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Tutorial 4 Answers

The document contains tutorial questions and answers related to Engineering Biotechnology, focusing on enzyme kinetics and the Arrhenius equation. It includes data tables for Vmax at different temperatures, calculations for activation energy, and the derivation of the Michaelis-Menten equation. Additionally, it discusses the Lineweaver-Burk plot and evaluates kinetic parameters for enzymes using glucose or xylose as substrates.

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34 views6 pages

Tutorial 4 Answers

The document contains tutorial questions and answers related to Engineering Biotechnology, focusing on enzyme kinetics and the Arrhenius equation. It includes data tables for Vmax at different temperatures, calculations for activation energy, and the derivation of the Michaelis-Menten equation. Additionally, it discusses the Lineweaver-Burk plot and evaluates kinetic parameters for enzymes using glucose or xylose as substrates.

Uploaded by

shumbataffy5
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd

Abdullatif Alfutimie Engineering Biotechnology Tutorial sheet 4

Q1

Q2

From Lecture 4 part 4 video at 6:44 minutes, you can conclude that

1
Q3

According to the Arrhenius equation, a plot of vmax versus 1/T on semi-logarithmic


coordinates should give a straight line. T is converted to kelvin. The parameter values are
listed and plotted below.

T (°c ) Vmax (mmol l–1 min–1) T (k) 1/t (k-1 ) ln 𝑉𝑚𝑎𝑥

30 456 303.15 0.003299 6.122493


45 1250 318.15 0.003143 7.130899
50 1590 323.15 0.003095 7.371489
60 2900 333.15 0.003002 7.972466

6
y = -6201x + 26.587
Ln (Vmax )

5
R² = 0.9989
4

0
0.00295 0.003 0.00305 0.0031 0.00315 0.0032 0.00325 0.0033 0.00335
1/T x 103 (K-1)

2
𝐸𝑎 1
ln 𝑉𝑚𝑎𝑥 = − ∗ + ln 𝐴
𝑅 𝑇
Therefore, Ea/R = 6201 K.

R = 8.3144 J k-1 gmol -1 = 8.3144 10–3 kJ k-1 gmol -1.

Therefore, E = 6201 K 8.3144 10-3 kJ k-1 gmol-1 = 51.6 kJ gmol -1.

A = 3.52 × 1011 mmol l-1 min-1.

The activation energy E is 51.6 kJ gmol-1; the Arrhenius constant A = 3.52 × 1011 mmol l-1 min-1

55C = (55 + 273.15) K = 328.15 K.

Applying the equation derived in (b) to evaluate Vmax

Ln Vmax=-6201x (1/328.15)+26.587=7.697

Vmax=2186.711

Q4

Please watch the video of lecture 4 part 4 for the derivation of Michaelis–Menten equation

Q5

MUG concentration Enzymic reaction rate, v 1/[MUG] 1/v


(mM) pmol MU/min
0.2 3.8 5 0.263
0.4 6.04 2.5 0.166
0.8 8.81 1.25 0.114
1.2 9.92 0.83 0.101
1.4 10.54 0.625 0.095
Plot the Lineweaver-Burk relationship:

From the intercept (or the slope): 1/vm = 0.068 and hence vm= 14.7 pmol min–1
–1/Km = –1.75 and hence Km=0.57 Mm

3
Q6

4
Q7

The kinetic parameters for the enzyme using glucose or xylose as substrate are evaluated by
plotting s/v versus s as Langmuir plots. The values are listed and plotted below.

5
𝑉𝑚
𝐾𝑐𝑎𝑡 =
E𝑡
𝑉𝑚
Therefore: 𝑐𝑎𝑡𝑎𝑙𝑦𝑡𝑖𝑐 𝑒𝑓𝑓𝑖𝑐𝑖𝑒𝑛𝑐𝑦 = 𝐸
𝑇 𝐾𝑚

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