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Practice Questions BBC

The document contains 27 questions related to the topics of enzyme technology and immobilization in biotechnology and biochemical engineering. The questions cover a range of concepts including the effects of heat, inhibitors and pH on enzyme activity; different types of enzyme inhibition; kinetic parameter evaluation; comparison of prokaryotic and eukaryotic cell structures and functions; major biological functions of proteins; enzyme classification; derivation of Michaelis-Menten equations; determination of kinetic constants from rate data; enzyme deactivation kinetics; substrate and product inhibition; mass transfer in biological systems; and methods of enzyme and cell immobilization. Recommended textbooks on biochemical engineering fundamentals and bioprocess engineering are also listed.

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BT20CME033 Gautam Tahilyani
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33 views3 pages

Practice Questions BBC

The document contains 27 questions related to the topics of enzyme technology and immobilization in biotechnology and biochemical engineering. The questions cover a range of concepts including the effects of heat, inhibitors and pH on enzyme activity; different types of enzyme inhibition; kinetic parameter evaluation; comparison of prokaryotic and eukaryotic cell structures and functions; major biological functions of proteins; enzyme classification; derivation of Michaelis-Menten equations; determination of kinetic constants from rate data; enzyme deactivation kinetics; substrate and product inhibition; mass transfer in biological systems; and methods of enzyme and cell immobilization. Recommended textbooks on biochemical engineering fundamentals and bioprocess engineering are also listed.

Uploaded by

BT20CME033 Gautam Tahilyani
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PDF, TXT or read online on Scribd
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SUB:-Biotechnology & Biochemical Engineering (CML386)

Enzyme technology

1. Write on the effect of heat on cell activity.


2. State and explain the action of inhibitors in bioreactions. Develop an expression for the rate of enzymatic
conversion with competitive inhibitors in M-M equation form and sketch a double reciprocal plot to determine
the kinetic parameters.
3. Discuss methods of evaluation of kinetic parameters in the Michaelis-Menten equation.
4. What is enzyme inhibition? Discuss all types of reversible inhibition.
5. Briefly compare prokaryotes with eucaryotes in terms of internal structure and functions.
6. Cite five major biological functions of proteins.
7. What are enzymes ? Discuss with example, the usefulness of enzyme under the head as enzyme vs catalysts.
8. Rate measurements were made on a food enzyme with and without the presence of an inhibitor with the
following results.

[S](mmol/lit) 25 50 75 100 150 200


Without inhibitor V (mmol/lit-min) 8.20 12.86 15.51 17.95 20.02 22.64
With inhibitor V(mmol/lit-min) 5.65 8.16 9.68 11.04 13.56 15.71
Inhibitor concentration, [I]=20mmol.

(i) use the Eadie –Hofstee plot to determine the type of inhibition.

(ii) determine km and Vmax for the enzyme without inhibition and the inhibitor parameter, ki.

9. The following table presents the rates,v(µmol/sec),at which an enzyme converts its substrate to
product.Reaction 1 represents data for the unhibited reaction and Reaction 2 and 3 represent data collected in
the presence of two different inhibitors, each present at 10mmol.Assuming the amount of enzyme is the same
in each case, determine km and Vmax for the enzyme in absence of inhibitors and for each inhibitor determine
ki and type of inhibition.
[S],mmol Reaction 1 Reaction 2 Reaction 3
v,(µmol/sec) (Inhibitor 1) (Inhibitor 2)
v,(µmol/sec) v,(µmol/sec)
1 2.5 1.17 0.77
2 4.0 2.1 1.25
5 6.3 4.0 2.0
10 7.6 5.7 2.5
20 9.0 7.2 2.86
10. Derive an equation for the half life period and enzyme deactivation.
11. Develop suitable mathematical expressions for relationship between substrate concentration and reaction rate
for substrate inhibition reactions.
12. The following data were obtained from enzymatic oxidation of phenol by phenol oxidase at different phenol
concentrations.
S (mg/l) 10 20 30 50 60 80 90 110 130 140 150
v (mg/l-h) 5 7.5 10 12.5 13.7 15 15 12.5 9.5 7.5 5.7
a. What type of inhibition is this?
b. Determine the constants Vm, Km and Ksi.
Determine the oxidation rate at [S] = 70 mg/l.

