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Formerly Kanpur University, Kanpur – 208024

A Documentary Support
For
Metric No. – 1.1.1
Programme Outcomes & Course Outcomes

Under the
Criteria - I
(Curriculum Design and Development)
Key Indicator - 1.1
In
Metric No. – 1.1.1

B.Sc. Bio-Technology

(Registrar)
C.S.J.M.University
Kanpur
CHHATRAPATI SHAHU JI MAHARAJ UNIVERSITY, KANPUR
Department of Life Sciences & Biotechnology

STRUCTURE OF SYLLABUS FOR THE

PROGRAM: B.Sc. (Hons.), SUBJECT: Biotechnology

FOUR YEAR UNDERGRADUATE PROGRAM (FYUP), CHOICE BASED CREDIT SYSTEM (CBCS) AS PER UGC
Under School of Life Sciences and Biotechnology

PREAMBLE
In view of the increasing demand for training manpower in the area of Molecular Biology, Genetic
Medicine and Biotechnology, it was consensus of the committee (Faculties & experts) that this
course should be broad based and should be able to give a good insight into modern biology and
important component of hands-on training to the students. Thus by nature it will be an
interdisciplinary course. The course curriculum for U.G program under choice based for B.Sc. in
Biotechnology (Hons.) presented in this document follows the nationwide exercise undertaken by
the UGC as part of curriculum restructuring initiative.
 SEMESTER-I
Paper code Courses offered Course Name Credit Max
(Core course) Marks
Theory Practical*
BBT – 1001 CC-1 Chemistry 4 100
BBT – 1001P Practical-1 Chemistry Practical 2 100
BBT – 1002 CC-2 Cell Biology 4 100
BBT – 1001P Practical-2 Cell Biology Practical 2 100
BBT – Ability Enhancement English Communication-I 4 100
1003/AECC-01 Compulsory Course
BBT – 1004/GE- Generic Elective 1004(A): Biotechnology and Human 4 100
01 (elect any one) Welfare
1004(B): I.P.R Entrepreneurship 4 100
Bioethics & Biosafety
Total 20 600
SEMESTER-II
Paper code Courses offered Course Name Theory Practical*
(Core course)
BBT – 2001 CC-3 Mammalian Physiology 4 100
BBT – 2001P Practical-3 Mammalian Physiology Practical 2 100
BBT – 2002 CC-4 Plant Physiology 4 100
BBT – 2001P Practical-4 Plant Physiology Practical 2 100
BBT – Ability Environmental Sciences 4 100
2003/AECC-01 Enhancement
Compulsory Course
BBT – 2004/GE- Generic Elective 2004 (A): Gene Organization, 4 100
02 (elect any one) Expression and Regulation
2004 (B): Development Biology 4 100
Total 20 600
SEMESTER-III
Paper code Courses offered Course Name Theory Practical*
(Core course)
BBT – 3001 CC-5 General Biochemistry 4 100
BBT – 3001P Practical-5 General Biochemistry Practical 2 100
BBT – 3002 CC-6 General Microbiology 4 100
BBT – 3002P Practical-6 General Microbiology Practical 2 100
BBT – 3003 CC-7 Genetics 4 100
BBT – 3003P Practical-7 Genetics Practical 2 100
BBT - Skill Enhancement Enzymology 4 100
3004/SEC-01 Course
Total 22 700
SEMESTER-IV

Paper code Courses offered Course Name Theory Practical*

(Core course)
BBT – 4001 CC-8 Bioanalytical Tools 4 100
BBT – 4001P Practical-8 Bioanalytical Tools Practical 2 100
BBT – 4002 CC-9 Intermediary Metabolism 4 100
BBT – 4002P Practical-9 Intermediary Metabolism Practical 2 100
BBT – 4003 CC-10 Immunology 4 100
BBT – 4003P Practical-10 Immunology Practical 2 100
BBT - Skill Enhancement Molecular diagnostics 4 100
4004/SEC-02 Course
Total 22 700
SEMESTER-V
 Paper code Courses offered Course Name Theory Practical*
(Core course)

BBT – 5001 CC-11 Molecular Biology 4 100

BBT – 5001P Practical-11 Molecular Biology Practical 2 100
BBT – 5002 CC-12 Biostatistics 4 100
BBT – 5002P Practical-12 Biostatistics Practical 2 100
BBT – 5003 Discipline Specific Animal Biotechnology 4 100
BBT – 5004 Elective (elect any Environmental Biotechnology 4 100
BBT -4005 two) Microbial Biotechnology 4 100
Total 20 600
SEMESTER-VI

Paper code Courses offered Course Name Theory Practical*

(Core course)
BBT – 6001 CC-13 Recombinant DNA Technology 4 100
BBT – 6001P Practical-13 Recombinant DNA Technology 2 100
Practical
BBT – 6002 CC-14 Genomics and Proteomics 4 100
BBT – 6002P Practical-14 Genomics and Proteomics Practical 2 100
BBT – 6003 Discipline Specific Plant Biotechnology 4 100
BBT – 6004 Elective (elect any Bioinformatics 4 100
BBT - 6005 two) Bioprocess Technology 4 100
Total 20 600
SEMESTER-VII

Paper code Courses offered Course Name Theory Practical*

(Core course)
In addition complete any THREE optional subject: BBT-7001(A)/(B)/(C)/(D)
BBT – 7001 (A) CC-15 Applied Biotechnology 4 100
BBT – 7001 (A)P Practical 2 100
BBT – 7001 (B) Applied Biochemistry 4 100
BBT – 7001 Practical 2 100
(B)P
BBT – 7001 (C) Applied Microbiology 4 100
BBT – 7001 Practical 2 100
(C)P
BBT – 7001 (D) Applied Food Technology 4 100
BBT – 7001 Practical 2 100
(D)P
BBT – 7002 CC-16 Research Methodology 4 100
Total 22 700
SEMESTER VIII
Paper code Courses offered Course Name Theory Practical* Theory
(Core course)
Develop the skill required to completed a substantial original research project
BBT-8001 CC-17 Research Project 20 700
Total 20 700
Grand Total 166 5200

C: Core Course; GE: Generic Elective; AECC: Ability Enhancement Compulsory Course; SEC: Skill Enhancement
Courses; DSE: Discipline Specific Elective
 PROGRAMME OUTCOMES (PO’s)

PO1: Graduate Attributes

A graduate student shall be able to develop skill and acquire knowledge in fundamentals of Chemistry,
Biology and will develop disciplinary theory and practical knowledge in the diversified areas of
Biochemistry. The students are given fundamentals in each course and they are encouraged to become
unique by allowing them to perform experiments in the areas of their interest. This will enable the students
to equip themselves with the basic practical training in different areas of Biochemistry having various
Biomolecules, nature and their structure and function. To take up further specialized Master level courses
in these areas or to take up suitable assignments/jobs in Biotech/Biochemical industries. The students shall
enjoy the academic freedom which will bring out the best from each student. These attributes are elaborated
as under:
PO2: Disciplinary Knowledge:
a) Ability to understand fundamental concepts of biology, chemistry and biochemistry.
b) Ability to apply basic principles of chemistry to biological systems and molecular biology.
c) Ability to relate various interrelated physiological and metabolic events.
d) A general awareness of current developments at the forefront in biotechnology, biochemistry
and allied subjects.
e) Ability to critically evaluate a problem and resolve to challenge blindly accepted concepts.
f) Zeal and ability to work safely and effectively in a laboratory.
g) Good experimental and quantitative skills encompassing preparation of laboratory reagents,
conducting experiments, satisfactory analyses of data and interpretation of results.
h) Awareness of resources, and their conservation.
i) Ability to think laterally and in an integrating manner and develop interdisciplinary approach.
j) Overall knowledge of the avenues for research and higher academic achievements in the field of
Biotechnology and allied subjects.

PROGRAMME SPECIFIC OUTCOMES (PSOs)

PSO1: Communication Skills:

a) Ability to speak and write clearly in English
b) Ability to listen to and follow scientific viewpoints and engage with them.
PSO2: Critical Thinking:
a) Ability to substantiate critical readings of scientific texts in order to persuade others.
b) Ability to place scientific statements and themes in contexts and also evaluate them in terms
of generic conventions.
PSO3: Problem Solving:
a) Ability to closely observe the situation, and apply lateral thinking and analytical skills. Analytical
PSO4: Reasoning:
a) Ability to evaluate the strengths and weaknesses in scholarly texts spotting flaws in their
arguments.
b) Ability to use critics and theorists to create a framework and to substantiate one’s argument
in one’s reading of scientific texts.
PSO4: Research-Related Skills:
a) Ability to problematize; to formulate hypothesis and research questions, and to identify and
consult relevant sources to find answers.
b) Ability to plan and write a research paper.
PSO5: Teamwork and Time Management:
a) Ability to participate constructively in class room discussions.
b) Ability to contribute to group work.
c) Ability to meet a deadline.
PSO6: Scientific Reasoning:
a) Ability to analyze texts, evaluating ideas and scientific strategies.
b) Ability to formulate logical and convincing arguments. Reflective Thinking: Ability to locate oneself
and see the influence of location—regional, national, global— on critical thinking.

SYLLABUS

SEMESTER-1

C1 CHEMISTRY
Paper Code (BBT 1001)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40
Course Objective(s)

 To educate the students to develop the knowledge of the fundamental principles of

chemistry

 To enable understanding of the nomenclature, structural, isomerism, stereochemistry of

organic compounds.

Course Outcome(s):

 Students will learn different fundamentals of basic chemistry of different chemistry

branches like organic chemistry, Inorganic, Physical etc.
  Studies includes chemical bonding i.e. formation of different molecules types of bonds,
hybridization, in thermodynamic studies free energy required for chemical and biochemical
reactions and chemical kinetics rates of chemical reaction.
 In stereo chemistry how different molecules/ bio-molecules are presented by different
methods along with their stereo aspects like chirality, etc.
 They will also learn electrochemical aspects during their course.
 They will also perform experimental verification of some parts of theory.

