Anda di halaman 1dari 4

Code No: R05322302 Set No.

1
III B.Tech Supplimentary Examinations, Aug/Sep 2008
ENZYME ENGINEERING
(Bio-Technology)
Time: 3 hours Max Marks: 80
Answer any FIVE Questions
All Questions carry equal marks
⋆⋆⋆⋆⋆

1. What are enzymes? Justify its role as biocatalysts? Discuss in detail. [16]

2. Write in detail about the isolation of intracellular enzymes from plant cells. [16]

3. Derive the Adiar equation for a tetrameric enzyme consisting of identical subunits,
and deduce the relationships between the apparent binding constants required for
the various types of co-operativity. [16]

4. What are substrate and product inhibition? Explain with help of mathematical
model. [16]

5. Discuss about different physical techniques of immobilization of enzymes along with


the different materials and methods commonly employed. [16]

6. (a) What is mass transfer effect.how to increase the mass transfer coefficient in
an immobilized enyme system.
(b) What are the combined effects of bulk substrate concentration and substrate
modulus on the effectiveness factor in immobilized enzyme catalysed reaction.
[8+8]

7. Write a comparative analysis on the the mode of operation of a packed -bed and
fluidized bed reactors. [16]

8. What are enzyme electrodes. Describe the types of electrochemical probes used in
enzyme electrodes. [16]

⋆⋆⋆⋆⋆

1 of 1
Code No: R05322302 Set No. 2
III B.Tech Supplimentary Examinations, Aug/Sep 2008
ENZYME ENGINEERING
(Bio-Technology)
Time: 3 hours Max Marks: 80
Answer any FIVE Questions
All Questions carry equal marks
⋆⋆⋆⋆⋆

1. Discuss in detail the application of enzymes in biotech industries? [16]

2. Write in detail about the isolation of extra cellular enzymes from plant cells. [16]

3. How the order of reaction changes with the reaction times in Michaelis Menton
type of enzyme kinetics? What is the critical point beyond which the change is
more prominent? [16]

4. Discuss about the Eadie-Hofstee and Linewaver-Burk plot in case of competitive


and un-competitive inhibition with help of mathematical model. [16]

5. (a) Write the economic argument for enzyme immobilization.


(b) Write the applications of immobilized enzymes in the food industry. [8+8]

6. (a) Discuss about penetration theory of mass transfer in immobilized enzyme


systems.
(b) Discuss about the conditions that produce an increased probability of external
diffusional control over the rate of an immobilized enzyme catalsyed reaction.
[8+8]

7. What are the types ,modes of operation of different configurations of reactors avail-
able with CSTR. [16]

8. Discuss about different ‘generation’ of biosensors and the advances made at each
stage. [16]

⋆⋆⋆⋆⋆

1 of 1
Code No: R05322302 Set No. 3
III B.Tech Supplimentary Examinations, Aug/Sep 2008
ENZYME ENGINEERING
(Bio-Technology)
Time: 3 hours Max Marks: 80
Answer any FIVE Questions
All Questions carry equal marks
⋆⋆⋆⋆⋆

1. What are the different methods used to assay the purity of protein? [16]

2. Write in detail about the isolation of intracellular enzymes from plant cells. [16]

3. What is an active site of an enzyme? How the active site involves in enzyme
substrate complex formation. Explain in detail about the determination of active
site concentration. [16]

4. (a) Derive the Lineweaver- Burk and Eadie-Hofstee equation from Michalis-Menton
equation in case of non-competitive inhibition.
(b) Derive the Lineweaver- Burk and Eadie-Hofstee equation from Michalis-Menton
equation in case of mixed inhibition. [8+8]

5. Write a Short notes on:

(a) covalent method of enzyme immobilization


(b) Stability of immobilized enzymes
(c) Advantages of immobilization of enzymes
(d) Liposomes as enzyme entrapers. [4+4+4+4]

6. Derive an expression for the effect of external diffusion on the rate of an immobilized
enzyme catalysed reaction on a flat impervious support. [16]

7. Derive a mathematical expression for the rate a reaction within a CSTR. [16]

8. Discuss how enzyme biosensors are superior to conventional biosensors. [16]

⋆⋆⋆⋆⋆

1 of 1
Code No: R05322302 Set No. 4
III B.Tech Supplimentary Examinations, Aug/Sep 2008
ENZYME ENGINEERING
(Bio-Technology)
Time: 3 hours Max Marks: 80
Answer any FIVE Questions
All Questions carry equal marks
⋆⋆⋆⋆⋆

1. What are the criteria to assay the protein purify at each step in protein purification?
Explain in detail. [16]

2. How enzymes are preliminarily purified from a crude enzyme extract? Explain in
detail. [16]

3. Give short notes on the following:

(a) Specificity of enzyme action


(b) Kinetics of single substrate reactions
(c) Turnover number. [16]

4. Discuss allosteric enzymes in terms of cooperativity. [16]

5. (a) Write about the properties of immobilized enzymes.


(b) Write about the carrier matrices used in the adsorption method of immobi-
lization of enzymes. [8+8]

6. Compare the variation of effectiveness factor with the substrate modulus and the di-
mensionless substrate concentration in the cases of internal and external diffusional
control of immobilized enzyme kinetics. [16]

7. Discuss the design and mode of operation for PBR. [16]

8. Discuss about different ‘generation’ of biosensors and the advances made at each
stage. [16]

⋆⋆⋆⋆⋆

1 of 1