In an experiment where you use different concentrations of avocado catalase to determine how that affects rate of the reaction with its substrate, hydrogen peroxide, why was the amount(concentration) of peroxide kept the same for all tubes? Why was the total volume of every tube 10cm?
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- For an experiment where you use different concentrations of avocado catalase to determine how it affects the rate of reaction with its substrate, hydrogen peroxide, what would be the independent variable? What would be the dependent variable?You set up the following two tubes: Tube 1: 1mL of alkaline phosphatase + 4mL of 400 µM p-NPP Tube 2: 1mL of alkaline phosphatase + 4mL of 200 µM p-NPP Which tube would have a faster reaction rate? Explain your reasoning (why does concentration of p-NPP matter? Relate it back to week 4 lab concepts). Week 4 lab concepts: - concentration gradient - differentially permeable membrane - solute, solvent, diffusion, osmosis, hypotonic, isotonic, hypertonic, molarity, osmolarityFor an experiment where you use different concentrations of catalase to determine how that affects rate of the reaction with its substrate, hydrogen peroxide, what effect does enzyme concentration have on reaction activity? Would it be possible to have too much catalase in the tube? What would happen?
- For an experiment that uses different concentrations of avocado catalase to determine how it affects the rate of the reaction with hydrogen peroxide, what type of graph would be appropriate for the results?An enzyme that catalyzes the reaction X ⇌ Y is isolated from two bacterial species. The enzymes have the same Vmax but different Km values for the substrate X. Enzyme A has a Km of 2.0 μM, and enzyme B has a Km of 0.5 μM. The plot below shows the kinetics of reactions carried out with the same concentration of each enzyme and with [X] = 1 μM. Which curve corresponds to which enzyme? Explain.An enzymatic reaction was carried out in a batch-operated reactor until exhaustion of the substrate. The formation of the product was monitored over time, obtaining the results shown in Table 1. Answer: a) Knowing that the initial substrate concentration was 0.2 M and that the stoichiometry reaction is: 1S –> 2P, estimate the substrate concentration over time from the data from [P] data in Table 1; b) Determine the parameters of the Michaelis-Menten equation, Vmax and Km, by fitting direct from the hyperbola function; c) Determine the parameters Vmáx and Km, by the linearized equation;
- An enzyme is found that catalyzes the reaction X ⇌ Y. Researchers find that the Km for the substrate X is 4 μM, and the kcat is 20 min−1.(a) In an experiment, [X] = 6 mM, and V0 = 480 nM min−1. What was the [Et] used in the experiment?(b) In another experiment, [Et] = 0.5 μM, and the measured V0 = 5 μM min−1. What was the [X] used in the experiment?(c) The compound Z is found to be a very strong competitive inhibitor of the enzyme, with an α of 10. In an experiment with the same [Et] as in (a), but a different [X], an amount of Z is added that reduces V0 to 240 nM min−1. What is the [X] in this experiment?(d) Based on the kinetic parameters given above, has this enzyme evolved to achieve catalytic perfection? Explain your answer briefly, using the kinetic parameter(s) that define catalytic perfection.in clinical chemistry, are enzymatic methods for determining glucose, cholesterol and uric acid more preferred than non-enzymatic methods? in microbiology, are there technologies that can help make bacterial culture and sensitivity done faster?Which two enzyme curves would be generated from a themophilic bacteria that lives in a strongly acid environment? Please provide a supportive statement about why you picked each of the two curves you picked. Your answer should include information from the graphs. (a) 3 5 MA A 100 7 8 20 2 40 60 Temperature (°C) I 80 ➤ (b) 1 2 3 4 PH 5 6 ➤ 9 10
- In the isolation of glycogen from liver, why it is necessary to filter the solution while it is still hot? Explain in 1-3 sentencesAn enzyme is found that catalyzes the reaction X = Y. Researchers find that the Km for the substrate X is 4 µM, and the kcat is 20 min-1. (a) In an experiment, [X] = 6 mM, and Vo = 480 nM min¬1. What was the [E] used in the experiment? (b) In another experiment, [E] = 0.5 µM, and the measured Vo = 5 µM min1. What was the [X] used in the experiment? (c) The compound Z is found to be a very strong competitive inhibitor of the enzyme, with an a of 10. In an experiment with the same [E] as in (a), but a different [X], an amount of Z is added that reduces Vo to 240 nM min. What is the [X] in this experiment?What would the activity of a lysozyme sample be if it was able to change the absorbance of a cell wall substrate sample from 0.815 to 0.610 in 45 seconds?