13. The following data on the substrate removal rate and the substrate concentration is available for some waste
water treatment.
[S](mol) 0.002 0.005 0.02 0.04 0.06 0.08 0.10
Rate, v (mol/min) 0.04 0.115 0.285 0.38 0.46 0.475 0.505
Estimate the value of substrate removal rate constant Km and the value of vmax.

1
14. Rate measurements were made on a food enzyme with and without the presence of an inhibitor with the
following results.

[S](mmol/L) Without inhibitor With Inhibitor V(mmol/L-min)


V(mmol/L-min)
25 8.20 5.65
50 12.86 8.16
75 15.51 9.68
100 17.95 11.04
150 20.02 13.56
200 22.64 15.71
Inhibitor concentration, [I] = 20mmol
i) Use the Eadie-Hofstee plot to determine the type of inhibition.
ii) Determine Km and Vmax for the enzyme without inhibition and the inhibitor parameter, Ki.
15. Discuss the influence of pH, temperature, fluid forces and chemical agents on enzyme activity.
16. What is inhibition? Discuss substrate inhibition in details.
17. Derive the Michaelis –Menten expression for a single substrate enzyme mediated biochemical reaction stating
the assumptions.
18. The following data have been obtained for two different initial enzyme concentrations for an enzyme
catalysed reaction.
E0=0.021g/l
Rate=g/l-min 1.14 0.87 0.70 0.59 0.50 0.44 0.39 0.35
E0=0.00935 g/l
Rate=g/l-min 0.67 0.51 0.41 0.34 0.29 ---- ---- ----
19. De-carboxylation of glyoxalate (S) by mitochondria is inhibited by malonate (I). Using the following data
obtained in batch experiments, determine the following:
a. What type of inhibition is this?
b. Determine the constants Vm, Km and KI .
glyox,[S](mM) Rate of CO2 evolution, v (mmoles/l-h)
[S] 1/[S] I=0 I=1.26 mM I=1.95 mM
0.25 4 1.02 0.73 0.56
0.33 3.030303 1.39 0.87 0.75
0.4 2.5 1.67 1.09 0.85
0.5 2 1.89 1.3 1
0.6 1.666667 2.08 1.41 1.28
0.75 1.333333 2.44 1.82 1.39
1 1 2.5 2.17 1.82

20. The Hydrolysis of urea is an only partially understood reaction shows inhibition. Data for hydrolysis of the
reaction given in Table1, where v=moles/lit-min and I is inhibitor molar concentration. (5)
[S] 0.2M 0.02M
a. Determine the Michaelis –Menten constant for this
v I v I
reaction.
b. What type of inhibition is this? Explain. 4.545 0 1.471 0
c. Determine Ki. 3.030 0.0012 0.980 0.0012
1.961 0.0027 0.667 0.0022
1.316 0.0044 0.546 0.0032
1.136 0.0061 0.490 0.0037
0.909 0.008 0.368 0.0044
0.870 0.0093 0.289 0.0059

2
Immobilization

20. Explain the role of diffusion in bioprocessing.


21. How mass transfer takes place in biological systems? Summarise the mass transfer resistances for the
transport of oxygen from air bubble to microbial cells.
22. What is meant by immobilization of enzymes? Describe different methods of immobilization.
23. Discuss Diffusion Effects in Enzymes Immobilized in a porous matrix. Explain relationship between
Effectiveness factor with particle size and Thiele modulus.
24. Discuss the effect of diffusion in surface bound enzymes on a non porous catalyst support.
25. Explain mechanism of mass transfer and chemical reactions in a symmetric slab of immobilized enzyme.
26. Explain the different methods of immobilization of enzymes, discussing the advantages and disadvantages.
27. Discuss formulation and characterization of immobilized cell biocatalysts.

Books:-

1. Biochemical Engineering fundamentals By Bailey ollis

2. Bioprocess Engineering:-Basic concept by Shuler & Kargi (PHI)

3. Biochemical Engineering:-principles & concepts by Syed Tanveer Ahmed Inamdar(PHI)

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