Basic mass transfer concepts, Fick’s law,Heap and In-situ Leaching, Single stage and multistage...
Transcript of Basic mass transfer concepts, Fick’s law,Heap and In-situ Leaching, Single stage and multistage...
Course
Code Course Name L-T-P Credits Year of Introduction
BT301 Mass Transfer Operations 3-1-0 4 2016
Prerequisite: Nil
Course Objectives
To provide students with fundamental concepts of mass transfer and an understanding of the
most important separation processes in a process industry.
Syllabus
Basic mass transfer concepts, Fick’s law, theories of mass transfer, equipment for mass transfer,
absorption, distillation, flash vaporization, simple distillation, steam distillation, material and energy
balances for continuous fractionation, single stage and multi stage extraction and leaching, drying
calculations, classification of drying equipment.
Expected outcome
Upon successful completion of this course, the student will be able to
i. Identify mechanisms of mass transfer and formulate rate equations
ii. Select a suitable separation equipment for a given separation
iii. Design an absorber
iv. Design a distillation column
v. Describe and do calculations for liquid-liquid extraction and leaching
vi. Explain the drying operation and calculate the drying time
Reference Books
1. Robert E Treybal, Mass Transfer Operations, 3/e, McGraw Hill, 1980.
2. Binay K Dutta, Principles of Mass Transfer and Separation Processes, PHI Learning Pvt. Ltd.,
2015.
3. N Anantharaman, K M Meera Sheriffa Begum, Mass Transfer: Theory and Practice, PHI
Learning Pvt. Ltd., 2011.
4. Christie J Geankoplis, Transport Processes and Separation Process Principles, 4/e, Prentice
Hall, 2003.
5. Warren L McCabe, Julian C Smith, P Harriot, Unit operations of chemical Engineering, 7/e,
McGraw Hill, 2005.
Course Plan
Module Contents Hours Sem. Exam
Marks
I Classification of mass transfer operations. Fick’s law of
diffusion, Measurement of diffusivity, One component
transferring to non-diffusing component and equimolar
counter diffusion. Diffusivity in gases. Theories of mass
transfer such as Film theory, Penetration theory, Surface
Renewal theory. Convective mass transfer, Mass transfer
coefficients. Interphase mass transfer, Dimensionless
numbers. Molecular diffusion in biological solutions and gels.
9 15%
II Absorption-Solubilities of gases in liquids, Material balances
for one component transferred in countercurrent and
cocurrent flows, Minimum Liquid-Gas Ratio for Absorbers,
One component transferred in counter current multistage
operation, Continuous-contact equipment.
9 15%
FIRST INTERNAL EXAM
III Distillation- Principle, Vapour- Liquid Equilibrium, Raoult’s
law, Daltons law, Relative volatility, Azeotropes, Flash
vaporization, Simple distillation, Rayleigh’s equation, Steam
distillation- Applications, General characteristics of tray and
packed towers.
Continuous fractionation, Material and energy balance in a
continuous fractionator, McCabe-Thiele method (only), Total
reflux ratio, minimum reflux ratio, optimum reflux ratio, feed
tray location, total condenser and partial condenser, reboiler,
Numerical problems.
10 15%
IV Liquid-liquid Extraction- principle, Industrial applications,
Selection of a solvent for good extraction, Single stage, cross
current and counter current extraction, Liquid-liquid
extraction equipment, super critical fluid extraction,
Numerical problems.
8 15%
SECOND INTERNAL EXAM
V Solid-Liquid extraction(Leaching), Industrial applications,
Heap and In-situ Leaching, Single stage and multistage
leaching, Leaching equipment, solid-liquid equilibria.
Adsorption: Adsorption equilibrium, adsorbent types,
equipment operation- adsorption column dynamics- fixed bed
and agitated bed adsorption, scale up of adsorption processes-
LUB method, computer simulation method.
10 20%
VI Drying - Principle, Heat and mass transfer in drying
applications, Commercial dryers- tray dryers, vacuum dryers,
fluidized bed dryers, tunnel dryers, roller or drum dryers, belt
dryers, freeze dryers, spray dryers, Different regimes of
drying, Cross circulation and Through circulation drying,
Freeze drying, Material and energy balance in a continuous
counter current dryer, Drying time, scale up and design of
drying systems.
10 20%
END SEMESTER EXAMINATION
QUESTION PAPER PATTERN:
Maximum Marks: 100 Exam Duration: 3 hours
The question paper consists of Part A, Part B and Part C.
Part A consists of three questions of 15 marks each uniformly covering Modules I and II. The
student has to answer two questions (15×2=30 marks).
Part B consists of three questions of 15 marks each uniformly covering Modules III and IV.
The student has to answer two questions (15×2=30 marks).
Part C consists of three questions of 20 marks each uniformly covering Modules V and VI.
The student has to answer two questions (20×2=40 marks).
For each question there can be a maximum of 4 subparts.
