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1. The following data were obtained for an enzyme-catalyzed reaction. Determine Vmax and Km by inspection. Plot the data using the Eadie-Hofstee method and determine these constants graphically. Explain the discrepancy in your two determinations. The initial rate data for the enzyme-catalyzed reaction are as follows: [S] mol/l μmol/min 5.0 × 104 125 2.0 x 104 125 6.0 × 10-5 121 4.0 × 10-5 111 3.0 × 10-5 96.5 2.0 × 10-5 62.5 1.6 x 10-5 42.7 1.0 × 10-5 13.9 8.0 x 106 7.50 2. Describe how varying either Km and Vmax affects the rate of catalysis.

1. The following data were obtained for an enzyme-catalyzed reaction. Determine Vmax and Km by inspection. Plot the data using the Eadie-Hofstee method and determine these constants graphically. Explain the discrepancy in your two determinations. The initial rate data for the enzyme-catalyzed reaction are as follows: [S] mol/l μmol/min 5.0 × 104 125 2.0 x 104 125 6.0 × 10-5 121 4.0 × 10-5 111 3.0 × 10-5 96.5 2.0 × 10-5 62.5 1.6 x 10-5 42.7 1.0 × 10-5 13.9 8.0 x 106 7.50 2. Describe how varying either Km and Vmax affects the rate of catalysis.

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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Chemical Engineering 1. The following data were obtained for an enzyme-catalyzed reaction. Determine Vmax and Km by inspection. Plot the data using the Eadie-Hofstee method and determine these constants graphically. Explain the discrepancy in your two determinations. The initial rate data for the enzyme-catalyzed reaction are as follows: [S] mol/l 5.0 x 104 2.0 × 104 6.0 x 10-5 4.0 x 10-5 3.0 x 10-5 2.0 × 10-5 1.6 × 10-5 1.0 x 10-5 8.0 x 10-6 answer Q2 please V μmol/min 125 125 121 111 96.5 62.5 42.7 13.9 7.50 2. Describe how varying either Km and Vmax affects the rate of catalysis.
Transcribed Image Text:Chemical Engineering 1. The following data were obtained for an enzyme-catalyzed reaction. Determine Vmax and Km by inspection. Plot the data using the Eadie-Hofstee method and determine these constants graphically. Explain the discrepancy in your two determinations. The initial rate data for the enzyme-catalyzed reaction are as follows: [S] mol/l 5.0 x 104 2.0 × 104 6.0 x 10-5 4.0 x 10-5 3.0 x 10-5 2.0 × 10-5 1.6 × 10-5 1.0 x 10-5 8.0 x 10-6 answer Q2 please V μmol/min 125 125 121 111 96.5 62.5 42.7 13.9 7.50 2. Describe how varying either Km and Vmax affects the rate of catalysis.
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