THEORY

Unit 1: Chemical Energetics (10 Lectures)

A Review of the Laws of Thermodynamics Important principles and definitions of
thermochemistry. Concept of standard state and standard enthalpies of formation, integral and
differential enthalpies of solution and dilution Calculation of bond energy, bond dissociation
energy, and resonance energy from thermochemical data Variation of enthalpy of a reaction with
temperature—Kirchhoff’s equation Statement of the Third Law of Thermodynamics and
calculation of the absolute entropies of substances

Unit 2: Chemical Equilibrium and Ionic Equilibrium (10 Lectures)

Free energy change in a chemical reaction. Thermodynamic derivation of the law of chemical
equilibrium. Distinction between ΔG and ΔGo , Le Chatelier’s principle. Relationships between
Kp, Kc and Kx for reactions involving ideal gases.
Strong, moderate and weak electrolytes, degree of ionization, factors affecting degree of
ionization, ionization constant and ionic product of water. Ionization of weak acids and bases, pH
scale, common ion effect. Salt hydrolysis-calculation of hydrolysis constant, degree of hydrolysis
and pH for different salts. Buffer solutions. Solubility and solubility product of sparingly soluble
salts – applications of solubility product principle.

Unit 3: Stereochemistry (10 Lectures)

Writing of Fischer projection, Newmann and Sawhorse projection and Wedge formulae.
Interconversion of one type of structural representation into another type. Conformations:
Restricted rotation about single bonds, Various conformations of ethane, butane, ethane-1,2-diol
and cyclohexane. Relative stability of different conformations in terms of energy difference is to
be discussed for all these compounds. Geometrical Isomerism: Requirements for a molecule to
show geometrical isomerism, CisTrans and E/ Z notation along with CIP rules for geometrical
isomers. Optical Isomerism: Optical activity, specific and molar rotation, chirality,
enantiomerism, diastereoisomers, racemic mixtures and their resolution by salt formation method.
Relative and absolute configuration: D / L nomenclature system for configuration of carbohydrates
(difference between d/l and D/L notations). Threo and Erythro designation. Rand S- configuration
(upto two chiral centres).

Unit 5: Substitution Reactions and Spectroscopy (10 Lectures)

Free radical substitution reactions: Halogenation of alkanes, allylic compounds and alkyl
benzenes. 34Nucleophilic substitution reactions: Mechanism of SN1 and SN2 reactions
(stereochemistry, nature of substrate, nucleophile and leaving group), Electrophilic Substitution
Reactions (aromatic compounds): General mechanism of electrophilic substitution reactions
(nitration, halogenation, sulphonation, Friedel Crafts alkylation and acylation), directive influence
of substituents.
Introduction to spectroscopy: Electromagnetic radiation, fundamental definitions,
electromagnetic spectrum, introduction to concepts of absorption and emission spectroscopy,
Beer-Lambert law. IR Spectroscopy: Fundamental and non-fundamental molecular vibrations, IR
spectrum, Study of hydrogen bonding. Electronic Spectroscopy: Electronic transitions, singlet and
triplet states, dissociation and predissociation. Laws of photochemistry: Fluorescence and
phosphorescence. Primary and secondary processes in photochemical reactions. Photochemical
and thermal reactions.

PRACTICALS

Organic preparations: Carry out the following preparations using 0.5 - 1 g of starting compound.
Recrystallize the product and determine the melting point of the recrystallized sample.
1. To prepare acetanilide by the acetylation of aniline.
2. To prepare p-bromoacetanilide.
3. Benzolyation of aniline or β-naphthol by Schotten-Baumann reaction
4. Hydrolysis of benzamide or ethyl bezoate.

Thermochemistry:
1. Determination of heat capacity of a calorimeter for different volumes.
2. Determination of the enthalpy of neutralization of hydrochloric acid with sodium hydroxide.
3. Determination of integral enthalpy of solution of salts (endothermic and exothermic).
pH-metric and potentiometric measurements:
1. Preparation of sodium acetate-acetic acid buffer solutions and measurement of their pH.
2. Potentiometric titrations of (i) strong acid vs strong base (ii) weak acid vs strong base
3. Determination of dissociation constant of a weak acid.

RECOMMENDED TEXTS
 1. Atkins, P. W. & Paula, J. de Atkin’s Physical Chemistry 9th Ed., Oxford University Press
(2011).
2. Ball, D. W. Physical Chemistry Thomson Press, India (2007).
3. Castellan, G. W. Physical Chemistry 4th Ed. Narosa (2004).
4. Mortimer, R. G. Physical Chemistry 3rd Ed. Elsevier: NOIDA, UP (2009).
5. Chang, R. Physical Chemistry for the Biosciences. University Science Books (2005).
6. I. L. Finar: Organic Chemistry (Vol. I & II), E. L. B. S.
7. R. T. Morrison & R. N. Boyd: Organic Chemistry, Pearson Education

C2 CELL BIOLOGY

Paper Code (BBT 1002)

(Credits: Theory-4, Practicals-2)

THEORY Lectures: 60

Course Objective(s):

● This course introduces the students to the basics of cell and its components.
● This gives them a strong foundation on the basic unit of life.
● The present course has been devised to familiarize students with the structural and functional
aspects of cell, the basic unit of life, and its different organelles. Knowing the components of
cells and how they work is fundamental to all biological sciences.

Course Outcome(s):

● Understanding of the structure of cell and various cellular events.

● Understanding of the function of various subcellular organelles.

● Students will learn about cell theory and techniques for fractionation of sub-cellular
organelles.

● They will be acquainted to various microscopic techniques to visualize subcellular

organelles.

● Students will have an understanding of the composition of cytoskeleton and extracellular

matrix.
 ● Students will acquire knowledge of cell cycle, cell division and cell death mechanisms.

THEORY

UNIT I (10 Periods)

Cell: introduction and classification of organisms by cell structure, cytosol, compartmentalization
of eukaryotic cells, cell fractionation. Cell Membrane and Permeability: Chemical Components of
Biological Membranes, Organization and Fluid Mosaic Model, Membrane as a dynamic entity,
cell recognition and membrane transport.

UNIT II (10 Periods)

Membrane Vacuolar system, cytoskeleton and cell motility: Structure and function of
microtubules, Microfilaments, Intermediate filaments. Endoplasmic reticulum: Structure, function
including role in protein segregation. Golgi complex: Structure, biogenesis and functions including
role in protein secretion.

UNIT III (10 Periods)

Lysosomes: Vacuoles and micro bodies: Structure and functions Ribosomes: Structures and
function including role in protein synthesis. Mitochondria: Structure and function, Genomes,
biogenesis. Chloroplasts: Structure and function, genomes, biogenesis Nucleus: Structure and
function, chromosomes and their structure.

UNIT IV (10 Periods)

Extracellular Matrix: Composition, molecules that mediate cell adhesion, membrane receptors for
extracellular matrix, macromolecules, regulation of receptor expression and function. Signal
transduction. Cancer: Carcinogenesis, agents promoting carcinogenesis, characteristics and
molecular basis of cancer.

PRACTICALS

1. Study the effect of temperature and organic solvents on semi permeable membrane.
2. Demonstration of dialysis.
3. Study of plasmolysis and de-plasmolysis.
4. Cell fractionation and determination of enzyme activity in organelles using sprouted seed or any
other suitable source.
5. Study of structure of any Prokaryotic and Eukaryotic cell.
6. Microtomy: Fixation, block making, section cutting, double staining of animal tissues like liver,
oesophagus, stomach, pancreas, intestine, kidney, ovary, testes.
7. Cell division in onion root tip/ insect gonads. 8. Preparation of Nuclear, Mitochondrial &
cytoplasmic fractions.

SUGGESTED READING
1. Karp, G. 2010. Cell and Molecular Biology: Concepts and Experiments. 6th Edition. John
Wiley & Sons. Inc.
2. De Robertis, E.D.P. and De Robertis, E.M.F. 2006. Cell and Molecular Biology.
8thedition.Lippincott Williams and Wilkins, Philadelphia.
3. Cooper, G.M. and Hausman, R.E. 2009. The Cell: A Molecular Approach. 5th edition.
ASMPress& Sunderland, Washington, D.C.; Sinauer Associates, MA.
4. Becker, W.M., Kleinsmith, L.J., Hardin. J. and Bertoni, G. P. 2009. The World of the Cell. 7th
edition. Pearson Benjamin Cummings Publishing, San Francisco.

AECC1 ENGLISH

Paper Code (BBT 1003)

(Credits 4: Theory-4)

Lectures: THEORY: 20

Course Objective(s):

● This course is designed to develop communication and vocabulary skills in the students.

Course Outcome(s):

● Analyze and restate the meaning of a text in English

● Demonstrate the skill to write in English without grammatical error
● Practice listening effectively to communication in English
● Develop the ability to speak English language with the right way of pronunciation
● Express the viewpoints with confidence in English
● Express values and skills gained through effective communication to other disciplines
● Compose articles and compositions in English
● Discuss and socialize effectively in English

THEORY

Introduction:
Theory of Communication, Types and modes of Communication Language of Communication: -
Verbal and Non-verbal (Spoken and Written) - Personal, Social and Business - Barriers and
Strategies - Intra Personal, Inter Personal and Group Communication

Speaking Skills:
Monologue - Dialogue - Group Discussion - Effective Communication/ Mis- Communication -
Interview - Public Speech Reading and Understanding - Close Reading - Comprehension -
Summary Paraphrasing - Analysis and Interpretation – Translation (from Indian language to
English and vice-versa) Literary/Knowledge Texts

Writing Skills:
Documenting - Report Writing - Making notes - Letter Writing

SUGGESTED READING

1. Language through Literature (forthcoming) ed. Dr. Gauri Mishra, Dr Ranjana Kaul, Dr Brat
Biswas
2. Fluency in English Part II Oxford University Press, 2006
3. Business English, Pearson, 2008.