Course
Code Course Name L-T-P Credits
Year of
Introduction
BT303 Chemical and Biological Reaction
Engineering 3-0-0 3 2016
Prerequisite: Nil
Course Objectives
To introduce the fundamentals of chemical reaction engineering, chemical kinetics and their
mathematical description; the behavior, analysis and design of batch, semi-batch,
continuously stirred tank reactors and tubular reactors.
To impart knowledge on non-isothermal and non-homogeneous systems
To introduce heterogeneous catalytic reactions and catalytic reactors.
Syllabus
Concepts of reaction rate- Derivation of rate expressions from reaction mechanisms and equilibrium-
Design of chemical and biochemical reactors- chemical/biochemical pathways; enzymatic, pathway,
and cell growth kinetics- heterogeneous and enzymatic catalysis- heat and mass transport in reactors,
including diffusion to and within catalyst particles and cells or immobilized enzymes.
Expected outcome
Upon successful completion of this course, the student will be able to
i. Define reaction rate and evaluate rate equation.
ii. Explain how temperature affects chemical reaction rate and determine the reaction rate
constant and the equilibrium constant.
iii. Differentiate between batch, semibatch, and continuous operations around ideal reactors.
iv. Derive the reactor design equations using conversion as the main variable for batch reactors,
CSTRs, and PFRs, and find analytical solutions.
v. Describe the kinetics of cell growth and enzyme reactions.
vi. Explain the nature of catalytic reactions with regard to the multiple steps of mass transfer and
surface reaction. Explain the concept of the rate limiting step.
Reference Books
1. Octave Levenspiel, Chemical Reaction Engineering, 3/e, Wiley student Education, 2006.
2. H Scott Fogler, Essentials of Chemical Reaction Engineering, Pearson Education, 2011
3. J E Bailey, D F Ollis, Biochemical Engineering Fundamentals, 2/e, McGraw-Hill Chemical
Engineering Series, 1986.
4. Hill C G, Root T W, Introduction to Chemical Engineering Kinetics & Reactor Design, John
Wiley, 2014.
5. Martin Schmal, Chemical Reaction Engineering, Essentials, Exercises and Examples, CRC
Press, 2011.
6. J M Smith, Chemical Engineering Kinetics, McGraw Hill International.
Course Plan
Module Contents Hours Sem. Exam
Marks
I Overview of chemical & biological reaction engineering -
Definition of reaction rate-Kinetics of homogeneous reaction-
Searching for a mechanism-Evaluation of rate equation.
6 15%
II Introduction to reactor design-Classification of reactors-
Design of single and multiple reactions.
6 15%
FIRST INTERNAL EXAM
III Non isothermal reactor design- Heat effects in reactors-
General graphical design procedure-Energy balance for batch,
mixed flow and plug flow reactor – isothermal, adiabatic and
non-adiabatic operation-Optimum temperature progression.
Multiple steady states.
8 15%
IV Basics of non-ideal flow-Residence time distribution.
Measurement of the RTD-Pulse and step input -C,E,F curves-
RTD in ideal reactors-Segregation model and conversion in
non-ideal reactors
7 15%
SECOND INTERNAL EXAM
V Kinetics of cell growth and enzymes. Cell growth kinetics;
substrate uptake and product formation in microbial growth;
enzyme kinetics, Michaelis-Menten rate form-
Biological reactors – chemostats-Theory of the chemostat-Fed
batch or semi-continuous fermenter operation-Oxygen transfer
in fermenters-Applications of gas-liquid transport with
reaction.
8 20%
VI Heterogeneous catalytic processes-Classification of catalysts,
promoters, inhibitors, catalyst poisons-Rate equations for
fluid-solid catalytic-reactions-Mass Transfer between fluid and
catalyst surface-Internal transport effects-Commercially
significant types of heterogeneous catalytic reactors.
7 20%
END SEMESTER EXAMINATION
QUESTION PAPER PATTERN:
Maximum Marks: 100 Exam Duration: 3 hours
The question paper consists of Part A, Part B and Part C.
Part A consists of three questions of 15 marks each uniformly covering Modules I and II. The
student has to answer two questions (15×2=30 marks).
Part B consists of three questions of 15 marks each uniformly covering Modules III and IV.
The student has to answer two questions (15×2=30 marks).
Part C consists of three questions of 20 marks each uniformly covering Modules V and VI.
The student has to answer two questions (20×2=40 marks).
For each question there can be a maximum of 4 subparts.
Course
Code Course Name L-T-P Credits
Year of
Introduction
BT305 Cellular and Molecular Biology 3-0-0 3 2016
Course Objectives
This will serve as foundational course on understanding the cellular organization and
molecular basis of life, and will pave way for the better learning of advanced courses on the
complexity of multicellular and multiorganismal interactions of life systems.
Syllabus
Basics of Cell Biology (structure & function), Cell Organization- Different Sub-cellular organelles.
Cell cycle and its control, Membrane transport – Different types, Signal Transduction, DNA
replication, DNA Damage and Repair, Expression of genetic information, Transcription, Post
transcriptional modifications, Genetic code, Translation, Post translational modifications, Regulation
of activity of Genes and Gene products in Prokaryotes, Operon, Hormonal control of gene expression
in eukaryotes.
