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For a test of enzyme-catalyzed kinetics, the following data were recorded product (mmol/mL) (mmol/mL-min) 30 0.1 0 0.033 30 0.02 30 0.01 30 0.005 49.6 0.1 9.6 0.033 49.6 0.01 9.6 0.0067 49.6 0.00:5 2.63 1.92 1.47 0.96 0.56 5.13 3.70 1.89 1.43 1.6 1.6 1.6 a. Determine the M-M constants (MAx and KM) and the specific rate of product formation (kCAT) for the reaction at 30 °C 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 oC 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 product (mmol/mL) (mmol/mL-min) 30 0.1 0 0.033 30 0.02 30 0.01 30 0.005 49.6 0.1 9.6 0.033 49.6 0.01 9.6 0.0067 49.6 0.00:5 2.63 1.92 1.47 0.96 0.56 5.13 3.70 1.89 1.43 1.6 1.6 1.6 a. Determine the M-M constants (MAx and KM) and the specific rate of product formation (kCAT) for the reaction at 30 °C 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 oC 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
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
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For a test of enzyme-catalyzed kinetics, the following data were recorded product (mmol/mL) (mmol/mL-min) 30 0.1 0 0.033 30 0.02 30 0.01 30 0.005 49.6 0.1 9.6 0.033 49.6 0.01 9.6 0.0067 49.6 0.00:5 2.63 1.92 1.47 0.96 0.56 5.13 3.70 1.89 1.43 1.6 1.6 1.6 a. Determine the M-M constants (MAx and KM) and the specific rate of product formation (kCAT) for the reaction at 30 °C 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 oC 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.
Transcribed Image Text:For a test of enzyme-catalyzed kinetics, the following data were recorded product (mmol/mL) (mmol/mL-min) 30 0.1 0 0.033 30 0.02 30 0.01 30 0.005 49.6 0.1 9.6 0.033 49.6 0.01 9.6 0.0067 49.6 0.00:5 2.63 1.92 1.47 0.96 0.56 5.13 3.70 1.89 1.43 1.6 1.6 1.6 a. Determine the M-M constants (MAx and KM) and the specific rate of product formation (kCAT) for the reaction at 30 °C 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 oC 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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