GE1 BIOTECHNOLOGY AND HUMAN WELFARE

Paper Code (BBT 1004 [A])
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40
Course Objective(s):

● To introduce methods and strategies commonly used in protein engineering, polysaccharide production.
● To acquire knowledge and application of beneficial microbes in the agriculture sector.
● To study and understand the impact of development on environment safety and its significance for
sustainable ways of development.
● To provide knowledge of the basics about implications of biotechnology in Human Health and Forensic
Sciences.

Course Outcome(s):

● Recognize the importance of various molecular techniques used in biotechnological

industry and the importance of modern agriculture and its application.
● Understand the importance of biotechnology in relation to environment and pollution.
● Learn about various applications-based techniques in biotechnology like forensic science
and the related activities currently going on and that will lay the foundations for the
future work in relation to crime.
● Comprehend the application of biotechnology in therapeutic drug and vaccine
development, gene therapy and diagnostics

THEORY

UNIT I (10 Periods)

Industry: protein engineering; enzyme and polysaccharide synthesis, activity and secretion,
alcohol and antibiotic formation.

UNIT II (10 Periods)

Agriculture: N2 fixation: transfer of pest resistance genes to plants; interaction between plants and
microbes; qualitative improvement of livestock.

UNIT III (10 Periods)

Environments: e.g. chlorinated and non-chlorinated organ pollutant degradation; degradation of
hydrocarbons and agricultural wastes, stress management, development of biodegradable
polymers such as PHB.

UNIT IV (05 Periods)

Forensic science: e.g. solving violent crimes such as murder and rape; solving claims of paternity
and theft etc. using various methods of DNA finger printing.

UNIT V (05 Periods)

Health: e.g. development of non-toxic therapeutic agents, recombinant live vaccines, gene therapy,
diagnostics, monoclonal in E.coli, human genome project.

PRACTICALS

(Wherever wet lab experiments are not possible, the principles and concepts can be demonstrated
through any other material or medium including videos/virtual labs etc.)

1. Perform of ethanolic fermentation using Baker’s yeast

2. Study of a plant part infected with a microbe
3. To perform quantitative estimation of residual chlorine in water samples
4. Isolation and analysis of DNA from minimal available biological samples
5. Case studies on Bioethics (any two)

SUGGESTED READING
1. Sateesh MK (2010) Bioethics and Biosafety, I. K. International Pvt Ltd.
2. Shree Krishna V (2007) Bioethics and Biosafety in Biotechnology, New age international
publishers

GE2 I.P.R. ENTREPRENEURSHIP BIOETIHCS & BIOSAFETY

Paper Code (BBT 1004 [B])
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 60
Course Objective(s):

● To develop the understanding of Intellectual property, Entrepreneurship, IPR, Biosafety, GMO

and bioethics.

Course Outcome(s):

 Teachings like good laboratory procedure and practices, standard operating procedures
for biotechnology research, legal and institutional framework for biosafety, international
agreements and protocols for biosafety.
 Learn about the Intellectual property rights and their usages to protect work created by
human mind that has commercial value.
 Makes students aware about different national and international IPR issues including
patents, trademarks, copyrights etc. and various international agreements and treaties.
 The course makes student understand the Regulatory bodies for Bioethics in India and
International considerations.
 Students will become aware of Institutional Ethical Committee and International laws on
Biosafety. Students will analyse and imbibe the Objectives and role of WIPO which will
also help in interpreting impact of Intellectual property and its legal protection in
research.
 The course is designed to have applications of research in innovation and
entrepreneurship by involving the significance of patents and copyrights to have
sustenance at global level.

THEORY

UNIT-I (10 Periods)

Introduction to Indian Patent Law. World Trade Organization and its related intellectual property
provisions. Intellectual/Industrial property and its legal protection in research, design and
development. Patenting in Biotechnology, economic, ethical and depository considerations.

UNIT II (10 Periods)

Entrepreneurship: Selection of a product, line, design and development processes, economics on
material and energy requirement, stock the product and release the same for making etc. The basic
regulations of excise: Demand for a given product, feasibility of its production under given
constraints of raw material, energy input, financial situations export potential etc.

UNIT III (10 Periods)

Bioethics – Necessity of Bioethics, different paradigms of Bioethics – National & International.
Ethical issues against the molecular technologies.

UNIT IV (10 Periods)

Biosafety– Introduction to biosafety and health hazards concerning biotechnology. Introduction to
the concept of containment level and Good Laboratory Practices (GLP) and Good Manufacturing
Practices (GMP).

PRACTICALS

1. Proxy filing of Indian Product patent

2. Proxy filing of Indian Process patent
3. Planning of establishing a hypothetical biotechnology industry in India
4. A case study on clinical trials of drugs in India with emphasis on ethical issues.
5. Case study on women health ethics.
6. Case study on medical errors and negligence.
7. Case study on handling and disposal of radioactive waste.

SUGGESTED READING

1. Entrepreneurship: New Venture Creation : David H. Holt

2. Patterns of Entrepreneurship: Jack M. Kaplan
3. Entrepreneurship and Small Business Management: C.B. Gupta, S.S. Khanka, Sultan Chand &
Sons.
4. Sateesh MK (2010) Bioethics and Biosafety, I. K. International Pvt Ltd. 5. Sree Krishna V
(2007) Bioethics and Biosafety in Biotechnology, New age international publishers

SEMESTER-2

C3 MAMMALIAN PHYSIOLOGY
Paper Code (BBT 2001)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40
Course Objective(s):
● To understand the basic concept of mammalian digestion, respiration, circulation, muscular
system and nervous system.

Course Outcome(s):

 Illustrate the integration of individual functions of all cells, tissues and organs into
functional whole-human body.
 Detect gross organs in the body
 Identify various bones of the skeletal system
 Find various blood indices
 Determine the blood groups
 Measure blood pressure
 Integrate the knowledge of whole body organs and their mechanisms.
 Compare various health conditions and their effects.

THEORY

UNIT I: Digestion and Respiration (10 Periods)

Digestion: Mechanism of digestion & absorption of carbohydrates, Proteins, Lipids and nucleic
acids. Composition of bile, Saliva, Pancreatic, gastric and intestinal juice Respiration: Exchange
of gases, Transport of O2 and CO2, Oxygen dissociation curve, Chloride shift.

UNIT II: Circulation (10 Periods)

Composition of blood, Plasma proteins & their role, blood cells, Haemopoisis, Mechanism of
coagulation of blood. Mechanism of working of heart: Cardiac output, cardiac cycle, Origin &
conduction of heart beat.

UNIT III: Muscle physiology and osmoregulation (10 Periods)

Structure of cardiac, smooth & skeletal muscle, threshold stimulus, All or None rule, single muscle
twitch, muscle tone, isotonic and isometric contraction, Physical, chemical & electrical events of
mechanism of muscle contraction. Excretion: modes of excretion, Ornithine cycle, Mechanism of
urine formation.

UNIT IV: Nervous and endocrine coordination (10 Periods)

Mechanism of generation & propagation of nerve impulse, structure of synapse, synaptic
conduction, saltatory conduction, Neurotransmitters Mechanism of action of hormones (insulin
and steroids) Different endocrine glands– Hypothalamus, pituitary, pineal, thymus, thyroid,
parathyroid and adrenals, hypo & hyper-secretions.

PRACTICALS
1. Finding the coagulation time of blood
2. Determination of blood groups
3. Counting of mammalian RBCs
4. Determination of TLC and DLC
5. Demonstration of action of an enzyme
6. Determination of Haemoglobin

SUGGESTED READING

1. Guyton, A.C. & Hall, J.E. (2006). Textbook of Medical Physiology. XI Edition. Hercourt Asia
PTE Ltd. /W.B. Saunders Company.
2. Tortora, G.J. & Grabowski, S. (2006). Principles of Anatomy & Physiology. XI Edition. John
wiley&sons,Inc.

C4 PLANT ANATOMY AND PHYSIOLOGY

Paper Code (BBT 2002)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40
Course Objective(s):

● To develop the understanding of plant anatomy, growth and development.

● To develop understanding of nutrients requirement of plants.

Course Outcome(s):

 Understand the basics of plant physiology and physiological mechanisms governing plant
growth and development
 Learn the basics of transport in plants and movement of solutes and water
 Remember the basics of photosynthesis, respiration and hormonal signalling as it impacts
plant growth and development
 Comprehend and increase the awareness and appreciation for plants in environment, as
well as to understand their diverse physiological functions.

THEORY

UNIT I: Anatomy (10 Periods)

The shoot and root apical meristem and its histological organization, simple & complex permanent
tissues, primary structure of shoot & root, secondary growth, growth rings, leaf anatomy (dorsi-
ventral and isobilateral leaf)

UNIT II: Plant water relations and micro &macro nutrients (10 Periods)
Plant water relations: Importance of water to plant life, diffusion, osmosis, plasmolysis, imbibition,
guttation, transpiration, stomata & their mechanism of opening & closing. Micro &macro
nutrients: criteria for identification of essentiality of nutrients, roles and deficiency systems of
nutrients, mechanism of uptake of nutrients, mechanism of food transport.

UNIT III: Carbon and nitrogen metabolism (10 Periods)

Photosynthesis- Photosynthesis pigments, concept of two photo systems, photphosphorylation,
calvin cycle, CAM plants, photorespiration, compensation point Nitrogen metabolism- inorganic
& molecular nitrogen fixation, nitrate reduction and ammonium assimilation in plants.

UNIT IV: Growth and development (10 Periods)

Growth and development: Definitions, phases of growth, growth curve, growth hormones (auxins,
gibberlins, cytokinins, abscisic acid, ethylene) Physiological role and mode of action, seed
dormancy and seed germination, concept of photoperiodism and vernalization.

PRACTICALS

1. Preparation of stained mounts of anatomy of monocot and dicot’s root, stem & leaf.
2. Demonstration of plasmolysis by Tradescantia leaf peel.
3. Demonstration of opening & closing of stomata
4. Demonstration of guttation on leaf tips of grass and garden nasturtium.
5. Separation of photosynthetic pigments by paper chromatography.
6. Demonstration of aerobic respiration.
7. Preparation of root nodules from a leguminous plant.

