A yeast disaccharidase can hydrolyze sucrose and maltose according to the following table: Use Lineweaver-Burk representation to calculate the respective KMs and maximum speeds for each substrate under the conditions of the experiment. Saccharose(mM) Glucose released (µmol10 min) Maltose (mM) Glucose released (µmol10 min) 5 40 5 48 10 60 10 80 20 80 20 120 50 100 50 172 100 109 100 200
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A yeast disaccharidase can hydrolyze sucrose and maltose according to the following table:
Use Lineweaver-Burk representation to calculate the respective KMs and maximum speeds for each substrate under the conditions of the experiment.
Saccharose(mM) |
Glucose released (µmol10 min) |
Maltose (mM) |
Glucose released (µmol10 min) |
5 | 40 | 5 | 48 |
10 | 60 | 10 | 80 |
20 | 80 | 20 | 120 |
50 | 100 | 50 | 172 |
100 | 109 | 100 | 200 |
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- Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the above enzyme (lactase). (enzyme lactase has a Vo of 0.111111111111 mM per minute when [S] = 1.0 mM, and a Vo of 0.20 mM per minute when [S] = 5.0 mM) 0.125 per minute 0.25 per minute 0.50 per minute 1.25 per minute 5.0 per minuteTable 1 shows the kinetic data that have been obtained for glucoamylase from Aspergillus niger at different temperatures in the production of glucose from maltodextrin. The rates of reaction measured are using an enzymes concentration of 0.003 μmolml-1. Outline and describe the reaction scheme of the production of glucose from maltodextrin by using glucoamylase.The yeast S.cerevisae is cultivated for ethanol production in a 10000 L fermenter operated continuously at steady state. The reactor is fed by a 50 g/L of sucrose, with a feed flow of 400 L/h. Assuming that the yeast growth kinetics follow the Monod model and using the following information:Data: μmax= 0.1h-1 ; Ks=0.5g/L; Yx/s=0.15 g/g; Yp/s=0.45g/g. a) What are the concentrations of biomass, sucrose and ethanol at the exit of the fermenter?b) Calculate the productivity in ethanol (Pp) and sketch the curve of variation of Pp vs. dilution rate.c) In terms of ethanol productivity, would it be more or less advantageous if the reactor were operated with a feed rate of 1200L/h? Justify.
- An enzyme has a V of 1.2 uM s The Km for its substrate is 10 µM. max Calculate the initial reaction velocity, Vo, for each substrate concentration, [S]. Calculate Vo when [S] is 2 µM. Vo = µM s Calculate Vo when [S] is 10 µM. Vo = µM s-1 Calculate Vo when [S] is 30 µM. Vo = µM s-1The equil ibrium constant for the attachment of a substrate to the active site of an enzyme was measured as 200.In a separate experiment, the rate constant for the secondorder attachment was found to be 1.5 x 108 dm3 mol-1 s- 1.What is the rate constant for the loss of the unreacted substrate from the active site?Table 1 shows the kinetic data that have been obtained for glucoamylase from Aspergillus niger at different temperatures in the production of glucose from maltodextrin. The rates of reaction measured are using an enzymes concentration of 0.003 μmolml-¹. Table 1: Glucoamylase Activity at different temperatures Maltodextrin Concentration (μmol/L) 0.5 1 1.5 2.2 5.5 11 Initial Reaction Velocity (μmol/L.s) T = 40°C 2.1 3.5 4.9 5.6 589 8.3 9.3 T = 60°C 5.2 9.7 13 16 23 31
- Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) 0.20 per minute 0.50 per minute 1.0 per minute 2.0 per minute 5.0 per minutePenicillin is hydrolyzed and thereby rendered inactive by penicillinase, an enzyme present in some resistant bacteria. The mass of this enzyme in Staphylococcus aureus is 29.6 kd. The amount of penicillin hydrolyzed in 1 minute in 10 ml solution containing 10–9 g of purified penicillinase was measured as a function of the concentration of penicillin. Assume that the concentration of penicillin does not change during the assay. [Penicillin] µM Amount hydrolyzed (nanomoles) 1 0.11 3 0.25 5 0.34 10 0.45 30 0.58 50 0.61 a) Plot V0 versus [S] and 1/V0 1/[S]. Does penicillinase appear to obey Michaelis-Menten kinetics? b) What is the value of KM? c) What is the value of Vmax? d) What is the turnover number of penicillinase under these conditions?A bacterial enzyme catalyzes the hydrolysis of maltose as shown in the reaction given below: Maltose + H2O -> 2 glucose If the reaction has a Km of 0.135 mM and a V max of 65 umol/min. What is the reaction velocity when the concentration of maltose is 1.0 mM? (Please take note of the units)
- Discuss how the equation for enzymatic reaction (given below) was demonstrated in the experimental results in Table 1. Use the appropriate color codes (-), (+), (++), (+++) to describe the expected results in Table 1 Table 1. Enzyme Action MIXTURE ENZYME ACTIVITY Water + catechol (tt A) Enzyme + catechol (tt B) Water + enzyme (tt C)In biological systems, enzymes are used to accelerate the rates of certain bio- logical reactions. Glucoamylase is an enzyme that aids in the conversion of starch to glucose (a sugar that cells use for energy). Experiments show that 1 pg mol of glucoamylase in a 4% starch solution results in a production rate of glucose of 0.6 ug mol/(mL)(min). Determine the production rate of glucose for this system in the units of Ib mol/(ft³)(day). Ibmol Answer: 0.0639 ft day True FalseHexokinase in red blood cells has a Km of approximately 50 µM. What concentration of blood glucose would yield a velocity equal to 90 % Vmax? Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a 500 mM 0.0450 mM 4500 μΜ 5000 µM e 5.0 mM 0.50 mM 450 μΜ 4.5 mM 50 μΜ.