Expected outcome
Upon successful completion of this course, the student will be able to
i. Explain complexities of cell structure and function.
ii. Explain molecular controls that govern the cells’ dynamic properties.
iii. Explain cellular interactions with the organism as a whole.
iv. Explain mechanism of cell replication.
v. Explain the mechanism of gene regulation.
Reference Books
1. Freifelder D, Molecular Biology, Jones and Bartlett Publishers Inc., 1987.
2. Nelson DL, Cox MM, Lehninger Principles of Biochemistry, W.H. Freeman and Co.
3. Jeremy M Berg, John L Tymoczko, Lubert Stryer, Biochemistry, 5/e, W.H. Freeman and Co.,
2002.
4. Geoffrey Zubay, William W. Parson, Dennis E. Vance, Biochemistry, 4/e, McGraw Hill
Publishers, 1995.
5. Benjamin Lewin, Genes VI, VII, VIII, Oxford University Press.
6. Harvey Lodish, Arnold Berk, S Lawrence Zipursky, Paul Matsudaira, David Baltimore, James
Darnell, Molecular Cell Biology, 4/e, W. H. Freeman and Company, 2000.
Course Plan
Module Contents Hours Sem. Exam
Marks
I Basics of Cell Biology (structure & function) – Discovery of
cell and Cell Theory; Comparison between Prokaryotic and
Eukaryotic cells, plant and animal cells; Plasma membrane;
Mitochondria; Chloroplast; ER; Golgi complex; Lysosome,
endosome and micro bodies; Ribosome; Nucleus
7
15%
II Cell cycle - An overview of cell cycle; Components of cell
cycle control system; Necrosis and Apoptosis.
Membrane transport–by Simple diffusion, Facilitated
diffusion and Active transport. Co- transport. Na-K ATPase.
Signal Transduction.
7
15%
FIRST INTERNAL EXAM
III Replication –Enzymology of DNA replication, Initiation of
Synthesis of the Leading Strand, Bidirectional Replication,
Termination of Replication, Replication of Eukaryotic
Chromosomes.
DNA mutation and Repair: Different types of Mutation,
Tautomeric shifts, Base excision repair, Nucleotide excision
repair, Mismatch Repair, Recombination repair and Direct
reversal. Prokaryotic SOS response.
7
15%
IV Expression of genetic information: Central Dogma,
Transcription: Basic features of RNA synthesis, E.coli RNA
polymerase, Classes of RNA molecules, processing of tRNA
and rRNA in E.coli, Transcription in Eukaryotes, Post
transcriptional Modifications: Poly(A) Tailing, Capping and
Splicing.
7 15%
SECOND INTERNAL EXAM
V Translation: Outline of Translation, The Genetic Code,
Codon-Anticodon interaction, Wobble hypothesis, Protein
Synthesis in Eukaryotes. Post translational modifications.
7 20%
VI Regulation of activity of Genes and Gene products in
Prokaryotes: General aspects of Regulation, The lactose
system and the operon model, The Arabinose operon, The
Tryptophan operon, Transcriptional Control by hormones (in
Eukaryotes)
7 20%
END SEMESTER EXAMINATION
QUESTION PAPER PATTERN:
Maximum Marks: 100 Exam Duration: 3 hours
The question paper consists of Part A, Part B and Part C.
Part A consists of three questions of 15 marks each uniformly covering Modules I and II. The
student has to answer two questions (15×2=30 marks).
Part B consists of three questions of 15 marks each uniformly covering Modules III and IV.
The student has to answer two questions (15×2=30 marks).
Part C consists of three questions of 20 marks each uniformly covering Modules V and VI.
The student has to answer two questions (20×2=40 marks).
For each question there can be a maximum of 4 subparts.
Course
Code Course Name L-T-P Credits
Year of
Introduction
BT307 Bioprocess Instrumentation 3-0-0 3 2016
Prerequisite: Nil
Course Objectives
To Gain knowledge on various instruments in bioprocess
To know about different types of biosensors
To evaluate the operating principles of different instruments
To study about data analysis and computer linked systems
To get an idea of fermentation software system
Syllabus
Functional elements of an instrument, sensors, monitoring and control of fermentation processes,
digital computers and data processing, advanced control mechanisms, batch bioreactors.
Expected outcome
Upon successful completion of this course, the student will be able to
i. Explain the working principle of an instrument
ii. Select suitable instruments for measuring process variables
iii. Explain the working principle of analytical instruments
iv. Explain the elements of digital computers
v. Understand the components of a computer-controlled fermentation processes
Reference Books
1. Eckmann D P, Industrial Instrumentation, Wiley Eastern Limited, 1975.
2. Alok Barua, Fundamentals of Industrial Instrumentation, Wiley India Pvt. Ltd., 2011.
3. Patranabis D, Principles of Industrial Instrumentation, Tata McGraw-Hill Education, 2001.
4. Keith Wilson, John Walker, Principles and Techniques of Practical Biochemistry, Cambridge
University Press, 2000.
5. Peter F Stanbury, Allan Whitaker, Stephen J. Hall, Principles of Fermentation Technology,
3/e, Butterworth-Heinemann, 2016.