SUGGESTED READING

1. Dickinson, W.C. 2000 Integrative Plant Anatomy. Harcourt Academic Press, USA.
2. Esau, K. 1977 Anatomy of Seed Plants. Wiley Publishers.
3. Fahn, A. 1974 Plant Anatomy. Pergmon Press, USA and UK.
4. Hopkins, W.G. and Huner, P.A. 2008 Introduction to Plant Physiology. John Wiley and Sons.
5. Mauseth, J.D. 1988 Plant Anatomy. The Benjammin/Cummings Publisher, USA.
6. Nelson, D.L., Cox, M.M. 2004 Lehninger Principles of Biochemistry, 4 th edition, W.H.
Freeman and Company, New York, USA.
7. Salisbury, F.B. and Ross, C.W. 1991 Plant Physiology, Wadsworth Publishing Co. Ltd. 8. Taiz,
L. and Zeiger, E. 2006 Plant Physiology, 4 th edition, Sinauer Associates Inc .MA, USA
 AECC2 ENVIRONMENTAL SCIENCES
Paper Code (BBT 2003)
(Credits 4: Theory-4)
Lectures: THEORY: 20
Course Objective(s)

● To provide Knowledge about the importance of conserving biodiversity and to acquire a broad
base of knowledge of environmental systems
● It enables the students to understand the fundamental and applied aspects of environmental
biotechnology
● To understand the pros and cons of the usage of bioscience in various aspects of environment
and its applications

Course Outcome(s):

● Student understood the concept of environmental pollution, types of pollutants and

related hazards.
● Acquire knowledge on environment protection acts and understand the need to conserve
environment by implementing policies with the help of different organizations.
● Students will understand the structure, growth and the interactions of populations in the
environment. Build awareness on disaster management, environmental movements and
ethics.
● Field visit enhance the skill techniques among the students to document assets, study
local polluted site and ecosystem structure and environmental impact.

THEORY

Unit 1: Introduction to environmental studies (2 lectures)

Multidisciplinary nature of environmental studies; Scope and importance; Concept of
sustainability and sustainable development.

Unit 2: Ecosystems (6 lectures)

What is an ecosystem? Structure and function of ecosystem; Energy flow in an ecosystem: food
chains, food webs and ecological succession. Case studies of the following ecosystems: a) Forest
ecosystem b) Grassland ecosystem c) Desert ecosystem d) Aquatic ecosystems (ponds, streams,
lakes, rivers, oceans, estuaries)
Unit 3: Natural Resources (8 lectures)
Renewable and Non-renewable Resources, Land resources and landuse change; Land degradation,
soil erosion and desertification. Deforestation: Causes and impacts due to mining, dam building
on environment, forests, biodiversity and tribal populations. Water: Use and over-exploitation of
surface and ground water, floods, droughts, conflicts over water (international & inter-state).
Energy resources: Renewable and non renewable energy sources, use of alternate energy sources,
growing energy needs, case studies.

Unit 4: Biodiversity and Conservation (8 lectures)

Levels of biological diversity : genetic, species and ecosystem diversity; Biogeographic zones of
India; Biodiversity patterns and global biodiversity hot spots, India as a mega-biodiversity nation;
Endangered and endemic species of India, Threats to biodiversity : Habitat loss, poaching of
wildlife, man-wildlife conflicts, biological invasions; Conservation of biodiversity : In-situ and
Ex-situ conservation of biodiversity. Ecosystem and biodiversity services: Ecological, economic,
social, ethical, aesthetic and Informational value.

Unit 5: Environmental Pollution (8 lectures)

Environmental pollution: types, causes, effects and controls; Air, water, soil and noise pollution,
Nuclear hazards and human health risks, Solid waste management: Control measures of urban and
industrial waste. Pollution case studies.

Unit 6: Environmental Policies & Practices (7 lectures)

Climate change, global warming, ozone layer depletion, acid rain and impacts on human
communities and agriculture 2/2, Environment Laws: Environment Protection Act; Air
(Prevention & Control of Pollution) Act; Water (Prevention and control of Pollution) Act; Wildlife
Protection Act; Forest Conservation Act. International agreements: Montreal and Kyoto protocols
and Convention on Biological Diversity (CBD). Nature reserves, tribal populations and rights, and
human wildlife conflicts in Indian context.

Unit 7: Human Communities and the Environment (6 lectures)

Human population growth: Impacts on environment, human health and welfare. Resettlement and
rehabilitation of project affected persons; case studies. Disaster management: floods, earthquake,
cyclones and landslides. Environmental movements: Chipko, Silent valley, Bishnois of Rajasthan.
Environmental ethics: Role of Indian and other religions and cultures in environmental
conservation. Environmental communication and public awareness, case studies (e.g., CNG
vehicles in Delhi).

Unit 8: Field work (Equal to 5 lectures)

Visit to an area to document environmental assets: river/ forest/ flora/fauna, etc.
Visit to a local polluted site-Urban/Rural/Industrial/Agricultural.
Study of common plants, insects, birds and basic principles of identification.
Study of simple ecosystems-pond, river, Delhi Ridge, etc.

SUGGESTED READINGS:

1. Carson, R. 2002. Silent Spring. Houghton Mifflin Harcourt.

2. Gadgil, M., & Guha, R. 1993. This Fissured Land: An Ecological History of India. Univ. of
California Press. 3. Gleeson, B. and Low, N. (eds.) 1999. Global Ethics and Environment,
London, Routledge.
4. Gleick, P. H. 1993. Water in Crisis. Pacific Institute for Studies in Dev., Environment &
Security. Stockholm Env. Institute, Oxford Univ. Press.
5. Groom, Martha J., Gary K. Meffe, and Carl Ronald Carroll. Principles of Conservation Biology.
Sunderland: Sinauer Associates, 2006.
6. Grumbine, R. Edward, and Pandit, M.K. 2013. Threats
7. Singh, J.S., Singh, S.P. and Gupta, S.R. 2014. Ecology, Environmental Science and Conservation. S.
Chand Publishing, New Delhi.
8. Sodhi, N.S., Gibson, L. & Raven, P.H. (eds). 2013. Conservation Biology: Voices from the Tropics.
John Wiley & Sons.

GE2 GENE ORGANIZATION, EXPRESSION AND REGULATION

Paper Code (BBT 2004 [A])
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40

Course Objective(s):

● To develop the understanding of genes, chromosomes, transcription and translation.

Course Outcome(s):

 Define the roles of DNA and proteins in cell development and metabolism
 Determine the amino acid sequence of a protein given the nucleotide sequence of a gene.
 Describe the roles that the promoter, coding region, and, termination sequence of a gene play
in gene expression.
 Recognize the differences between the structure of proteins, amino acids, genes, and
nucleotides
 Draw the process of gene expression and include the following in your drawing. Gene, RNA
polymerase, promoter, coding region, termination sequence, intron, cell, nucleus, cytoplasm,
RNA, tRNA, ribosome, anticodon, codon, amino acid, protein, peptide bond.
THEORY

Unit 1 Structure of genes and chromosomes (Lectures : 6)

Definition of a gene, chromosomal organization of genes in viruses, bacteria and eukaryotes.
Supercoiling of DNA.

Unit 2 Replication of genomes (Lectures: 6)

General features of DNA replication, properties of prokaryotic and eukaryotic DNA polymerases.
Replication of DNA and telomeres in linear chromosomes. Replication of RNA genomes.

Unit 3 Recombination of DNA (Lectures: 4)

Homologous genetic recombination, Holliday model, proteins and enzymes mediating
recombination.

Unit 4 Gene mutations and repair (Lectures: 6)

Molecular basis of mutations, multiple repair systems, mismatch repair, base excision repair,
nucleotide excision repair, direct repair and translation DNA synthesis.

Unit 5 Transcription of genes (Lectures: 6)

General features of gene transcription, prokaryotic and eukaryotic RNA polymerases, stages of
transcription, initiation, elongation and termination. Inhibitors of transcription.

Unit 6 RNA processing (Lectures: 3)

Processing of eukaryotic mRNA, splicing of introns, alternate splicing and editing, ribosomal and
tRNA processing.

Unit 7 Protein synthesis (Lectures: 5)

Features of the genetic code, amino acylation of tRNAs, structure and assembly of ribosomes;
three stages of protein synthesis - initiation, elongation and termination. Inhibitors of protein
synthesis.

Unit 8 Regulation of gene expression (Lectures: 4)

Regulation of transcription in prokaryotes, concept of operons. Lac operon - control by negative
and positive regulatory proteins, Trp operon - control by attenuation. Regulation of transcription
in eukaryotes, regulatory sequences - enhancers, silencers response elements, nucleosome
alterations, DNA-protein interactions and RNA interference.

PRACTICALS

1. Quantitative determination of DNA and RNA by absorbance at 260 nm and using A260/A280
ratio to distinguish between them.
2. To study the viscosity of DNA solutions.
3. Isolation of chromosomal DNA from E. coli.
4. Isolation of total RNA from yeast cells.

SUGGESTED READINGS

1. Lehninger: Principles of Biochemistry (2013) 6th ed., Nelson, D.L. and Cox, M.M., W.H.
Freeman and Company (New York), ISBN:13; 978-1-4641-0962-1 / ISBN:10-14641- 0962-1.

GE2 DEVELOPMENTAL BIOLOGY

Paper Code (BBT 2004 [B])
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40
Course Objective(s):

● Describe the events in the developmental process,

● Predict the results of genetic or embryological manipulations, based on their knowledge of the
developmental process,
● Make hypotheses about the mechanisms involved in the process based on experimental results
● Design experiments to test hypotheses about the developmental process.

