Container-1 starch The amount of substrate amylase water pH=7,8+ temperature -2 °C+ Container-2 Container-1 lipid lipase The amount of substrate water pH=7,8 + temperature -60 °C- Container-3 Container-2 Protein Pepsin a) In which containers the reaction takes place? Explain it. Container-1 and 3. b) How should the graphs of change in the amount of substrate and product in the experimental setups be? water pH=2+ temperature -36 "C+ optimal The amount of substrate Container-3
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- Give a complete and well descriptive definition of the following:1.1 Fractional saturation1.2Allostery1.3 Metal activated enzymes 1.4 Metalloenzymes1.5 Acid-base catalysisThe following structure is D-sorbose. Which reagent will oxidize D-sorbose? CH2OH C = 0 Н-С-ОН НО - С - Н Н-С-ОН CH2OH Benedict's reagent None of the above Sodium hydroxide Tollen's reagent Barfoed's reagentEnzyme Urease Chymotrypsin Alcohol Dehydrogenase Lysozyme Enzyme Official Name (write N/A if not applicable) Enzyme Official Number (4 digits) Simple or Conjugated Enzyme (specify cofactor if applicable) Type of Reaction Catalyzed Substrate Optimum pH Optimum Temperature Function/s Disease (give 1 and describe briefly)
- Given the active site diagram below, indicate the mechanism(s) of catalysis. 5 HO OH HN OH ΝΗ *HN ΝΗ Zn²+ Acid-base, Metal ion 3 Metal ion, By Approximation Metal ion Acid-Base, By Approximation Acid-baseAn enzymatic reaction follows M-M kinetics with Vmax= 2.5 mol m-3s-1and Km = 5 mM.Calculate the time required for 50% conversion of the substrate in a batch reactor if theinitial substrate concentration is0.2 M.Show your calculation steps.A mixture of dipeptides consisting of Lys-Gly, Thr-His, Ser-Leu, Glu-Gln was applied to column packed with cation-exchange resin at pH 6.0. Which of these dipeptides would be eluted from the column first? O Lys-Gly first O Thr-His first O Ser-Leu first O Glu-Gln first OA mixture of Thr-His and Ser-Leu first
- Populate the table with expected results using color codes (-), (+), (++), and (+++). Table 3. Effect of pH on enzyme activity pH of catechol solution Enzyme Activity pH 1 pH 5 pH 7 pH 10 Conclude by defining optimum pH and stating optimum pH value for PPOGiven the active site diagram below, identify the mechanism(s) of catalysis. 5 2 Metal ion Induced Fit Acid-base HN S is. By Approximation Acid-base, Metal ion -3 45.15. The following data were obtained when glucose (C6H₁2O6) was added to a batch culture of microorganisms. Determine the reaction order for the disappearance of glucose. TIME. min 0 10 20 30 40 50 CONCENTRATION, g/m³ Glucose Cells 100 67 50 40 33 29 1500 1516 1525 1530 1534 1535
- Describe the effect of the following changes would have on the rate of a reaction that involves the substrate UREA and the liver enzyme UREASE 1. Increasing the UREA concentration 2. Increasing the UREASE concentration 3. Increasing the temperature from its optimum value to a value 10degree higher than this value 4. Lowering the pH from the optimum value of 5.0 to a value of 3.0A laboratory technician has been tasked to generate a solution for an enzymatic reaction. The solution needed to contain glutamic acid at a final concentration of 12.25 mM They found a concentrated stock solution in their chemical cabinet and used a measuring cylinder to dilute the stock solution to the desired final volume of the solution.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).