Exam Details
Subject | enzyme technology | |
Paper | ||
Exam / Course | m.sc. biotechnology | |
Department | ||
Organization | solapur university | |
Position | ||
Exam Date | November, 2016 | |
City, State | maharashtra, solapur |
Question Paper
Master of Science I (Biotechnology) Examination: Oct/Nov 2016
Semester II (Old CGPA)
SLR No. Day
Date Time Subject Name Paper
No. Seat No.
SLR SK
107
Saturday
09/11/2016
10.30 AM
To
01.00 PM
Enzyme Technology
C
II
Instructions: All question of Section I are compulsory.
Answer any four questions from Section -II.
All question carry equal marks.
Draw neat and labeled diagrams wherever necessary
Total Marks: 70
Section- I
Q.1 Rewrite the following sentences by selecting correct answers from given
alternative.
07
Some of are autocatalytic molecule and considered as
enzyme.
RNAs DNAs
Carbohydrates lipids
The plot of temperature against enzyme reaction rate gives
shape.
Parabolic hyperbolic
bell sigmoidal
enzyme catalyzes the first step of pyrimidine biosynthesis.
Phosphorylase Ribonuclease
Carboxypeptidase Aspartate transcarbamoylase
In presence of competitive inhibitors the Vmax of reaction
Increases decreases
becomes half of it remains constant
may be expressed as international unit per mg protein.
Specific activity Enzyme activity
Turnover negative Molar catalytic activity
When substrate itself binds to allosteric site of enzyme and activates
enzyme then it is known as modulator.
Heterotropic positive Hemotropic positive
Hetertropic negative Hotmotropic engineering
The improvement or alteration in existing pathway is a task of
immobilization metabolic engineering
protein engineering enzyme engineering
Define the following terms: 07
Antibodies
Allosteric site
International unit
Uncompetitive
Turnover
Transition state
Streospecificity
Page 1 of 2
Section-II
Answer Any Four
Q.2 Write an essay on factors affecting catalytic efficiency of enzyme. 14
Q.3 Describe bisubstrate reactions with their types and kinetics. 14
Q.4 Illustrate the protein ligand interactions with quantitative measurement. 14
Q.5 What is immobilization? Give various methods and industrial application of it. 14
Q.6 Answer any TWO of the following: 14
Give an account of isozymes.
Derive an euation of Michaelis -Menten for unisubstrate reaction of enzyme.
Illustrate the structure and function relationship of lysozyme.
Q.7 Answer any TWO of the following: 14
Write a note on glucose oxidase as biosensor.
Explain the allosteric regulation of enzyme.
Discuss the structure and function relationship of trypsin.
Semester II (Old CGPA)
SLR No. Day
Date Time Subject Name Paper
No. Seat No.
SLR SK
107
Saturday
09/11/2016
10.30 AM
To
01.00 PM
Enzyme Technology
C
II
Instructions: All question of Section I are compulsory.
Answer any four questions from Section -II.
All question carry equal marks.
Draw neat and labeled diagrams wherever necessary
Total Marks: 70
Section- I
Q.1 Rewrite the following sentences by selecting correct answers from given
alternative.
07
Some of are autocatalytic molecule and considered as
enzyme.
RNAs DNAs
Carbohydrates lipids
The plot of temperature against enzyme reaction rate gives
shape.
Parabolic hyperbolic
bell sigmoidal
enzyme catalyzes the first step of pyrimidine biosynthesis.
Phosphorylase Ribonuclease
Carboxypeptidase Aspartate transcarbamoylase
In presence of competitive inhibitors the Vmax of reaction
Increases decreases
becomes half of it remains constant
may be expressed as international unit per mg protein.
Specific activity Enzyme activity
Turnover negative Molar catalytic activity
When substrate itself binds to allosteric site of enzyme and activates
enzyme then it is known as modulator.
Heterotropic positive Hemotropic positive
Hetertropic negative Hotmotropic engineering
The improvement or alteration in existing pathway is a task of
immobilization metabolic engineering
protein engineering enzyme engineering
Define the following terms: 07
Antibodies
Allosteric site
International unit
Uncompetitive
Turnover
Transition state
Streospecificity
Page 1 of 2
Section-II
Answer Any Four
Q.2 Write an essay on factors affecting catalytic efficiency of enzyme. 14
Q.3 Describe bisubstrate reactions with their types and kinetics. 14
Q.4 Illustrate the protein ligand interactions with quantitative measurement. 14
Q.5 What is immobilization? Give various methods and industrial application of it. 14
Q.6 Answer any TWO of the following: 14
Give an account of isozymes.
Derive an euation of Michaelis -Menten for unisubstrate reaction of enzyme.
Illustrate the structure and function relationship of lysozyme.
Q.7 Answer any TWO of the following: 14
Write a note on glucose oxidase as biosensor.
Explain the allosteric regulation of enzyme.
Discuss the structure and function relationship of trypsin.
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