Course Plan
Module Contents Hours Sem. Exam
Marks
I Introduction to bioprocess Instrumentation - Definition of
instrumentation, concept of an instrument - Functional
elements and functions of an instrument - Classification of
instruments - Static and dynamic characteristics of measuring
instruments. Transducers their principles and working,
different types of transducers: Piezoelectric transducers,
electromagnetic transducers, optical transducers, transducers
for biomedical applications - Instrumentation diagram.
7 15%
II Biosensors: Various components of biosensors - On-line
sensors for cell properties - off-line analytical methods -
potentiometric biosensors - Transducers, calorimetric, optical,
potentiometric/amperometric, conductometric/resistometric
biosensors, Biosensors for glucose, alcohol, carbon dioxide,
cell population, BOD
7
15%
FIRST INTERNAL EXAM
III Methods of measuring process variables – Temperature:
measurements, temperature scales, basic principles and
working of thermometers, mercury in glass thermometers,
thermocouples, ranges of different types of temperature
measuring instruments. Sources of errors and precautions to
be taken in temperature measurements - Flow measurement:
Head flow meters, area flow meters, positive displacement
flow meters, mass and magnetic flow meters and strain
gauges.
7 15%
IV Pressure measurement: Principles of working of manometers,
various types of manometers - McLeod gauge, Knudsen
gauge, Bourdon gauge, bellows, diaphragm, electrical
pressure transducers, piezoelectric manometers, thermal
conductivity gauges-ionisation gauge high pressure
measuring instrument.
7 15%
SECOND INTERNAL EXAM
V Analytical instruments: Chromatography: GC, HPLC,
Spectroscopy: Mass spectroscopy, NMR, autoradiography,
Electrophoresis, schematic summary of biochemical reactor
instrumentation
7 20%
VI Elements of Digital computers; Computer Interfaces and
peripheral devices-Data Analysis-Data smoothing and
interpolation- State and parameter estimation. Components of
a computer linked system-Programmed batch bio-reaction-
Design and operation strategies for batch plants-Fermentation
software systems.
7 20%
END SEMESTER EXAMINATION
QUESTION PAPER PATTERN:
Maximum Marks: 100 Exam Duration: 3 hours
The question paper consists of Part A, Part B and Part C.
Part A consists of three questions of 15 marks each uniformly covering Modules I and II. The
student has to answer two questions (15×2=30 marks).
Part B consists of three questions of 15 marks each uniformly covering Modules III and IV.
The student has to answer two questions (15×2=30 marks).
Part C consists of three questions of 20 marks each uniformly covering Modules V and VI.
The student has to answer two questions (20×2=40 marks).
For each question there can be a maximum of 4 subparts.
Course
Code Course Name L-T-P Credits
Year of
Introduction
BT309 Enzyme Engineering and Technology 3-0-0 3 2016
Prerequisite: Nil
Course Objectives
To provide students an insight into the significance of enzymes and their applications, their
kinetics based on different models and theories, extraction and purification of enzymes, and
their immobilisation.
Syllabus
Introduction to enzymes, nomenclature and classification, enzymes as biocatalysts, enzyme
applications, kinetics of enzyme catalysed reactions, enzyme immobilisation, kinetics of immobilised
enzymes, immobilised enzyme applications, immobilized enzyme reactors, enzyme inhibition,
extraction and purification of enzymes, enzyme assays, enzyme fingerprinting, high throughput
screening systems, enzyme based biosensors.
Expected outcome
Upon successful completion of this course, students will be able to
i. Classify enzymes according to their function.
ii. Evaluate kinetic parameters and understand their significance.
iii. Explain various enzyme immobilization techniques.
iv. Explain the mechanism of enzyme modulation and regulation.
v. Explain the steps involved in the extraction and purification of enzymes.
Reference Books
1. Nicholas C Price, Lewis Stevens, Fundamentals of Enzymology -Cell and Molecular Biology
of Catalytic Proteins, Oxford University Press, 1999.
2. Andreas S Bommarius, Bettina R Riebel, Biocatalysis: Fundamentals and Applications,
Wiley-VCH, 2004.
3. Trevor Palmer, Philip L Boner, Enzymes- Biochemistry, Biotechnology and Clinical
Chemistry, Woodhead Publishing, 2007.
4. Robert A Copeland, Enzymes: A Practical Introduction to Structure, Mechanism, and Data
Analysis, Wiley-VCH, 2000.
5. Syed Ahmed Inamdar, Biochemical Engineering Principles and Functions, PHI Learning,
2012.
Course Plan
Module Contents Hours Sem. Exam
Marks
I Brief introduction to enzymes, nomenclature and
classification of enzymes, theory of enzyme action, structure–
functionality relationships, concept and determination of
enzyme activity, biocatalysis in aqueous and non-
conventional media.
6 15%
II Kinetics of enzyme catalysed reactions. Importance and
evaluation of kinetic constants. Deviation from hyperbolic
enzyme kinetics. Kinetics of bi substrate enzymes. Effect of
physical and chemical factors on enzyme activity.
