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Q3. Find the value of the rate constant at 600 K
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- Choices for slope: a. -1.35 x 10^4 b. 1.35 x 10^4 c. -1.09 x 10^4 d. 1.09 x 10^4 choices for y intercept: a. -27.8 b. 27.8 c. 37.4 d. -37.4 choices for pearson: a. -0.962 b. -1000 c. -0.982 activation energy a. 9.06 x 10^4 b. 113 c. 90.65 collision frequency factor A a. 1.15 x 10^12 b. 113 c. 90.65If 5 µM enzyme was used to obtain the data in the summary plot below, V-max = ________________ µM sec-1 and Km = ____________ µM for this enzyme (Enter numeric values to the nearest integer; Do NOT write units.)The following experimental data were collected during a study of the catalytic activity of an intestinalpeptidase with the substrate glycylglycine: Glycylglycine + H2O → 2 glycine [S] (mM) Rate of product formation (mol/min) 1.5 0.21 2.0 0.24 3.0 0.28 4.0 0.33 8.0 0.40 16.0 0.45 Use the graphical analysis (Lineweaver-Burk plot and equation) to determine the Km and Vmax for this enzyme preparation and substrate.
- The first-order degradation rate constant k was determined to be 0.0125/day for contaminant A and 0.0030/day for contaminant B in a soil. Calculate the half-life T1/2 and the 95% dissipation time for these contaminants in the soil. Compare the persistence between the two contaminants.Describe the effect, if any the following procedural errors would have on the calculated value of the Ksp. The undissolved Ca(IO3)2 was disturbed while pipetting out some of the supernatant liquid, allowing some of the solid to be drawn up into the pipet.The adsorption equilibrium isotherm for aqueous phenol solution and activated carbon can be determined from the following data: c kg phenol/m3 solution q kg phenol/kg carbon 0.3220 0.150 0.1170 0.122 0.0390 0.094 0.0061 0.059 0.0011 0.045 Determine the appropriate isotherm for this experimental run
- 0% 25% 50% 75% 100% Depth of H2O2 Solution (d) 2.1 cm 2.1 cm 2.1 cm 2.1 cm 2.1 cm Trial 1 Time 180 sec 84.61 sec 43.52 sec 36.90sec 25.90 sec Trial 2 Time 180 sec 92.25 sec 38.16 sec 34.36 sec 23.57sec Trial 3 Time 32.53 sec 18.82 sec Average Time (t) 180 sec 88.43 sec 40.84 Sec 34.5 sec 22.76 sec Rate of the Reaction(R = d/t) 0.012 cm/sec 0.02 cm/sec 0.051 cm/sec 0.061 cm/sec 0.0923cm/sec , graph rate of reaction on the y-axis and percent concentration of enzyme on the x-axis. If the points are linear, draw a “best-fit” straight line through or near all of the data points. Based on the information in the data table and your graph, explain the relationship between percent concentration of catalase and rate of reaction. Did your actual results match your hypotheses? If not, why?Benzene is dissolved at a constant initial concentration of 350 mg/l and is contained within a landfill in leachate water above bottom liner of the landfill system. It starts to diffuse through the liner at time t = 0. Using Equation Ci (x,t) = Co erfc x/ 2(D*t)0.5 related narrative, and (error function table), calculate the concentration of benzene at its breakthrough location as it diffuses through a 1.5 meter thick liner (x=1.5 meters represents breakthrough location where liner fails of contaminant is released), after 50 years. Assume D = 10-5 m2/sec (diffusion coefficient in free standing water) and w = 0.7 (coefficient of tortuousity). Clearly present your assumptions and your value of erf, Select the answer range which best fits the answer you calculate. Group of answer choices 315 to 350 mg/l My answer is not in the range of any of the choices my answer. 215 to 314 mg/l 175 to 200 mg/l 370 to 400 mg/lShow all steps leading to the final answer po. Here’s a pdf file in accordance with the topic po: https://drive.google.com/file/d/1_FnDtXCrFKSol3RNWIG_9tNQ7IxgxD6t/view?usp=drivesdk
- Using the kinetic data pictured, estimate Vmax and Km for the catalysis of Substrate 1 by the following enzyme (using the correct units).You are trying to come up with a drug to inhibit the activity of an enzyme thought to have a role in liver disease. In the laboratory the enzyme was shown to have a Km of 1.0 x 10-6 M and Vmax of 0.1 micromoles/min.mg measured at room temperature. You developed an uncompetitive inhibitor. In the presence of 5.0 x 10-5 M inhibitor, the apparent Vmax was determined to be 0.02 micromoles/min.mg. What is the Ki of the inhibitor?If the enzyme lactase has a Vo of 0.111111111111 mM per minute when [S] = 1.0 mM, and a Vo of 0.20 mM per minute when [S] = 5.0 mM, what is its Km? Calculate Vmax of the above enzyme (lactase). Calculate the slope on a Lineweaver-Burk plot (Km/Kmax) for the above enzyme (lactase).