You are required to isolate, purify and verify the purity of an enzyme from cytosol of a plant
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- There are six classes of enzymes, namely oxidoreductases, transferases, hydrolases, lyases, isomerases and ligases. (i) (ii) Cell disruption is one of the steps performed during enzyme production. Explain the reason of performing cell disruption in enzyme production and provide THREE (3) enzyme extraction methods for this type of enzyme. Explain the principles of gel electrophoresis as one of the methods used for enzyme purification.Pyridoxal phosphate (PLP) is a coenzyme for the enzyme ornithine aminotransferase. The enzyme was purified from cells grow in PLP = deficient media as well as from cells grown in media that contained pyridoxal phosphate. The stability of the two different enzyme preparations was then measured by incubating the enzyme at 37°C for different lengths of time and then assaying for the amount of enzyme activity remaining. The following results were obtained. (a) Why does the amount of active enzyme decrease with the time of incubation? (b) Why does the amount of enzyme from the PLP deficient cells decline more rapidly?To purify a given enzyme from a crude extract that contains it, fractional precipitations, exchange chromatography are successively tested ionic and exclusion chromatography, with the results shown in the following table: Volume of dissolution Protein concentration Enzymatic activity (ml) (mg/ml) (U/ml) a) Calculate the percentage of recovery of the enzyme after each of the manipulations to which it has been subjected. b) Indicate if it is necessary to continue purifying the enzyme or if it is expected to have reached its electrophoretic homogeneity.
- Associate the biochemical reaction in TSI agar to certain genera or species. Reaction Possible Organism(s) K/K K/A K/A, H2S* A/A A/A A/A, H2S*Briefly comment on the differences of using a fixed-time assay versus a kinetic assay to measure enzyme activity. Is it reasonable to assume that the reaction velocity obtained by measuring the amount of product after 30 minutes in a fixed-time assay is directly proportional to absorbance? How could you determine whether this was the case? Word limit 180 words including citation and referenceA technician prepares a buffer solution that will be used to facilitate the optimal pH for an enzyme involved in the biotechnological degradation of organic compounds. The buffer compound will facilitate a stable pH. To prepare the buffer they need to determine the required concentration of anita hara [conjugate acid or base]_08 They have been provided with the buffer parameters provided in the images. Provide the answer to three decimal places and include an appropriate unit. Note: You may need to round the numbers to get the required answer. Final volume of solution: 200 ml VEENER Total buffer compound concentration: 150 mM Ratio conjugate base/weak acid: 1.58/1 2000 Concentration weak acid: 0.058 M Final pH of solution: 6.5 Buffer compound pk.: 6.3 14 13 12 11 10 9
- During the early stages of an enzyme purification protocol, when cells have been lysed but cytosolic components have not been separated, the reaction velocity-versus-substrate concentration is sigmoidal. As you continue to purify the enzyme, the curve shifts to the right. Explain your results. This is an allosteric enzyme and you must use a Lineweaver-Burk plot to determine KM and Vmax correctly. This is an enzyme that displays Michaelis-Menten kinetics and you purify away an inhibitor. This is an allosteric enzyme and during purification you purify away an activator. This is an allosteric enzyme displaying a double-displacement mechanism and during purification you purify away one of the substrates: This is an enzyme that displays Michaelis-Menten kinetics, and you must use a Lineweaver-Burk plot to determine KM and Vmax correctly.Two experiments were performed with the enzymeribonuclease. In experiment 1 the effect of increasingsubstrate concentration on reaction velocity was measured.In experiment 2 the reaction mixtures were identical tothose in experiment 1 except that 0.1 mg of an unknowncompound was added to each tube. Plot the data accordingto the Lineweaver-Burk method. Determine the effect of theunknown compound on the enzyme’s activity. (Substrateconcentration is measured in millimoles per liter. Velocity ismeasured in the change in optical density per hour.)A purified protein sample was used in a reaction, resulting in an activity of 696.7 nmol min-1. The reaction volume was 145.0 µL and the final volume before loading the plate was 1,050 µL. The total reaction time was 4.25 min. The amount of protein used in the reaction was 4.270 µg. Calculate the specific activity of the sample (in nmol min-1 µg-1).
- Studies were carried out to investigate some kinetic properties of alkaline phosphatase (ALP) extracted from Lepus townsendii liver. Incubation of ALP extract with 4- nitrophenylphosphate (4-NPP) formed the basis for determination of enzyme activity. Spectrophotometric method was used to assay the enzyme activity, and the kinetic constants- maximum enzyme velocity (Vmax) and Michealis-Menten constant (Km) were evaluated. Figure 2 shows the Lineweaver-Burk plot of ALP assay in the presence of inhibitor NaH;PO4 (0) and the control (+) analysis. [I]: concentration of inhibitor = 0.67 mM. 1/V, uM*min x 104 40- 30 20 y-Intercept 10 x-intercept -1/K. (1+ [1]/K)/ 12 1/[S)x 102 (M) Figure2 (i) Estimate Km and Vmax in the absence and presence of the inhibitor. (ii) What is the type of inhibition illustrated by the inhibitor? Explain.Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the Vmax value for this reaction. Report your answer to four significant figures in units of uM/min.True or False Immobilization improves the stability of the enzyme. EnaLne, has a half-life of 10 days in free solution, but under identical conditions of temperature, pH, and medium composition, the measured half-life of a packed column is 30 days. The enzyme is immobilized in a porous sphere 5 mm in diameter.