basic mass transfer concepts, fick’s law,heap and in-situ leaching, single stage and multistage...

18
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

Upload: others

Post on 10-Mar-2020

8 views

Category:

Documents


0 download

TRANSCRIPT

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.