1. Determination of Kinetic Constants in an Inhibited Enzyme Reaction. Biological oxidation of phenylacetic acid is inhibited by propionic acid present in wastewater. The following data were obtained for enzymatic oxidation of phenylacetic acid at different concentrations of propionic acid: a. What kind of inhibition is this? b. Determine Vmax, Km, and KI? Table 1 S (mM) 0.25 0.40 V (mM/1*hr), I = 0 mM 1.0 1.7 V (mM/l*hr), I = 1 mM 0.65 1.1 V (mM/1*hr), I = 2 mM | 0.55 0.9 930 1111 0.50 0.60 0.75 1.00 1.9 2.1 2.4 2.5 1.3 1.4 1.8 2.2 1.0 1.3 1.4 1.8 *mM = millimolar

Introduction to Chemical Engineering Thermodynamics
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1. Determination of Kinetic Constants in an Inhibited Enzyme Reaction.
Biological oxidation of phenylacetic acid is inhibited by propionic acid present in
wastewater. The following data were obtained for enzymatic oxidation of phenylacetic acid
at different concentrations of propionic acid:
a. What kind of inhibition is this?
b. Determine Vmax, Km, and KI?
Table 1
S (mM)
0.25
0.40
0.50
0.60
0.75
1.00
V (mM/1*hr), I = 0 mM
1.0
1.7
1.9
2.1
2.4
2.5
V (mM/l*hr), I = 1 mM
0.65
1.1
1.3
1.4
1.8
2.2
V (mM/1*hr), I = 2 mM
0.55
0.9
1.0
1.3
1.4
1.8
*mM = millimolar
B) → p =
A) Non Competitive Inhibition
CsxVMax
KM + Cs + KMK₂C₁ + K₂CsC₁)
Where
KM = 1.42 & 1 = 0, & Vмax
€ 6.95, & V = -76
K₂ = 0.68 & K₁
=
1.43
Transcribed Image Text:1. Determination of Kinetic Constants in an Inhibited Enzyme Reaction. Biological oxidation of phenylacetic acid is inhibited by propionic acid present in wastewater. The following data were obtained for enzymatic oxidation of phenylacetic acid at different concentrations of propionic acid: a. What kind of inhibition is this? b. Determine Vmax, Km, and KI? Table 1 S (mM) 0.25 0.40 0.50 0.60 0.75 1.00 V (mM/1*hr), I = 0 mM 1.0 1.7 1.9 2.1 2.4 2.5 V (mM/l*hr), I = 1 mM 0.65 1.1 1.3 1.4 1.8 2.2 V (mM/1*hr), I = 2 mM 0.55 0.9 1.0 1.3 1.4 1.8 *mM = millimolar B) → p = A) Non Competitive Inhibition CsxVMax KM + Cs + KMK₂C₁ + K₂CsC₁) Where KM = 1.42 & 1 = 0, & Vмax € 6.95, & V = -76 K₂ = 0.68 & K₁ = 1.43
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