Determine the extent of advantage in terms of G factor reduction if a kraft cooking temperature is reduced from 1700C to 1650C, keeping the target H factor constant at1200 (at the cooking temperature) in both cases. The activation energies for the two processes are 32 and 40.3 kcal/mole.
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Determine the extent of advantage in terms of G factor reduction if a kraft cooking temperature is reduced from 1700C to 1650C, keeping the target H factor constant at1200 (at the cooking temperature) in both cases. The activation energies for the two processes are 32 and 40.3 kcal/mole.
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- What would be the standard free energy change if FADH 2 is used to reduce O 2 to water? Standard reduction potential values to be used for calculations.Calculate the reduction potential of cytochrome a3 (°' = 0.385 V) at 25.0°C when the Fe3+ form = 87.0 μM and the Fe2+ form = 25.0 μM. 0.440 V 0.353 V 0.417 V 0.387 VFrom your Lineweaver-Burk plot,the vlaues are: Km Vmax Uninhibited 0.09 mmol/L 3.02 min/mmol Inhibited 6.22 mmol/L 9.98 min/mmol By describing the potential changes in the kinetic parameters, identify and justify the type of inhibitor that was inhibiting the acid phosphatase activity.
- What would be the standard free energy change if FADH 2 is used to reduce O 2 to water? Standard reduction potential values to be used for calculations. BIU (.a >5 €. Σ FMAerobic degradation of an organic compound by mixed cultureof organism in wastewater can be represented by following reaction. C3H6O3 + a O2 + b NH3 → c C5H7NO2 + d H2o + e CO2 A. Determine a, b, c, d and e, if YX/S = 0.4 d X/g S. B. Determine the yield coefficients YX/O2 and YX/NH3. C. Determine the degree of reductions for the substrate, bacteria and RQ for the organismsThe effect of temperature on the hydrolysis of lactose by a ß-galactosidase is shown below in Table 1. The temperature coefficient, Q10 is the factor by which the rate increases by raising the temperature 10°C. The universal gas constant, R is 8.314 J/mol.K. (a) (b) Table 1: Data of Vmax over temperature T (°C) 20 30 35 40 45 Vmax (umoles/min.mg protein) 4.50 8.65 11.80 15.96 21.36 Plot the graph of In Vm vs 1/T using any spreadsheet software (include all appropriate labels and equation). Calculate the activation energy Ea and temperature coefficient Q10.
- What is time constant ? The steel ball bearings of 40 mm diameter and initially at uniform temperature of 600 °C are quenched in an oil bath maintained at 50 °C temperature. The heat transfer coefficient between the ball bearing and oil is 325 W/m2-K and the thermodynamics properties of the bearing can be taken as : k 45 W/m-K and thermal diffusivity a = 1.25 x 10-5 m/s. Determine : The time duration for which bearing must remain in oil to attain 225 °C temperature. b. The instantaneous heat transfer rate from the bearings when they are first immersed in oil and when they reach 225 °C.What is Thomas Slope Method. Why is it used to determine Biochemical Oxygen Demand (BOD) reaction rate constant, K? Based on your findings, please derive the linearized equation for the estimation of the reaction rate constant, K.Determine the Ki for the inhibitor at 30 °Cand decide what type of inhibitor is being used. Eo T I S V (g/I) (°C) (mmol/ml) (mmol/ml) (mmol/ml-min) 1.6 30 0.1 2.63 1.6 30 0.033 1.92 1.6 30 0.02 1.47 1.6 30 0.01 0.96 1.6 30 0.005 0.56 1.6 49.6 0.1 5.13 1.6 49.6 0.033 3.70 1.6 49.6 0.01 1.89 1.6 49.6 0.0067 1.43 1.6 49.6 0.005 1.11 0.92 30 0.1 1.64 0.92 30 0.02 0.90 0.92 30 0.01 0.58 0.92 30 0.6 0.1 1.33 0.92 30 0.6 0.033 0.80 0.92 30 0.6 0.02 0.57
- You make reaction progress curve by plotting absorbance vs time (seconds) and find the equation of the line to be y = -0.00235x + 0.7129. Calculate the U/µL and U/mL of lactate dehydrogenase activity in this fraction. The LDH activity is done identical to what is indicated in the lab manual. Show each step of the calculation from AU/time to M/min, to mol/min, to µmol/min to µmol/min/µL (=U/µL).What is the Vmax of an enzyme at 1 µM with an activation free energy (AG#) of 55000 J/mol at 298K? -AG # RT k cat = 6.2× 10¹² (Ideal gas constant R = 8.314 J K¯1 mol-¹1) 0.14 μM s-1 -1 S-1 1.4 μM s 14 μM s-1 0.14 mM s-1 1.4 mM s-1Please provide an explanation for how to work through this practice problem: Using table 12.1, calculate the free energy change for the synthesis of ATP from cAMP and inorganic phosphate. (Note: cAMP is hydolyzed to AMP, and the free engery of hydrolysis for ATP and ADP is approximately equal.) Table 12.1: (Compound: Change in Free Energy in kJ/mol) cAMP: -50.4 Creatine phosphate: -43.3 ATP: -30.5 Glucose 6-phosphate: -13.9 AMP: -9.2