For a test of enzyme-catalyzed kinetics, the following data were recorded 0 product (°C) (mmoVmL) (mmol/mL-min) 30 0.1 30 0.033 30 0.02 30 0.01 30 0.005 49.6 0.1 49.6 0.033 49.6 0.01 49.6 0.0067 49.6 0.005 2.63 1.92 1.47 0.96 0.56 5.13 3.70 1.89 1.43 1.11 a. Determine the M-M constants (VMAx and KM) and the specific rate of product formation (kcaT) for the reaction at 30 oC and at 49.6 °C. Use the Lineweaver-Burke plot to determine the constants, b. Demonstrate the effect of the temperature change from 30 °C to 49.6 °C by plotting the measured reaction rate vs. the substrate concentration (a plot of the M-M curves). Indicate that the enzyme activity is in the temperature activation region or in the temperature deactivation region
For a test of enzyme-catalyzed kinetics, the following data were recorded 0 product (°C) (mmoVmL) (mmol/mL-min) 30 0.1 30 0.033 30 0.02 30 0.01 30 0.005 49.6 0.1 49.6 0.033 49.6 0.01 49.6 0.0067 49.6 0.005 2.63 1.92 1.47 0.96 0.56 5.13 3.70 1.89 1.43 1.11 a. Determine the M-M constants (VMAx and KM) and the specific rate of product formation (kcaT) for the reaction at 30 oC and at 49.6 °C. Use the Lineweaver-Burke plot to determine the constants, b. Demonstrate the effect of the temperature change from 30 °C to 49.6 °C by plotting the measured reaction rate vs. the substrate concentration (a plot of the M-M curves). Indicate that the enzyme activity is in the temperature activation region or in the temperature deactivation region
Introduction to Chemical Engineering Thermodynamics
8th Edition
ISBN:9781259696527
Author:J.M. Smith Termodinamica en ingenieria quimica, Hendrick C Van Ness, Michael Abbott, Mark Swihart
Publisher:J.M. Smith Termodinamica en ingenieria quimica, Hendrick C Van Ness, Michael Abbott, Mark Swihart
Chapter1: Introduction
Section: Chapter Questions
Problem 1.1P
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![For a test of enzyme-catalyzed kinetics, the following data were recorded
0
product
(°C) (mmoVmL) (mmol/mL-min)
30 0.1
30 0.033
30 0.02
30 0.01
30 0.005
49.6 0.1
49.6 0.033
49.6 0.01
49.6 0.0067
49.6 0.005
2.63
1.92
1.47
0.96
0.56
5.13
3.70
1.89
1.43
1.11
a. Determine the M-M constants (VMAx and KM) and the specific rate of product formation (kcaT) for the
reaction at 30 oC and at 49.6 °C. Use the Lineweaver-Burke plot to determine the constants,
b. Demonstrate the effect of the temperature change from 30 °C to 49.6 °C by plotting the measured
reaction rate vs. the substrate concentration (a plot of the M-M curves). Indicate that the enzyme activity
is in the temperature activation region or in the temperature deactivation region](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fa542bcb0-f1d3-4680-abac-57a59b839b85%2Fff049418-e226-4850-af37-cca777ef43d3%2F3dum45k.png&w=3840&q=75)
Transcribed Image Text:For a test of enzyme-catalyzed kinetics, the following data were recorded
0
product
(°C) (mmoVmL) (mmol/mL-min)
30 0.1
30 0.033
30 0.02
30 0.01
30 0.005
49.6 0.1
49.6 0.033
49.6 0.01
49.6 0.0067
49.6 0.005
2.63
1.92
1.47
0.96
0.56
5.13
3.70
1.89
1.43
1.11
a. Determine the M-M constants (VMAx and KM) and the specific rate of product formation (kcaT) for the
reaction at 30 oC and at 49.6 °C. Use the Lineweaver-Burke plot to determine the constants,
b. Demonstrate the effect of the temperature change from 30 °C to 49.6 °C by plotting the measured
reaction rate vs. the substrate concentration (a plot of the M-M curves). Indicate that the enzyme activity
is in the temperature activation region or in the temperature deactivation region
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