8 15%
FIRST INTERNAL EXAM
III Immobilization of enzymes. Immobilisation methods, mass
transfer effects in immobilized enzyme systems.
Effectiveness factor. Applications of immobilized enzymes in
process. Design of immobilized enzyme reactors – Packed
bed, Fluidized bed and Membrane bioreactors.
8 15%
IV Enzyme inhibition types- Competitive, Non competitive and
un competitive inhibitions. Inhibition kinetics. Allosteric
regulation of enzymes. Enzyme deactivation, deactivation
model and half-life period, modulation and regulation of
enzyme activity.
6 15%
SECOND INTERNAL EXAM
V Extraction and purification of enzymes. Methods of enzyme
production, Extraction of soluble and membrane bound
enzymes. Nature of extraction medium. Purification of
enzymes. Criteria of purity. Determination of molecular
weight of enzymes.
8 20%
VI Enzyme assays. Industrial perspective of enzyme assays.
Enzyme fingerprinting, High throughput screening systems,
Enzyme based biosensors.
6 20%
END SEMESTER EXAMINATION
QUESTION PAPER PATTERN:
Maximum Marks: 100 Exam Duration: 3 hours
The question paper consists of Part A, Part B and Part C.
Part A consists of three questions of 15 marks each uniformly covering Modules I and II. The
student has to answer two questions (15×2=30 marks).
Part B consists of three questions of 15 marks each uniformly covering Modules III and IV.
The student has to answer two questions (15×2=30 marks).
Part C consists of three questions of 20 marks each uniformly covering Modules V and VI.
The student has to answer two questions (20×2=40 marks).
For each question there can be a maximum of 4 subparts.
Course
Code Course Name L-T-P Credits
Year of
Introduction
BT361 Animal and Plant Cell Technology 3-0-0 3 2016
Prerequisite: Nil
Course Objectives
To provide students an overview and current developments in different areas of animal and
plant biotechnology.
To understand the role of animal and plant cell technology in pharmaceutical and food
industry, agriculture and ecology.
Syllabus
Plant tissue culture techniques, Protoplast culture, Gene transfer methods and applications of plant
genetic engineering, Basic techniques in animal cell culture, Different types of cell cultures, Gene
transfer methods in animals and application.
Expected outcome
Students who successfully complete this course will be able to
i. Explain various plant tissue culture techniques.
ii. Explain isolation and culture of protoplast.
iii. Explain gene transfer methods.
iv. Explain different types of cell cultures and culture techniques.
v. Explain the techniques for gene transfer in animals.
Reference Books
1. Hammond J, McGarvey P, Yusibov V (Eds), Plant Biotechnology -New Products and
Applications, Springer, 1999.
2. Tong-Jen Fu, Gurmeet Singh, Wayne R. Curtis (Eds), Plant Cell and Tissue Culture for the
production of Food Ingredients, Springer Science & Business Media, 1999.
3. Rian Freshney, Culture of Animal Cells: A Manual of Basic Technique and Specialized
Applications, 6/e, Wiley-Blackwell, 2010.
4. John R W Masters (Ed.), Animal Cell Culture - A Practical Approach, 3/e, Oxford University
Press, 2000.
5. Jackson JF, Linskens HF (Eds.), Genetic Transformation of Plants, Springer, 2003.
6. M K Razdan, Introduction to Plant tissue culture, Science Publishers, 2003.
7. H S Chawla, Introduction to Plant Biotechnology, Science Publishers, 2002.
Course Plan
Module Contents Hours Sem. Exam
Marks
I Plant tissue culture techniques - micropropagation, somatic
embryogenesis, somaclonal variation and applications,
organogenesis, haploids (Anther, Pollen, Embryo and ovule
culture) and their applications, Endosperm culture, meristem
culture and production of triploids.
6 15%
II Protoplast culture - Introduction to protoplast isolation,
culture and regeneration, methods of fusing protoplasts,
somatic hybridization, Protoplast and tissue culture
manipulation for genetic manipulation of plants, embryo
rescue, artificial seeds, immobilization of plant cells.
6 15%
FIRST INTERNAL EXAM
III Gene Transfer methods - Agrobacterium tumefaciens
mediated transfer- techniques of transferring agronomically
important genes using Ti plasmid, Ri plasmid, binary vectors,
Use of 35S and other promoters, genetic markers, reporter
genes methods of direct gene transfer- particle bombardment,
electroporation, microinjection, transformation of monocots.
Applications of Plant Genetic Engineering – crop
improvement, herbicide resistance, insect resistance, virus
resistance, Industrial enzymes, Molecular farming for
therapeutic protein (Plantibodies, Plantigens, Edible
Vaccines), delay of fruit ripening, plants as bioreactors,
ecological impact of transgenic plants.
10 15%
IV Basic techniques in animal cell culture - Types of cell
culture media: natural media, synthetic media, role of carbon
dioxide, serum and supplements. Preparation and sterilization
of cell culture media, serum and other reagents.