Course Outcome(s):

● Name, describe and order the main stages of development common to most multicellular
organisms.
● Describe the main anatomical changes that occur during development.
● Identify the cellular behaviors that lead to morphological change during development.
● Describe the hierarchy of gene activation that occurs in early Drosophila development.
● Understand how gene activation plays a role in differentiation and development.
 ● Describe the unique characteristics of the Hox genes and explain how they act as master
regulators of development in multicellular organisms.
● Describe the main signaling pathways that play important roles in development.
● Explain how embryonic stem cells and their alternatives can be used in medical treatments
THEORY

UNIT I: Gametogenesis and Fertilization (10 Periods)

Definition, scope & historical perspective of development Biology, Gametogenesis –
Spermatogenesis, Oogenesis Fertilization - Definition, mechanism, types of fertilization. Different
types of eggs on the basis of yolk.

UNIT II: Early embryonic development (20 Periods)

Cleavage: Definition, types, patterns & mechanism Blastulation: Process, types & mechanism
Gastrulation: Morphogenetic movements–epiboly, emboly, extension, invagination, convergence,
de-lamination. Formation & differentiation of primary germ layers, Fate Maps in early embryos.

UNIT III: Embryonic Differentiation (20 Periods)

Differentiation: Cell commitment and determination- the epigenetic landscape: a model of
determination and differentiation, control of differentiation at the level of genome, transcription
and post-translation level Concept of embryonic induction: Primary, secondary & tertiary
embryonic induction, Neural induction and induction of vertebrate lens.

UNIT IV: Organogenesis (10 Periods)

Neurulation, notogenesis, development of vertebrate eye. Fate of different primary germ layers
Development of behaviour: constancy & plasticity, Extra embryonic membranes, placenta in
Mammals.

PRACTICALS

1. Identification of developmental stages of chick and frog embryo using permanent mounts
2. Preparation of a temporary stained mount of chick embryo
3. Study of developmental stages of Anopheles.
4. Study of the developmental stages of Drosophila from stock culture/ photographs.
5. Study of different types of placenta.

SUGGESTED READING

1. Gilbert, S. F. (2006). Developmental Biology, VIII Edition, Sinauer Associates, Inc., Publishers,
Sunderland, Massachusetts, USA.
2. Balinsky, B.I. (2008). An introduction to Embryology, International Thomson Computer Press.
3. Kalthoff, (2000). Analysis of Biological Development, II Edition, McGraw-Hill Professional.

SEMESTER-3
C5 GENERAL BIOCHEMISTRY
Paper Code (BBT 3001)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40
Course Objective(s)

● Understand the basics of biomolecules and surrounding interaction.

● Understand basic details of amino acid & protein molecules, carbohydrate, Nucleic Acid, Lipid,
vitamin molecules and their classification
● Understand the basics of macromolecules involved in the Cellular Signaling

Course Outcome(s):

 As Biochemistry is the branch of science concerned with the chemical and physico-chemical
processes and substances that occur within living organisms, therefore students will be able to
understand how biomolecules relate to a particular process (metabolism) within a living cell.
 Students will be acquainted with the knowledge of structures, functions, and interactions of
proteins, nucleic acids, carbohydrates and lipids.
 The course will help the students to understand the abnormalities in the metabolism their
relationship to various diseases. In addition to, it will help to understand the mechanism
underlying correct disorders with dietary modifications or genetic modifications.
 Students will learn about enzyme kinetics and types of inhibition as enzymes are important in
catalyzing various reactions in the body

THEORY

Unit 1 Biomolecules in their cellular environment (05 lectures)

The cellular basis of life. Cellular structures – prokaryotes and eukaryotes. Chemical principles in
biomolecular structure. Major classes of biomolecules. Role of water in design of biomolecules.

Unit 2 Amino acids and peptides (05 lectures)

Types of amino acids and their chemistry, derivatives of amino acids and their biological role.
Introduction to biologically important peptides.

Unit 3 Sugars and polysaccharides (05 lectures)

Basic chemistry of sugars, optical activity. Disaccharides, trisaccharides and polysaccharides -
their distribution and biological role.
Unit 4 Nucleosides, nucleotides and nucleic acids (05 lectures)
Structures and chemistry, DNA structures and their importance, different types of RNA. Unusual
DNA structures, other functions of nucleotides.

Unit 5 Lipids (10 lectures)

Various classes of lipids and their distribution, storage lipids, structural lipids in membranes, lipids
as signals, cofactors and pigments.

Unit 6 Vitamins, coenzymes and metal ions (05 lectures)

Occurrence and nutritional role. Coenzymes and their role in metabolism. Metal ion containing
biomolecules - heme, porphyrins and cyanocobalamin; their biological significance.

Unit 7 Signalling molecules (05 lectures)

Second messengers - cAMP, cGMP, IP3, diacyl glycerol, Ca2+, NO. Brief account of their
importance and role in signalling and signal transduction.

PRACTICALS
1. General safety procedures in a laboratory. Use of auto pipettes. Making solutions and buffer
preparation - acetate and tris buffers.
2. Qualitative tests for biomolecules - carbohydrates, lipids, amino acids, proteins, bases and
nucleic acids.
3. Separation of amino acids by paper chromatography.
4. Separation of sugars/bases by TLC and their identification.
5. Estimation of ascorbic acid in fruit juices.

SUGGESTED READINGS
1. Lehninger: Principles of Biochemistry (2013) 6th ed., Nelson, D.L. and Cox, M.M., W.H.
Freeman and Company (New York), ISBN:13; 978-1-4641-0962-1 / ISBN:10-14641- 0962-1.
2. Textbook of Biochemistry with Clinical Correlations (2011) 7th ed., Devlin, T.M., John Wiley
& Sons, Inc. (New York), ISBN:978-0-470-28173-4.

C6 GENERAL MICROBIOLOGY
Paper Code (BBT 3002)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40

Course Objective(s)
● 1. To make the students to understand the basic concepts of the biology of microorganisms
 ● 2. To learn the general principles for microbial the growth, evolution and classification
● 3. To make the students to understand the role of microbes in human life.

Course Outcome(s):
● To become aware with the contributions of Louis Pasteur, Edward Jenner and Robert Koch
in microbiology and immunology.
● To get acquainted with the discovery of antibiotics and their targets, drug/antibiotic
resistance, preventive and therapeutic approaches of infectious diseases, hospital acquired
infections.
● Understanding the importance of microorganisms as model systems in genetics and
biochemistry.
● To know the contribution of gut microbiome in human health.
● Exposure to the basic concepts of metabolic engineering and synthetic biology.
● To understand the concepts of fight against major killer diseases – tuberculosis, HIV and
malaria.

THEORY

UNIT I (10 Periods)

Fundamentals, History and Evolution of Microbiology. Classification of microorganisms:
Microbial taxonomy, criteria used including molecular approaches, Microbial phylogeny and
current classification of bacteria. Microbial Diversity: Distribution and characterization
Prokaryotic and Eukaryotic cells, Morphology and cell structure of major groups of
microorganisms eg. Bacteria, Algae, Fungi, Protozoa and Unique features of viruses.

UNIT II (10 Periods)

Cultivation and Maintenance of microorganisms: Nutritional categories of micro-organisms,
methods of isolation, Purification and preservation.

UNIT III (10 Periods)

Microbial growth: Growth curve, Generation time, synchronous batch and continuous culture,
measurement of growth and factors affecting growth of bacteria. Microbial Metabolism: Metabolic
pathways, amphi-catabolic and biosynthetic pathways Bacterial Reproduction: Transformation,
Transduction and Conjugation. Endospores and sporulation in bacteria.

UNIT IV (10 Periods)

Control of Microorganisms: By physical, chemical and chemotherapeutic Agents Water
Microbiology: Bacterial pollutants of water, coliforms and non coliforms. Sewage composition
and its disposal. Food Microbiology: Important microorganism in food Microbiology: Moulds,
Yeasts, bacteria. Major food born infections and intoxications, Preservation of various types of
foods. Fermented Foods.

PRACTICALS

1. Isolation of bacteria & their biochemical characterization.

2. Staining methods: simple staining, Gram staining, spore staining, negative staining, hanging
drop.
3. Preparation of media & sterilization methods, Methods of Isolation of bacteria from different
sources. 4. Determination of bacterial cell size by micrometry. 5. Enumeration of microorganism
- total & viable count.

SUGGESTED READING

1. Alexopoulos CJ, Mims CW, and Blackwell M. (1996). Introductory Mycology. 4 th edition.
John and Sons, Inc.
2. Jay JM, Loessner MJ and Golden DA. (2005). Modern Food Microbiology. 7thedition, CBS
Publishers and Distributors, Delhi, India.
3. Kumar HD. (1990). Introductory Phycology. 2nd edition. Affiliated East Western Press.
4. Madigan MT, Martinko JM and Parker J. (2009). Brock Biology of Microorganisms. 12th
edition. Pearson/Benjamin Cummings.
5. Pelczar MJ, Chan ECS and Krieg NR. (1993). Microbiology. 5th edition. McGraw Hill Book
Company.
6. Stanier RY, Ingraham JL, Wheelis ML, and Painter PR. (2005). General Microbiology. 5th
edition. McMillan.
7. Tortora GJ, Funke BR, and Case CL. (2008). Microbiology: An Introduction. 9 th edition.
Pearson Education.
8. Willey JM, Sherwood LM, and Woolverton CJ. (2008) Prescott, Harley and Klein’s
Microbiology. 7th edition. McGraw Hill Higher Education.

C7 GENETICS
Paper Code (BBT 3003)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40
Course Objective(s):
● To make the students to understand the principles and theories of inheritance.
● To learn the concepts of chromosome morphology.
● To make the students to understand the gene expression and regulation.
Course Outcome(s):
● Students are able to understand the basic concept of transmission of genetics.
● Students enrich with the knowledge of Mendelian and Non-Mendelian genetics.
● Understanding the concepts of gene interactions and its applications in knowing genetic
disorders.
● They learn about chromosomal aberrations and structure of chromosomes.

