A sample of yeast extract has been analyzed of its invertase activity. The effect of temperature on the invertase activity was monitored using the same dinitrosalicylic acid assay used in your experiment in the laboratory. Refer to the data below. What is the optimum temperature of invertase in deg C?
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- You are studying a biochemical pathway and isolate Neurospora mutants I, II, and III.Mutant I can grow if you supplement the medium with Z.Mutant II can grow if you supplement the medium with X, Y, or Z.Mutant III can grow if you supplement the medium with X and Z, but not with Y. Draw a biochemical pathway that shows the correct order for compounds X, Y, and Z and for the enzymes that each mutant is defective for.Sydney Brenner isolated Salmonella typhimurium mutants that were implicated in the biosynthesis of tryptophan and would not grow on minimal medium. When these bacterial mutants were tested on minimal medium to which one of four compounds (indole glycerol phosphate, indole, anthranilic acid, and tryptophan) had been added, the growth responses shown in the following table were obtained. Mutant Minimal medium Anthranilic acid Indole glycerol phosphate Indole Tryptophan trp-1 − − − − + trp-2 − − + + + trp-3 − − − + + trp-4 − − + + + trp-6 − − − − + trp-7 − − − − + trp-8 − + − − + trp-9 − − − − + trp-10 − − − − + trp-11 − − − − + Give the order of indole glycerol phosphate, indole, anthranilic acid, and tryptophan in a biochemical pathway leading to the synthesis of tryptophan. Indicate which step in the pathway is affected by each of the mutations.Is the following statement correct or incorrect? It is only possible to employ enzymes that are present naturally in yeast or bacteria for biocatalysis.
- The substrate which was used to investigate the enzymatic activity of wheat bran phosphatase was p-nitrophenyl phosphate. It is converted to p-nitrophenol and inorganic phosphate by this enzyme. P-nitrophenol has a pKa of 7.1 and is colorless, while its conjugate base, p-nitrophenolate has a yellow color. The enzyme assay was performed at pH 5.1 after the 0.5 N KOH is added at the end of each enzyme assay, the pH of the assay mixture is raised to 9.1. Why was the base added?A researcher is interested to test the antibacterial activity of a Philippine Plant crude extracts against Beta-lactamase producing Klebsiella pneumonia isolated in a hospital setting. He will use the following concentrations of crude extract, 500mg/ml, 250mg/ml and 100mg/ml. Positive control: Tetracycline 10mg/ml and DMSO as the negative control. Given this research scenario kindly construct a research framework.What reaction would you expect when performing a positive control in the oxidase assay? What would it mean if a known oxidase-positive bacterium did not cause the expected reaction?
- After testing the potency of different β-lactamase inhibitors against purified OXA-M290 enzyme, the antimicrobial activity of combinations of β-lactam antibiotics and β-lactamase inhibitors is tested against the E. coli KGH1 strain that produces OXA-M290. The results of these studies can be used to identify the best antibiotic to treat an infection caused by this E. coli strain. Broth microdilution tests are carried out with a panel of β-lactam antibiotics and β-lactamase inhibitors to determine their MICs against E. coli KGH1. These tests are carried out in a 96-well microplate. Three β-lactam antibiotics (amoxicillin, ceftazidime, and ertapenem) and three β-lactamase inhibitors (sulbactam, tazobactam, and vaborbactam) are tested. The rows in the microplate correspond to the following antibiotics and inhibitors: Row A: amoxicillinRow B: amoxicillin + sulbactamRow C: ceftazidimeRow D: ceftazidime + sulbactamRow E: ertapenemRow F: ertapenem + sulbactamRow G: ertapenem + tazobactamRow H:…For the production of a secondary metabolic by Streptomyces coelicolor, a fed batch was performed. At the end of the single batch phase, the following conditions were reached in the reactor: V=10000L, cell concentration X=10g/L and product concentration P=0.1g/L. The feeding was then started with constant flow F= 200L/h, for 100h. Knowing that the substrate concentration in the feeding medium was SF= 80g/L and in the fermentation medium it was practically null, calculate: a) The final concentration of cells and productb) If the reactor were fed with a constant dilution rate (D), what should be the value of D used to reach the same cell concentration obtained in the situation with constant flow?μp= 0.01 g of product/ (g of cells.h)Y x/s = 0.15g cells/g of substrateGiven this research scenarios kindly construct a research framework. A researcher is interested to test the antibacterial activity of a Philippine Plant crude extracts against Beta-lactamase producing Klebsiella pneumonia isolated in a hospital setting. He will use the following concentrations of crude extract, 500mg/ml, 250mg/ml and 100mg/ml. Positive control: Tetracycline 10mg/ml and DMSO as the negative control.
- For an experiment where you will using different concentrations of avocado catalase to determine how that affects the rate of the reaction with its substrate, hydrogen peroxide, what would be the general protocol? What is the control in the experiment?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?200 ml of a 2% protein solution containing an enzyme that you want to purify. Half of the sample is subjected to method A, consisting of fractionated precipitations and 5 ml of final solution are obtained, with a concentration protein equal to 5 mg / ml and enzymatic activity equal to 2000 U / ml. The other half is subjected to method B, consisting of ion exchange chromatography, and a final solution of 10 ml, with protein richness equal to 10 mg / ml and with an activity enzymatic also equal to 2000 U / ml. You want to know: a) Which of the two methods has provided the purest enzyme. b) By which of the methods the greatest amount of enzyme has been obtained.