5 15%
SECOND INTERNAL EXAM
V Different types of cell cultures - Trypsinization, Cell
separation, Primary cell culture, Continuous cell lines,
Suspension culture, Organ culture. Development of cell lines,
Characterization and maintenance of cell lines.
Characteristics of cells in culture: Contact inhibition,
anchorage dependence, cell-cell communication, cell
synchronization, Cell senescence.
8 20%
VI Gene transfer methods in Animals and application –
Microinjection, Embryonic Stem cell gene transfer,
Retrovirus & Gene transfer. Development of recombinant
vaccines, monoclonal antibody their applications,
introduction to transgenic. Animal cloning: Techniques,
relevance and ethical issues
7 20%
END SEMESTER EXAMINATION
QUESTION PAPER PATTERN:
Maximum Marks: 100 Exam Duration: 3 hours
The question paper consists of Part A, Part B and Part C.
Part A consists of three questions of 15 marks each uniformly covering Modules I and II. The
student has to answer two questions (15×2=30 marks).
Part B consists of three questions of 15 marks each uniformly covering Modules III and IV.
The student has to answer two questions (15×2=30 marks).
Part C consists of three questions of 20 marks each uniformly covering Modules V and VI.
The student has to answer two questions (20×2=40 marks).
For each question there can be a maximum of 4 subparts.
Course
Code Course Name L-T-P Credits
Year of
Introduction
BT363 Metabolic Engineering and
Synthetic Biology 3-0-0 3 2016
Prerequisite: Nil
Course Objectives
This course will focus on theoretical, quantitative, and experimental methods for understanding and
engineering cellular systems for biotechnological applications. The course will seek to teach students
the theory behind the methods; encouraging understanding, which will allow new uses and application
in alternative areas to become apparent.
Syllabus
Introduction to metabolic engineering, Synthesis of primary metabolites, Biosynthesis of secondary
metabolites, Bioconversions, Regulation of enzyme production, Metabolic Flux- methods for analysis,
application, Metabolic engineering with bioinformatics, Introduction to synthetic biology,
Applications of synthetic biology.
Expected outcome
Students who successfully complete this course should be able to
Describe different models of cellular reaction
Explain regulation of metabolites at enzyme and whole cell levels.
Explain metabolic flux analysis and its applications.
Explain bioinformatics applications in metabolic engineering.
Explain ethical, legal and social implications of synthetic biology.
Reference Books
1. Huimin Zhao (Ed.), Synthetic Biology: Tools and Applications, Academic Press. 2013
2. Vikram Singh, Pawan K. Dhar (Eds.), Systems and Synthetic Biology,Springer, 2015.
3. Lehninger A L, Nelson D L, Cox M M, Principles of Biochemistry, Palgrave MacMillan, 2002.
4. G Stephanopoulos, AAristidou, J Nielsen, Metabolic Engineering Principles and
Methodologies, Academic Press, 1998.
5. S Y Lee, ET Papoutsakis, Metabolic Engineering, Marcel Dekker, New York, 1999.
6. David Fell, Understanding the Control of Metabolism, Portland Press, London, 1997.
7. EO Voit, Computational Analysis of Biochemical Systems, Cambridge University Press, 2000.
Course Plan
Module Contents Hours Sem. Exam
Marks
I Introduction: Metabolic regulation, Basic concepts of
Metabolic Engineering – Overview of cellular metabolism –
Different models for cellular reactions, induction – Jacob
Monod model and its regulation, Differential regulation by
isoenzymes, Feedback regulation.
Synthesis of Primary Metabolites: Amino acid synthesis
pathways and its regulation at enzyme level and whole cell
level, Alteration of feedback regulation, Limiting
accumulation of end products.
Biosynthesis of Secondary Metabolites: Regulation of
secondary metabolite pathways, precursor effects, prophase,
idiophase relationship, Catabolite regulation by passing
control of secondary metabolism, producers of secondary
metabolites, applications of secondary metabolites
9 15%
II Bioconversions: Applications of Bioconversions, Factors
affecting bioconversions, Specificity, Yields, Cometabolism,
Product inhibition, mixed or sequential bioconversions,
Conversion of insoluble substances.
Regulation of Enzyme Production: Strain selection, Genetic
improvement of strains, Gene dosage, metabolic pathway
manipulations to improve fermentation, Feedback repression,
Catabolite Repression, optimization and control of metabolic
activities. The modification of existing - or the introduction of
entirely new - metabolic pathways.
9 15%
FIRST INTERNAL EXAM
III Metabolic Flux: Integration of anabolism and catabolism,
metabolic flux distribution analysis in bioprocess, material
balance, kinetic types, equilibrium reaction. Experimental
determination method of flux distribution, Metabolic flux
analysis and its applications, Thermodynamics of cellular
processes.
6 15%
IV Metabolic Engineering with Bioinformatics: Metabolic
pathway modeling, Analysis of metabolic control and the
structure metabolic networks, Metabolic pathway synthesis
algorithms, Applications of Metabolic Engineering:
Application in pharmaceuticals, chemical bioprocess, food
technology, agriculture, environmental bioremediation and
biomass conversion.