THEORY

UNIT I (10 Periods)

Introduction: Historical developments in the field of genetics. Organisms suitable for genetic
experimentation and their genetic significance. Cell Cycle: Mitosis and Meiosis: Control points in
cell-cycle progression in yeast. Role of meiosis in life cycles of organisms. Mendelian genetics :
Mendel’s experimental design, monohybrid, di-hybrid and tri hybrid crosses, Law of segregation
& Principle of independent assortment. Verification of segregates by test and back crosses,
Chromosomal theory of inheritance, Allelic interactions: Concept of dominance, recessiveness,
incomplete dominance, co-dominance, semi-dominance, pleiotropy, multiple allele, pseudo-allele,
essential and lethal genes, penetrance and expressivity.

UNIT II (10 Periods)

Non allelic interactions: Interaction producing new phenotype complementary genes, epistasis
(dominant & recessive), duplicate genes and inhibitory genes. Chromosome and genomic
organization: Eukaryotic nuclear genome nucleotide sequence composition –unique & repetitive
DNA, satellite DNA. Centromere and telomere DNA sequences, middle repetitive sequences-
VNTRs & dinucleotide repeats, repetitive transposed sequences- SINEs & LINEs, middle
repetitive multiple copy genes, noncoding DNA. Genetic organization of prokaryotic and viral
genome. Structure and characteristics of bacterial and eukaryotic chromosome, chromosome
morphology, concept of euchromatin and heterochromatin. packaging of DNA molecule into
chromosomes, chromosome banding pattern, karyotype, giant chromosomes, one gene one
polypeptide hypothesis, concept of cistron, exons, introns, genetic code, gene function.

UNIT III (10 Periods)

Chromosome and gene mutations: Definition and types of mutations, causes of mutations, Ames
test for mutagenic agents, screening procedures for isolation of mutants and uses of mutants,
variations in chromosomes structure - deletion, duplication, inversion and translocation (reciprocal
and Robertsonian), position effects of gene expression, chromosomal aberrations in human beings,
abonormalities– Aneuploidy and Euploidy. Sex determination and sex linkage: Mechanisms of sex
determination, Environmental factors and sex determination, sex differentiation, Barr bodies,
dosage compensation, genetic balance theory, Fragile-X-syndrome and chromosome, sex
influenced dominance, sex limited gene expression, sex linked inheritance.
UNIT IV (10 Periods)
Genetic linkage, crossing over and chromosome mapping: Linkage and Recombination of genes
in a chromosome crossing over, Cytological basis of crossing over, Molecular mechanism of
crossing over, Crossing over at four strand stage, Multiple crossing overs Genetic mapping. Extra
chromosomal inheritance: Rules of extra nuclear inheritance, maternal effects, maternal
inheritance, cytoplasmic inheritance, organelle heredity, genomic imprinting. Evolution and
population genetics: In breeding and out breeding, Hardy Weinberg law (prediction, derivation),
allelic and genotype frequencies, changes in allelic frequencies, systems of mating, evolutionary
genetics, natural selection.

PRACTICALS

1. Permanent and temporary mount of mitosis.

2. Permanent and temporary mount of meiosis.
3. Mendelian deviations in dihybrid crosses
4. Demonstration of - Barr Body -Rhoeo translocation.
5. Karyotyping with the help of photographs
6. Pedigree charts of some common characters like blood group, color blindness and PTC tasting.
7. Study of polyploidy in onion root tip by colchicine treatment.

SUGGESTED READING

1. Gardner, E.J., Simmons, M.J., Snustad, D.P. (2006). Principles of Genetics. VIII Edition John
Wiley & Sons.
2. Snustad, D.P., Simmons, M.J. (2009). Principles of Genetics. V Edition. John Wiley and Sons
Inc.
3. Klug, W.S., Cummings, M.R., Spencer, C.A. (2009). Concepts of Genetics. IX Edition.
Benjamin Cummings.
4. Russell, P. J. (2009). Genetics- A Molecular Approach. III Edition. Benjamin Cummings.
5. Griffiths, A.J.F., Wessler, S.R., Lewontin, R.C. and Carroll, S.B. IX Edition. Introduction to
Genetic Analysis, W. H. Freeman & Co.

SEC1 ENZYMOLOGY
Paper Code (BBT 3004)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40
Course Objective(s):
● To understand the theories of enzyme catalysis and the mechanisms of enzyme regulation
 ● To solve enzyme kinetics related exercise and estimate important parameter
● To understand the kinetic of enzyme inhibition and regulation
● To understand the methods for protein sequencing, analysis of secondary and tertiary
structures of enzymes and Protein folding in vitro & in vivo.

Course Outcome(s):
 The subject is of relevance to students from a wide range of disciplines such as health,
environment and medical sciences.
 Students will be able to proceed towards various concepts in biotechnology, the knowledge on
enzyme and enzyme reactions.
 Enzyme kinetics will provide the importance and utility of enzyme kinetics in research.
 Students will learn critical analysis of scientific phenomena involving enzymes and will be able
to competently work with enzyme systems in both academia and industry.
 Students will get an understanding of procedures involved in purification of enzymes, enzymes
assays and quantitative evaluation of the influencing parameters such as concentrations of
substrate / enzyme, pH, temperature and effects of inhibitors on enzyme activity.

THEORY

UNIT - I (10 Periods)

Isolation, crystallization and purification of enzymes, test of homogeneity of enzyme preparation,
methods of enzyme analysis. Enzyme classification (rationale, overview and specific examples)
Zymogens and their activation (Proteases and Prothrombin). Enzyme substrate complex: concept
of E-S complex, binding sites, active site, specificity, Kinetics of enzyme activity, Michaelis-
Menten equation and its derivation, Different plots for the determination of Km and Vmax and
their physiological significance, factors affecting initial rate, E, S, temp. & pH. Collision and
transition state theories, Significance of activation energy and free energy.

UNIT – II (10 Periods)

Two substrate reactions (Random, ordered and ping-pong mechanism) Enzyme inhibition types of
inhibition, determination of Ki, suicide inhibitor. Mechanism of enzyme action: General
mechanistic principle, factors associated with catalytic efficiency: proximity, orientation,
distortion of strain, acid-base, nucleophilic and covalent catalysis. Techniques for studying
mechanisms of action, chemical modification of active site groups, specific examples-:
chymotrypsin, Iysozyme, GPDH, aldolase, RNase, Carboxypeptidase and alcohol dehydrogenase.
Enzyme regulation: Product inhibition, feed backcontrol, covalent modification.

UNIT – III (10 Periods)

Allosteric enzymes with special reference to aspartate transcarbomylase and phosphofructokinase.
Qualitative description of concerted and sequential models. Negative cooperativity and half site
reactivity. Enzyme - Enzyme interaction, Protein ligand binding, measurements analysis of
binding isotherm, cooperativity, Hill and scatchard plots, kinetics of allosteric enzymes.
Isoenzymes– multiple forms of enzymes with special reference to lactate dehydrogenase.
Multienzyme complexes. Ribozymes. Multifunctional enzyme-eg Fatty Acid synthase.

UNIT – IV (10 Periods)

Enzyme Technology: Methods for large scale production of enzymes. Immobilized enzyme and
their comparison with soluble enzymes, Methods for immobilization of enzymes. Immobilized
enzyme reactors. Application of Immobilized and soluble enzyme in health and industry.
Application to fundamental studies of biochemistry. Enzyme electrodes. Thermal stability and
catalytic efficiency of enzyme, site directed mutagenesis and enzyme engineering– selected
examples, Delivery system for protein pharmaceuticals, and structure function relationship in
enzymes, structural motifs and enzyme evolution. Methods for protein sequencing. Methods for
analysis of secondary and tertiary structures of enzymes. Protein folding in vitro & in vivo.

PRACTICALS

1. Purification of an enzyme from any natural resource

2. Quantitative estimation of proteins by Bradford/Lowry’s method.
3. Perform assay for the purified enzyme.
4. Calculation of kinetic parameters such as Km, Vmax, Kcat

SUGGESTED READING

1. Biochemistry, LubertStryer, 6th Edition, WH Freeman, 2006.

2. Harper’s illustrated Biochemistry by Robert K. Murray, David A Bender, Kathleen M.Botham,
Peter J. Kennelly, Victor W. Rodwell, P. Anthony Weil. 28th Edition, McGrawHill, 2009.
3. Biochemistry, Donald Voet and Judith Voet, 2nd Edition, Publisher: John Wiley andSons, 1995.
4. Biochemistry by Mary K.Campbell& Shawn O.Farrell, 5th Edition, Cenage Learning,2005.
5. Fundamentals of Enzymology Nicholas Price and Lewis Stevens Oxford University Press 1999
6. Fundamentals of Enzyme Kinetics Athel Cornish-Bowden Portland Press 2004
7. Practical Enzymology Hans Bisswanger Wiley–VCH 2004
8. The Organic Chemistry of Enzyme-catalyzed Reactions Richard B. Silverman Academic Press
2002

SEMESTER-4
C8 BIOANALYTICAL TOOLS
Paper Code (BBT 4001)
 (Credits: Theory-4, Practicals-2)
THEORY Lectures: 40

Course Objective(s)
 To learn the principle and application of different tools utilized in biotechnology.

Course Outcome(s):
 Develop competence in handing various chromatographic techniques and apply them in
isolating and characterizing different biological molecules.
 Understanding the applications of centrifugation and chromatography in biological
investigations.
 Purify proteins by affinity chromatography using epitope tags such as histidine tag, GST
tag, Flag tag etc.
 Understanding the principles of Electrophoresis, Spectrophotometry and ELISA and their
applications in biological investigations/experiments.

THEORY

UNIT I (10 Periods)

Simple microscopy, phase contrast microscopy, florescence and electron microscopy (TEM and
SEM), pH meter, absorption and emission spectroscopy

UNIT II (10 Periods)

Principle and law of absorption fluorimetry, colorimetry, spectrophotometry (visible, UV,
infrared), centrifugation, cell fractionation techniques, isolation of sub-cellular organelles and
particles.

