4. How much lactic acid (C3H6O3) is produced when 225 g glucose (C6H12O6) is used as substrate in the fermentation. Assuming that the sugar is completely fermented to lactic acid. The molar masses of CsH12Os and C3H6O3 are 180.156 g/mol and 90.08 g/ml, respectively. The chemical reaction of lactic acid fermentation is shown below. (5 pts.) C6H12O6 → 2 C3H6O3

4. How much lactic acid (C3H6O3) is produced when 225 g glucose (C6H12O6) is used as substrate in the fermentation. Assuming that the sugar is completely fermented to lactic acid. The molar masses of CsH12Os and C3H6O3 are 180.156 g/mol and 90.08 g/ml, respectively. The chemical reaction of lactic acid fermentation is shown below. (5 pts.) C6H12O6 → 2 C3H6O3

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

See similar textbooks

Similar questions

Carbonic anhydrase catalyzes the hydration of CO. CO2 + H2O ¬ H½CO3 The Km of this enzyme for CO, is 1.20×104 µ.M. When [CO,] = 3.60×104 µM, the rate of reaction was 4.50 umol·mL! sec-1 a What is Vmax for this enzyme? umol·mL-!sec-!
The lipase substrate emulsion contains 0.500 mg of olive oil per 3 mL Also, the molar mass of the olive oil is 885 g/mol. If all of the olive oil in a 3 mL reaction is "digested" by pancreatic lipase in a reaction, how many molecules of olive oil have been degraded?
Aerobic 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 organisms
The 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.
1. Hydrolysis of 1 M glucose 6-phosphate catalyzed by glucose 6-phosphatase is 99% complete at equilibrium (i.e., 1% of the substrate remains). Which of the following statements is most nearly correct? (R= 8.315 J/mol-K; T = 298 K) A AG" is-11 kl/mol. B) AG" is +5 kJ/mol. C) AG" is 0 kJ/mol. DAG" is +11 kJ/mol. E) AG" cannot be determined from the information given. Explain your choice in one line: -2.16x298 (2) - 11386.15 -> 11.4 КТ 5 The high state conculto alle My negative and st" positive (either for D) then onditions, one
13. Calculate the equilibrium constant K'eg, for each of the following reactions at pH 7.0 and 25°C. glucose + Pi a. Glucose 6-phosphate + H20 enz. Glucose 6-phosphatase; AG'O=-13.8kJ/mol
10) The graph shown below is the pre-steady state data for the serine protease (chymotrypsin) enzyme. Explain how this result suggests the formation of a covalent enzyme intermediate in the active site during the first step in the pathway. 3.0 2.0 1.0 1 3 Time (min) p-Nitrophenol (mol/mol of enzyme) 2.
Pepsin, a peptidase that hydrolyzes proteins, functions in the stomach at an optimum pH of 1.5–2.0. How is the rate of a pepsin-catalyzed reaction affected by each of thefollowing conditions? increasing the concentration ofproteins changing the pH to0 running the reaction at 0°C using lesspepsin
Urease enzyme hydrolysed urea at [S]= 0.03 mmol/L with a Km value of around 0.06 mmol/L. The initial velocity observed was 1.5x103 mmol/L.min1. Calculate the initial velocity of the enzymatic reaction when using [S]= 0.12 mmol/L.
1. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins ofbacterial wall) are 37 C- temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. 2 Consider the matic reaction schee: Asnaragine + H20 Aspartate+ NH3:
5) In an experiment to investigate the inhibition of the enzyme-glucosidase the following data for the rates of reaction with glucopyranoside for various substrate concentrations was obtained. By constructing a Leaver-Burk plot, determine the value of the Michaelis constant. [S]/ (10-6 mol dm-3) v/ (10-3 mol dm-3 s-1) 1.00 2.00 3.00 4.00 16.7 33.3 41.1 49.8
when saturated with substrate, an enzyme has a maximum initial rate of 110mumoles of substrate converted to product per second. At a substrate concentration of 100mu M, the same enzyme converts substrate to product at a rate of 0.010mmoles/ sec. Assuming that Michaelis - Menten kinetics are followed, calculate the reaction rate when substrate concentration is 2x10^-3M.