 2. What is anaerobic oxidation? In your observation, which is the Hydrogen acceptor in the experiment, methylene blue or milk? 3. If the sample turned to blue or black upon the addition of I2 solution, is the honey genuine or not? Explain your answer 4. What changes do you think take place as the color changes upon the addition of phenol, pyrogallol or catechol and guac solution to the potato extract? 5. Differentiate an enzyme activator from an indicatorExperiment 2: Protein Digestion by Pepsin Label 4 test tubes P1, P2, P3, and P4 (“P” is for Pepsin, a proteolytic enzyme.) To each of the test tubes, add the following, and measure the pH before incubating: Test tube P1: Add 1 mL (1000 ml) albumin + 2 mL (2000 ml) distilled water Record the pH of this tube, here: ______ Test tube P2: Add 1 mL (1000 ml) albumin + 1 mL (1000 ml) HCl + 1 mL (1000 ml) distilled water Record the pH of this tube, here: ______ Test tube P3: Add 1 mL (1000 ml) albumin + 1 mL (1000 ml) pepsin + 1 mL (1000 ml) distilled water Record the pH of this tube, here: ______ Test tube P4: Add 1 mL (1000 ml) albumin + 1 mL HCl (1000 ml) + 1 mL pepsin (1000 ml) Record the pH of this tube, here: ______ 1. Are the results of this experiment consistent with what you know about pepsin? ________________________ 2. List some possible experimental errors that may have influenced your results.
- answer the following questions 1.What is the wavelength used for the spectrophotometer? What is the principle of the spectrophotometer? 2.What is the reagent used to detect glucose in the oh and temperature experiments? What is its principle?3.What is the optimum temperature for invertase reactions?4.What is the optimum ph for the invertase reactions?John was not paying attention and accidently placed the 5% starch solution in test tube 9 instead of albumin. After incubation and addition of 5ml Biuret reagent, there was no color change in the solution. Why didn’t the pepsinogen act on the 5% starch solution even though HCL was present? Consider the structure and function of an enzyme in your answer.My question is: Could you explain steps? (etc. why do we heat or add chemicals like nacl or ammonium sulphate?) 1)Casein Isolation from MilkExperimental Procedure* Put 100 ml of milk in a 500 ml beaker and heat it to 40 0C. * Also heat 100 ml acetate buffer and slowly add it to the beaker with milk while stirring. * The final pH of the mixture should be 4.8. * Cool the suspension to room temperature and wait 5 more minutes before filtering. * Wash the precipitate several times with small volumes of water and then suspend it in approximately 30 ml of ethanol.Filter the suspension in the buchner funnel and wash the precipitate a second time with a mixture of equal proportions of ethanol and ether. * Finally, wash the precipitate on filter paper with 50 ml of ether and soak and dry. * Make the ether evaporate by spreading the powder. * Weigh the casein and calculate the percentage yield of the protein. * Compare with theoretical yield of 3.5 g per 100 ml milk. 2)Purification of Egg…
- Write your correct observations and inferences/conclusions for each of the following: Digestion of Proteins Test Sample Observations Egg + Water + 0.1 M HCl Egg + 2% pepsin + 0.1 M HCl Egg + 2% pepsin + water A1. Identify the substrate(s), enzyme(s) and hydrolysis products in the digestion of protein. Represent your answer using a general chemical equation. A2. Why does a person with low production of stomach HCl will have difficulty in digesting proteins? A3. Name the sites and enzymes present that helps digest proteins in our body?Question 1 i. Discuss 4 effects of heat on food. ii. Distinguish between caramelization and maillard reactions giving an example of each.An enzyme is present at 100 nM (nanomolar) and has a Vmax value of 25 uM/s (micromolar/second). The Km for the substrate is 5.2 uM. What is the kcat value? Report your answer to three significant figures in units of 1/s. Do NOT include the units in your answer.
- Enzyme 1 is Aconitase and the starting material goes through both the hydration and dehydration mechanism. I just need help with enzyme 2 and intermediate B, thank youANSWER BOTH QUESTIONS 1. Enzyme are classified into how many major groups and systematically named by how many numbers separated by dots? A. 4 groups and 6 numbers, respectively B. 6 groups and 4 numbers, respectively C. 4 groups and 4 numbers, respectively D. 5 groups and 2 numbers, respectively 2. Which of the following can cause the rate of enzyme activity to increase? I. Increasing the temperature starting from the optimum temperature II. Increasing the temperature until it reaches the optimum temperature III. Decreasing the temperature starting from the optimum temperature IV. Decreasing the temperature until it reaches the optimum temperature A. I and II only B. I and III only II only C. I and IV only D. II and IV only1. pH cannot affect the enzyme - activity A. True B. False 2. It took 6 mins for the disappearance of blue-black color in test tube 4 with 60 degrees Celsius temperature. A. True B. False