UNIT III (10 Periods)

Introduction to the principle of chromatography. Paper chromatography, thin layer
chromatography, column chromatography: silica and gel filtration, affinity and ion exchange
chromatography, gas chromatography, HPLC.

UNIT IV (10 Periods)

Introduction to electrophoresis. Starch-gel, polyacrylamide gel (native and SDS-PAGE), agarose-
gel electrophoresis, pulse field gel electrophoresis, immuno- electrophoresis, isoelectric focusing,
Western blotting. Introduction to Biosensors and Nanotechnology and their applications.

PRACTICAL
1. Native gel electrophoresis of proteins
2. SDS-polyacrylamide slab gel electrophoresis of proteins under reducing conditions.
3. Preparation of the sub-cellular fractions of rat liver cells.
4. Preparation of protoplasts from leaves.
5. Separation of amino acids by paper chromatography.
6. To identify lipids in a given sample by TLC.
7. To verify the validity of Beer’s law and determine the molar extinction coefficient of NADH.

SUGGESTED READING

1. Karp, G. 2010. Cell and Molecular Biology: Concepts and Experiments. 6th Edition. John
Wiley& Sons. Inc.
2. De Robertis, E.D.P. and De Robertis, E.M.F. 2006. Cell and Molecular Biology. 8th edition.
Lippincott Williams and Wilkins, Philadelphia.
3. Cooper, G.M. and Hausman, R.E. 2009. The Cell: A Molecular Approach. 5th edition. ASM
Press & Sunderland, Washington, D.C.; Sinauer Associates, MA.
4. Becker, W.M., Kleinsmith, L.J., Hardin. J. and Bertoni, G. P. 2009 The World of the Cell.7th
edition. Pearson Benjamin Cummings Publishing, San Francisco.

C9 INTERMEDIARY METABOLISM
Paper Code (BBT 4002)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 60
Course Objective(s)
 To learn the basic concept of different metabolic pathways.
 Students will be taught the metabolic pathways of carbohydrate, amino acid, lipid and
coenzymes and their regulation.

Course Outcome(s):

● To understand the relevance, basic concepts and theories of chemistry as relevant to a

biological system.
● To understand the properties of biomolecules and their nature of existence in the living
system.
● To understand the relevance and basic concepts of experimental biochemistry.
 ● To understand the nature and commonly used types of biochemical experiments.
● To understand integration of metabolism with the help of different cycles.

THEORY

Unit 1 Basic concepts and design of metabolism (05 Periods)

The nature of metabolism. Role of oxidation and reduction and coupling of these. ATP as energy
currency.

Unit 2: Glycolysis and gluconeogenesis (05 Periods)

Glycolysis a universal pathway, fructose and galactose oxidation, anaerobic glycolysis,
fermentation, gluconeogenesis, reciprocal regulation of glycolysis and gluconeogenesis.

Unit 3: The citric acid cycle (05 Periods)

Pyruvate dehydrogenase complex, oxidation of acetyl CoA, amphibolic role, regulation and
glyoxylate pathway.

Unit 4: Oxidative phosphorylation (05 Periods)

The respiratory chain in mitochondria, proton gradient powering ATP synthesis, glycerol-3-
phosphate and malate-aspartate shuttle, regulation of oxidative phosphorylation.

Unit 5: Photosynthesis, Calvin cycle and pentose phosphate pathway (06 Periods)
The light reaction, chlorophyll, accessory pigments, reaction centres, two photo systems,
generation of proton gradient and NADPH, Calvin cycle, synthesis of glucose, starch, sucrose,
regulation, C4 pathway. Pentose phosphate pathway, importance and regulation.

Unit 6: Glycogen metabolism (02 Periods)

Glycogenolysis, phosphorylase regulation, role of epinephrine and glucagon for glycogenolysis,
glycogenesis; reciprocal regulation of glycogenesis and glycogenolysis.

Unit 7: Fatty acid synthesis and degradation (02 Periods)

TAG as energy source, β oxidation of fatty acids in mitochondria and peroxisomes, ketone bodies.
Biosynthesis of fatty acids - elongation and unsaturation of fatty acids. Regulation of fatty acid
oxidation and synthesis.

Unit 8: Amino acid catabolism and anabolism (03 Periods)

Protein degradation to amino acids, urea cycle, feeder pathways into TCA cycle. Nitrogen fixation,
synthesis of non-essential amino acids.
Unit 9: Nucleotide metabolism (03 Periods)
Biosynthesis - de novo and salvage pathways, regulation of nucleotide synthesis by feedback
inhibition, degradation and excretion.

Unit 10: Integration of metabolism (04 Periods)

Brief role of hormones - catecholamines, insulin, glucagon; metabolic shifts to provide fuel to
brain during fasting and starvation, role of cortisol in signaling stress - increase in gluconeogenesis
and muscle protein breakdown.

PRACTICALS

1. Alcohol fermentation by yeast.

2. H2S production, indole production and ammonia production by bacteria.
3. Urea estimation.
4. Uric acid estimation.
5. Nitrogen fixation by cyanobacteria.

SUGGESTED READINGS

1. Biochemistry (2012) 7th ed., Campbell, M.K. and Farrel, S.O. Brooks/Cole, Cengage Learning
(Boston), ISBN: 13:978-1-111-42564-7.

C10 IMMUNOLOGY
Paper Code (BBT 4003)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40

Course Objectives
● Understand the basics of Immunology and types of Immunity. Antigens as haptens, epitopes
and Factors influencing immunogenicity, and Antibodies as their Structure, types, production
and functions of immunoglobulins also about Clonal selection theory and Antigen Antibody
reactions as Precipitation, Haem-agglutination and ELISA.
● Understand of Major Histocompatibility complexes, structure of MHC, Hypersensitivity,
Autoimmunity and Immunodeficiency.
● Understand Passive and Active immunization, Types of Vaccines: Inactivated, Attenuated,
Recombinant and Sub Unit Vaccines, Peptide and DNA Vaccines.

Course Outcomes:
● Understanding of the overview of immune system including cells, organs and receptors.
● To learn structure and functions of different classes of immunoglobulins, the genetic basis
of antibody diversity and the importance of humoral, cell-mediated and innate immune
responses in combating pathogens.
● To understand mechanisms involved in different types of hypersensitivity, and the
importance of conventional vs recombinant vaccines.
● To get acquainted with the importance of antigen-antibody interaction in disease diagnosis.
● To understand the principles of tolerance, autoimmunity and the role of immunity in
protection against pathogens.

THEORY

UNIT I (10 Periods)

Immune Response - An overview, components of mammalian immune system, molecular structure
of Immuno-globulins or Antibodies, Humoral & Cellular immune responses, T lymphocytes &
immune response (cytotoxic T-cell, helper T-cell, suppressor T-cells), T-cell receptors, genome
rearrangements during B-lymphocyte differentiation, Antibody affinity maturation class
switching, assembly of T-cell receptor genes by somatic recombination.

UNIT II (10 Periods)

Regulation of immunoglobulin gene expression – clonal selection theory, allotypes&idiotypes,
allelic exclusion, immunologic memory, heavy chain gene transcription, genetic basis of antibody
diversity, hypotheses (germ line & somatic mutation), antibody diversity.

UNIT III (10 Periods)

Major Histocompatibility complexes – class I & class II MHC antigens, antigen processing.
Immunity to infection – immunity to different organisms, pathogen defense strategies, avoidance
of recognition. Autoimmune diseases, Immunodeficiency-AIDS.

UNIT IV (10 Periods)

Vaccines & Vaccination – adjuvants, cytokines, DNA vaccines, recombinant vaccines, bacterial
vaccines, viral vaccines, vaccines to other infectious agents, passive & active immunization.
Introduction to immunodiagnostics – RIA, ELISA.

PRACTICALS
1. Differential leucocytes count
2. Total leucocytes count
3. Total RBC count
4. Haemagglutination assay
5. Haemagglutination inhibition assay
6. Separation of serum from blood
7. Double immunodiffusion test using specific antibody and antigen.
8. ELISA.

SUGGESTED READING

1. Abbas AK, Lichtman AH, Pillai S. (2007). Cellular and Molecular Immunology. 6 th edition
Saunders Publication, Philadelphia.
2. Delves P, Martin S, Burton D, Roitt IM. (2006). Roitt’s Essential Immunology. 11th edition
Wiley-Blackwell Scientific Publication, Oxford.
3. Goldsby RA, Kindt TJ, Osborne BA. (2007). Kuby’s Immunology. 6th edition W.H. Freeman
and Company, New York.
4. Murphy K, Travers P, Walport M. (2008). Janeway’sImmunobiology. 7th edition Garland
Science Publishers, New York.
5. Peakman M, and Vergani D. (2009). Basic and Clinical Immunology. 2nd edition Churchill
Livingstone Publishers, Edinberg.
6. Richard C and Geiffrey S. (2009). Immunology. 6th edition. Wiley Blackwell Publication.

SEC2 MOLECULAR DIAGNOSTICS

Paper Code (BBT 4004)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40

Course Objective(s)
 Recall the basics of molecular diagnostics.
 Explain potential applications of molecular diagnostics.
 Compare existing and new concepts, methodologies and research results and apply them
in and academic or industrial research environment.

Course Outcome(s):
  Demonstrate various diagnostic lab techniques such as identification of causative agent of
disease using DNA or protein-based methods, microscopic analysis, and rapid
immunoassay
 Perform molecular techniques which include the isolation of DNA and genetic
manipulation, Rapid immunoassay, DNA fingerprinting analysis
 Appraise the significance of sensitive and accurate diagnosis in the detection of disease

THEORY

UNIT I (10 Periods)

Enzyme Immunoassays: Comparison of enzymes available for enzyme immunoassays,
conjugation of enzymes. Solid phases used in enzyme immunoassays. Homogeneous and
heterogeneous enzyme immunoassays. Enzyme immunoassays after immuno blotting. Enzyme
immuno histochemical techniques. Use of polyclonal or monoclonal antibodies in enzymes
immuno assays. Applications of enzyme immunoassays in diagnostic microbiology

UNIT II (10 Periods)

Molecular methods in clinical microbiology: Applications of PCR, RFLP, Nuclear hybridization
methods, Single nucleotide polymorphism and plasmid finger printing in clinical microbiology
Laboratory tests in chemotherapy: Susceptibility tests: Micro-dilution and macro-dilution broth
procedures. Susceptibility tests:Diffusion test procedures. Susceptibility tests: Tests for
bactericidal activity. Automated procedures for antimicrobial susceptibility tests.

