QUESTION 1
One of the major concerns in fermented foodstuff is the presence of urethane in their products, as this compound is known to be carcinogenic. Therefore, the removal of urea, a precursor of urethane, must be achieved efficiently to comply with governmental limiting levels of urethane. One of the most common processes for the removal of urea in the industrial production of alcoholic beverages is the use of urease enzyme.
Using 10 g∙dm-3 of urease, initial laboratory tests have determined the effect of urea concentration on the rate of the degradation reaction at 30 °C, and the following data was obtained:
Urea substrate concentration, [S] (kmol m-3) |
0.100 |
0.200 |
0.500 |
1.000 |
Initial reaction rate, r (kmol m-3 s-1) |
8.333 |
9.090 |
9.615 |
9.803 |
Calculate the kinetic parameters of this enzyme reaction (Vm and Km) in the initial laboratory tests.
MCQ Options:
Vm = 10 kmol m3 Km = 0.02 kmol m-3 s-1 |
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Vm = 1 kmol m3 Km = 0.2 kmol m-3 s-1 |
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Vm = 10 mol m3 h-1 Km = 0.02 mol m-3 |
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Vm = 10 kmol m3 s-1 Km = 0.02 kmol m-3 |
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Vm = 0.1 kmol m3 s-1 Km = 0.002 kmol m-3 |
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Vm = 0.1 mol m3 h-1 Km = 0.04 mol m-3 |
2. Calculate the time needed to degrade 99% of the urea in a 0.5 dm3 solution in a batch reactor, at 30 °C, in the presence of urease. The initial concentration of urea in the reactor is 0.1 mol∙dm-3 and the urease concentration is 2∙10-4g∙dm-3.
MCQ Options:
29.62 mins |
||
29.62 seconds |
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4.83 x 10-4 mins |
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4.83 mins |
||
15.92 mins |
||
48.35 mins |
QUESTION 1 One of the major concerns in fermented foodstuff is the presence of urethane...
4. An enzyme hydrolyzed a substrate concentration of 0.03mmol/L, the initial velocity was 0.5 X 10-3 mmol/L.min' and the maximum velocity was 4.5 x 10-3 mmol/L.min.l. Calculate the Km value. 5. Urease hydrolyzed urea at [s]=0.03mmol/L with a km of 0.06 mmol/L. The initial velocity observed was 1.5X10-3 mmol/L.min-1 Calculate the maximum velocity of the enzyme reaction.
6. An enzyme with a km of 0.06mmol/L hydrolyzed a substrate of a concentration 0.03 mmol/L. The initial velocity ws 0.0015 mmol/L.min!. Calculate the substrate concentration which gives an initial velocity of 0.003 mmol/L. min-1 7. Urease hydrolyzed urea at [s]=0.03mmol/L with a km of 0.06 mmol/L. The initial velocity observed was 1.5X10-3 mmol/L.min Calculate the initial velocity of the enzyme reaction when using [s]=0.12mmol/L
The Michaelis constant for urease at room temperature is 2.0 mM, and k2-2.5x 104 s-1 at phH 7.5. Calculate the initial rate of the reaction when the urea concentration is 0.025 mM and the urease concentration is 7.O uM 1.8 x 10-3 M s1 O 2.2 x 10-3 M s1 3.4 x 10-3M s1 5.7 x 10-3 M s-1 Question 4 (2 points) The rate constant for a pseudo-first-order reaction is 0.122 s1. Find the initial concentration of the reactant...
PROBLEM 1 The elementary liquid phase irreversible reaction (A + B -> C) is to be carried out in a flow reactor. An equimolar feed with A and B enters the reactor at 300K at a volumetric flow rate of 2 L/s, and feed molar concentration of A equal to 0.1 kmol/m3 a. A. Calculate the conversion of A that can be achieved in one 500 Liter Mixed Flow Reactor under adiabatic conditions. b. Calculate the conversion of A that...
10.What type of inhibitor is this? How do you know? (2)
11.For your assigned inhibitor 1, what are the apparent Km &
Vmax? (NOTE: apparent Km& Vmax are just the Km & Vmax in
presence of inhibitor, at a given concentration.) (2)
Kinetics experiments were performed on PGI. Enzyme activity
(initial velocity, Vo) was measured at varying concentrations of
Glucose-6-phosphate (G6P). The enzyme concentration used in all
experiments was 1.5 μM.
12.What will be the reaction rate with 0.500 mM...
C370S19HW3 Name Please attach your plots to this sheet and turn in your work on Monday June 3 The enzyme urease catalyzes the hydrolysis of urea. 1. (3) Write the reaction catalyzed by Urea below: 2. (2) Of the 7 classes of Enzymes, which type is urease? 3. The rate of this reaction was determined for a series of solutions in which the concentration of urea was changed while maintaining a fixed urease concentration of 3.0 HM. The following data...
1. M. L. Bender and T. H. Marshall [J. Am. Chem. Soc., 90, 201(1968)] studied the elastase-mediated hydrolysis of p-nitrophenyl trimethylacetate to produce p-nitrophenol. These authors have proposed the following mechanism for this reaction: k. k2 E A ES where S, the substrate, is p-nitrophenyl trimethylacetate; P, the product, is p-nitrophenol; and A is trimethylacetiç acid. k,= 150 m3mole-ksec and k2= 2.60 ksec1. (a) Derive an equation for the rate of production of species P in terms of ki, k2,...
1. The kinetics of an enzyme was examined at various substrate concentrations in both the presence and absence of 3 mM inhibitor Z. The initial velocity data obtained are shown below: [S] (mmoles liter) v (mmoles"litermin) no inhibitor inhibitor Z 1.25 1.67 2.50 5.00 10.0 1.72 2.04 2.63 3.33 4.17 0.98 1.17 1.47 1.96 2.38 (4 pts) Estimat e Vmax and Kw in the presence and absence of inhibitor using the Michaelis Menton curve-fitting program on Kaleidagraph (see lab manual)....
Can you do b part in detail?
1. M. L. Bender and T. H. Marshall [J. Am. Chem. Soc., 90, 201(1968)] studied the elastase-mediated hydrolysis of p-nitrophenyl trimethylacetate to produce p-nitrophenol. These authors have proposed the following mechanism for this reaction: k. k2 E A ES where S, the substrate, is p-nitrophenyl trimethylacetate; P, the product, is p-nitrophenol; and A is trimethylacetiç acid. k,= 150 m3mole-ksec and k2= 2.60 ksec1. (a) Derive an equation for the rate of production of...
ngs you will do during the next m P-16, What is wrong with this solution? The ieversible liquid phase second ative thinking skills. that will increase your cre- order reaction kC is carried out in a CSTR、The entering concentration of A, CAP is 2 molar. and the exit concentration of A. CA is 0.1 molar. The volumetric flow rate, v is constant at 3 dm/s. What is the corresponding reactor volume? Solution 1. Mole Balance 3 dm 2 molA 6...