6 15%
SECOND INTERNAL EXAM
V Synthetic Biology - Introduction to Synthetic Biology and
systems biology as a new perspective, Basic concepts of
genomes, transcriptomes, proteomes. Basic and advanced
techniques in engineering biological systems.
6 20%
VI Applications of Synthetic Biology - Synthetic Biological
circuits and its design. Assembly of synthetic genomes for
minimal genome organisms. Fixing faulty genes by CRISPR
tools. Ethical, legal and social implications of synthetic
biology, Applications of Synthetic Biology.
6 20%
END SEMESTER EXAMINATION
QUESTION PAPER PATTERN:
Maximum Marks: 100 Exam Duration: 3 hours
The question paper consists of Part A, Part B and Part C.
Part A consists of three questions of 15 marks each uniformly covering Modules I and II. The
student has to answer two questions (15×2=30 marks).
Part B consists of three questions of 15 marks each uniformly covering Modules III and IV.
The student has to answer two questions (15×2=30 marks).
Part C consists of three questions of 20 marks each uniformly covering Modules V and VI.
The student has to answer two questions (20×2=40 marks).
For each question there can be a maximum of 4 subparts.
Course
Code Course Name L-T-P Credits
Year of
Introduction
BT365 Proteomics and Protein Engineering 3-0-0 3 2016
Prerequisite: Nil
Course Objectives
To enable the students to identify the importance of protein biomolecules
To realize the structure-function relationships in proteins
To learn advanced techniques of protein engineering and analysis
Syllabus
Introduction to the concept of proteome, Protein folding, Protein separation techniques, Detection of
proteins and Image analysis, Enhancing high-throughput proteome analysis, Functional proteomics,
Application of Proteomics and Protein engineering.
Expected outcome
Students who successfully complete this course will be able to
i. Analyze the various interactions in protein makeup.
ii. Explain the role of functional proteins in various fields.
iii. Describe the techniques involved in protein separation and purification.
iv. Explain the methods for detection of proteins.
v. Explain the latest application of protein science.
Reference Books
1. Pennington SR, Dunn MJ, Proteomics: From Protein Sequence to Function, Viva Books,
2001.
2. Daniel C Liebler, Introduction to Proteomics, Humana Press, 2001.
3. Twyman RM, Principles of Proteomics, BIOS Scientific Publishers, 2004.
4. Sahai S, Genomics and Proteomics-functional and computational aspects, Plenum
publications, 1999.
5. Moody PCE, Wilkinson AJ, Protein Engineering, IRL press, Oxford, 1990.
Course Plan
Module Contents Hours Sem. Exam
Marks
I Introduction to the concept of proteome, protein structure,
functional protein families, importance of proteomics in
biological functions, scope of proteomics, challenges of
proteomics.
Protein folding: Hierarchical protein folding, Molecular
chaperones, role of chaperones in protein folding, Defective
protein folding; Proteasomes, Prions, Polyketides and non-
ribosomal peptides- Combinational manipulation of
polyketides and non ribosomal peptides.
7 15%
II Protein separation techniques: ion-exchange, size-exclusion
and affinity chromatography techniques; Polyacrylamide gel
electrophoresis; Isoelectric focusing (IEF), IPG, Two
dimensional PAGE for proteome analysis, Equilibration
between dimensions- The second dimension: SDS-PAGE-
resolution and reproducibility of 2-Dimensional
Electrophoresis, liquid chromatography in proteomics.
7 15%
FIRST INTERNAL EXAM
III Detection of proteins in polyacrylamide gels and on
electroblot membranes: Use of Organic dyes and silver stains,
Reverse stains, Colloidal dispersion stains, organic
fluorophore stains, metal chelate stains.
Image analysis of two-dimensional gels: Data acquisition,
digital image processing, Protein spot detection and
quantitation, Gel matching, Data analysis, data presentation,
protein data bases.
7 15%
IV Enhancing high-throughput proteome analysis: impact of
stable isotope labeling – Introduction, Sample preparation,
two dimensional gel separation and analysis, Peptide
fingerprinting, Mass spectrometry: MALDI-MS, protein
identification using MS/MS data.
6 15%
SECOND INTERNAL EXAM
V Functional proteomics: Protein array, protein chips -
introduction, different types of protein chips, detection and
quantification of proteins bound to protein chips, emerging
protein chip technologies.
Application of Proteomics: Mining proteomes, protein
expression profile, identification of protein-protein
interactions and protein complexes, drug development and
toxicology.
8 20%
VI Protein engineering - Site Directed mutagenesis procedures
for specific protein function-Oligonucleotide directed and
random mutagenesis, DNA shuffling; Protein engineering-
basic principles, strategies, basic concepts of design of a new
protein molecule, specific example of enzyme engineering
(Subtilisin, Peroxidase).
7 20%
END SEMESTER EXAMINATION
QUESTION PAPER PATTERN:
Maximum Marks: 100 Exam Duration: 3 hours
The question paper consists of Part A, Part B and Part C.
Part A consists of three questions of 15 marks each uniformly covering Modules I and II. The
student has to answer two questions (15×2=30 marks).
Part B consists of three questions of 15 marks each uniformly covering Modules III and IV.
The student has to answer two questions (15×2=30 marks).
Part C consists of three questions of 20 marks each uniformly covering Modules V and VI.
The student has to answer two questions (20×2=40 marks).
For each question there can be a maximum of 4 subparts.
Course
Code Course Name L-T-P Credits
Year of
Introduction
BT367 Tissue Engineering and Stem Cells 3-0-0 3 2016
Prerequisite : Nil
Course Objectives
To provide the students with an overview of fundamental concepts of tissue engineering and
stem cells.
To introduce different types of stem cells and the techniques for engineering of stem cells.
To give an idea of milestones in stem cell research and expose students to current topics at the
frontier of this field.
Syllabus
Introduction to tissue engineering, Aspects of Cell culture, Molecular biology aspects, Scaffold and
transplant, Stem Cells, Molecular bases of pluripotency, Clinical translation of stem cells.
Expected outcome
Upon successful completion of this course, students will be able to
i. Explain basic experimental techniques used in tissue engineering and stem cell research.
ii. Explain different cell types, cell characterization, and cell culture bioreactors.
iii. Describe sources, properties, and potential therapeutic applications of stem cells.
iv. Explain molecular bases of pluripotency.
v. Explain applications of stem cells in pharmacological and toxicological studies.
Reference Books
1. Song Li, Nicolas L'Heureux, Jennifer Elisseeff (Eds.), Stem Cell and Tissue Engineering,
World Scientific, 2011.
2. Artmann, Minger, Hescheler (Eds.), Stem Cell Engineering: Principles and Applications,
Springer, 2011.
3. Clemens Van Blitterswijk, Jan De Boer, Tissue Engineering, Elsevier, 2014.
4. Robert Lanza, Essentials of stem cell biology, Academic Press, 2009.
5. Peter J Quesenberry, Gary S Stein, Bernard G Forget, Sherman M Weissman (Eds.), Stem Cell
Biology and Gene Therapy, WILEY-LISS, 1998.
6. Kursad Turksen (Ed.), Embryonic Stem Cell Protocols, Volume 1: Isolation and
Characterization, Springer, 2006.
Course Plan
Module Contents Hours Sem. Exam
Marks
I Introduction to tissue engineering- structure and
organization of tissues- Epithelial, connective; vascularity and
angiogenesis, basic wound healing, cell migration, current
scope of development and use in therapeutic and in-vitro
testing. Scientific challenges.
6 15%
II Aspects of Cell culture- Different cell types, progenitor cells
and cell differentiations, different kind of matrix, cell-cell
interaction; cell expansion, cell transfer, cell storage and cell
characterization, cell culture bioreactors.
Molecular biology aspects- Cell signalling molecules,
growth factors, hormone and growth factor signalling, growth
factor delivery in tissue engineering, cell attachment:
differential cell adhesion, receptor-ligand binding, Cell
surface markers.
8 15%
FIRST INTERNAL EXAM
III Scaffold and transplant: Engineering biomaterials,
Degradable materials, porosity, mechanical strength, 3-D
architecture and cell incorporation. Engineering tissues for
replacing bone, cartilage, tendons, ligaments, skin and liver.
Basic transplant immunology stems cells; Case studies and
regulatory issues-cell transplantation for liver,
musculoskeletal, cardiovascular, neural, visceral tissue
engineering. Ethical, FDA and regulatory issues.
8 15%
IV Stem Cells: Origin, Identification, Isolation, Characterization
and maintenance of Embryonic stem cells, Adult stem cells,
Epithelial stem cell –skin and intestinal stem cells, Induced
pluripotent stem cells, Hematopoietic stem cells,
Mesenchymal stem cells and Neural stem cells (NSC). Cancer
stem cells.
7 15%
SECOND INTERNAL EXAM
V Molecular bases of pluripotency, Stem cell niches within
mammalian tissues– Mammalian testis, HSC, Epidermis hair
follicle, Gut epithelium and Neural stem cells. Metaplasia and
transdifferentiation – pancreas to liver, regeneration,
experimental conversion of a cells phenotype.
6 20%
VI Clinical translation of stem cells: Therapeutic cloning using
stem cells, Cord blood transplantation & cord blood banking,
Stem cells for clinical regeneration and repair, organ cloning,
tissue engineering, Use of embryological stem cells in
pharmacological and toxicological screens, Regulation and
ethics of stem cell research and its applications.
7 20%
END SEMESTER EXAMINATION
QUESTION PAPER PATTERN:
Maximum Marks: 100 Exam Duration: 3 hours
The question paper consists of Part A, Part B and Part C.
Part A consists of three questions of 15 marks each uniformly covering Modules I and II. The
student has to answer two questions (15×2=30 marks).
Part B consists of three questions of 15 marks each uniformly covering Modules III and IV.
The student has to answer two questions (15×2=30 marks).
Part C consists of three questions of 20 marks each uniformly covering Modules V and VI.
The student has to answer two questions (20×2=40 marks).
For each question there can be a maximum of 4 subparts.