UNIT III (10 Periods)

Automation in microbial diagnosis, rapid diagnostic approach including technical purification and
standardization of antigen and specific antibodies. Concepts and methods in idiotypes.
Antiidiotypes and molecular mimicry and receptors. Epitope design and applications.
Immunodiagnostic tests. Immuno florescence. Radioimmunoassay.

UNIT IV (10 Periods)

GLC, HPLC, Electron microscopy, flowcytometry and cell sorting. Transgenic animals.

PRACTICALS

(Wherever wet lab experiments are not possible the principles and concepts can be demonstrated
through any other material or medium including videos/virtual labs etc.)
1. Perform/demonstrate RFLP and its analysis
2. Kirby-Bauyer method (disc-diffusion method) to study antibiotic sensitivity of a bacterial
culture
3. A kit-basd detection of a microbial infection (Widal test)
4. Study of Electron micrographs (any four). 5. Perform any one immuno diagnostic test ( Typhoid,
Malaria, Dengue)

SUGGESTED READING

1. Practical Biochemistry, Principles and Techniques, Keith Wilson and John Walker
2. Bioinstrumentation, Webster
3. Advanced Instrumentation, Data Interpretation, and Control of Biotechnological Processes, J.F.
Van Impe,Kluwer Academic
4. Ananthanarayan R and Paniker CKJ. (2005). Textbook of Microbiology. 7th edition (edited by
Paniker CKJ). University Press Publication.
5. Brooks GF, Carroll KC, Butel JS and Morse SA. (2007). Jawetz, Melnick and Adelberg’s
Medical Microbiology. 24th edition. McGraw Hill Publication.
6. Goering R, Dockrell H, Zuckerman M and Wakelin D. (2007). Mims’ Medical Microbiology.
4th edition. Elsevier.
7. Joklik WK, Willett HP and Amos DB (1995). Zinsser Microbiology. 19th edition.
AppletonCentuary-Crofts publication.
8. Willey JM, Sherwood LM, and Woolverton CJ. (2008). Prescott, Harley and Klein’s
Microbiology. 7th edition. McGraw Hill Higher Education. 9. Microscopic Techniques in
Biotechnology, Michael Hoppert

SEMESTER-5
C11 MOLECULAR BIOLOGY
Paper Code (BBT 5001)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40

Course Objective(s)
 To teach the dynamic properties of chromatin and it’s folding.
 To teach topological properties of DNA, transposable elements and genetic code.
 To provide students with a deep insight and mechanism of the various cellular processes
such as DNA Replication, Transcription and Translation

Course Outcome(s):
  Study the discovery of DNA as genetic material, DNA replication, transcription, DNA
repair and translation.
 Analyse coding and non-coding regions of eukaryotic genome and their importance.
 Exposure with the importance of E. coli lac operon, PCR, expression vectors and their
importance in Biotechnology.
 To produce insulin using recombinant DNA technology.
 Acquaintance with the merits and demerits of transgenic crops.
 Exposure to the concepts of genomics, proteomics, metabolomics and their importance in
human health.

THEORY

UNIT I: DNA structure and replication (10 Periods)

DNA as genetic material, Structure of DNA, Types of DNA, Replication of DNA in prokaryotes
and eukaryotes: Semiconservative nature of DNA replication, Bi-directional replication, DNA
polymerases, The replication complex: Pre-primming proteins, primosome, replisome, Rolling
circle replication, Unique aspects of eukaryotic chromosome replication, Fidelity of replication.

UNIT II: DNA damage, repair and homologous recombination (10 Periods)
DNA damage and repair: causes and types of DNA damage, mechanism of DNA repair:
Photoreactivation, base excision repair, nucleotide excision repair, mismatch repair, translesion
synthesis, recombinational repair, nonhomologous end joining. Homologous recombination:
models and mechanism.

UNIT III: Transcription and RNA processing (10 Periods)

RNA structure and types of RNA, Transcription in prokaryotes: Prokaryotic RNA polymerase,
role of sigma factor, promoter, Initiation, elongation and termination of RNA chains Transcription
in eukaryotes: Eukaryotic RNA polymerases, transcription factors, promoters, enhancers,
mechanism of transcription initiation, promoter clearance and elongation RNA splicing and
processing: processing of pre-mRNA: 5’ cap formation, polyadenylation, splicing, rRNA and
tRNA splicing.

UNIT IV: Regulation of gene expression and translation (10 Periods)

Regulation of gene expression in prokaryotes: Operon concept (inducible and repressible system),
Genetic code and its characteristics, Prokaryotic and eukaryotic translation: ribosome structure and
assembly, Charging of tRNA, aminoacyl tRNA synthetases, Mechanism of initiation, elongation
and termination of polypeptides, Fidelity of translation, Inhibitors of translation ,Posttranslational
modifications of proteins.

PRACTICALS
1. Preparation of solutions for Molecular Biology experiments.
2. Isolation of chromosomal DNA from bacterial cells.
3. Isolation of Plasmid DNA by alkaline lysis method
4. Agarose gel electrophoresis of genomic DNA & plasmid DNA
5. Preparation of restriction enzyme digests of DNA samples
6. Demonstration of AMES test or reverse mutation for carcinogenicity

SUGGESTED READING

1. Karp, G. (2010). Cell and Molecular Biology: Concepts and Experiments. VI Edition. John
Wiley & Sons. Inc.
2. De Robertis, E.D.P. and De Robertis, E.M.F. (2006). Cell and Molecular Biology. VIII Edition.
Lippincott Williams and Wilkins, Philadelphia.
3. Becker, W.M., Kleinsmith, L.J., Hardin. J. and Bertoni, G. P. (2009). The World of the Cell.
VII Edition. Pearson Benjamin Cummings Publishing, San Francisco.
4. Watson, J. D., Baker T.A., Bell, S. P., Gann, A., Levine, M., and Losick, R., (2008) Molecular
Biology of the Gene (VI Edition.). Cold Spring Harbour Lab. Press, Pearson Pub.

C12 BIOSTATISTICS
Paper Code (BBT 5002)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40

Course Objective(s)
To provide training to students because there are more and more career fields that need
workers who are statistically literate, especially in our growing data-driven economies,
such as medicine and healthcare, data science, communications and public relations,
government and public policy, journalism, marketing, business, and finance.

Course Outcome(s):
 The students will understand the principles of collection of data in biological experiments,
proper statistical analysis of the data and its presentation.
 Students will understand the importance of sample size and various variables that affect
data.
 Students will know the importance of mean, standard error, standard deviation,
significance in presenting the data.
  Knowing statistical methods will help students in improving their analytical and
interpretation skill.
 Students will acquire hands-on practical training to plan biological experiments with
requisite sample size.
 After completion of experiments based on different sample sizes students will be able to
perform proper statistical analysis of the data using mean, median, mode, variance and
standard deviations.
 Students will be able to apply the principles of biological data management in real life
situations.
 Statistical training will improve computational, mathematical and computer skills of the
students by learning the use of ANOVA, AMOVA and student t-test.
 Students will be able to formulate a hypothesis, relevance to type of sample collected and
sample size.

THEORY

UNIT I (10 Periods)

Types of Data, Collection of data; Primary & Secondary data, Classification and Graphical
representation of Statistical data. Measures of central tendency and Dispersion. Measures of
Skewness and Kurtosis.

UNIT II (10 Periods)

Probability classical & axiomatic definition of probability, Theorems on total and compound
probability), Elementary ideas of Binomial, Poisson and Normal distributions.

UNIT III (10 Periods)

Methods of sampling, confidence level, critical region, testing of hypothesis and standard error,
large sample test and small sample test. Problems on test of significance, t-test, chi-square test for
goodness of fit and analysis of variance (ANOVA)

UNIT IV (10 Periods)

Correlation and Regression. Emphasis on examples from Biological Sciences.

PRACTICALS

1. Based on graphical Representation

2. Based on measures of Central Tendency & Dispersion
3. Based on Distributions Binomial Poisson Normal
4. Based on t, f, z and Chi-square
SUGGESTED READING

1. Le CT (2003) Introductory biostatistics. 1st edition, John Wiley, USA

2. Glaser AN (2001) High Yield Biostatistics. Lippincott Williams and Wilkins, USA
3. Edmondson A and Druce D (1996) Advanced Biology Statistics, Oxford University Press.
4. Danial W (2004) Biostatistics: A foundation for Analysis in Health Sciences, John Wiley and
Sons Inc.
DSE1 ANIMAL BIOTECHNOLOGY
Paper Code (BBT 5003)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40

Course Objective(s)
 Explain the methods of gene manipulations in animal cells and embryonic stem cells
 Develop breeding and conservation approaches in animals
 Appraise the legal and ethical issues related to animal maintenance
Course Outcome(s):
 Students will understand the basic concepts and terminology used in animal tissue culture.
 Students will understand and evaluate cell cultures constraints and possibilities as an in
vitro model.
 This course demonstrates knowledge of basic cell culture techniques
 Students will get the knowledge of how to establish a cell lines and its maintenance.
 This course demonstrates knowledge on design and how to use the cell culture facilities.
 Students will know the advantages and limitations of primary cell culture compared to
immortalized or transformed cell lines.

THEORY

UNIT I (10 Periods)

Gene transfer methods in Animals – Microinjection, Embryonic Stem cell, gene transfer,
Retrovirus & Gene transfer.

UNIT II (10 Periods)

Introduction to transgenesis. Transgenic Animals – Mice, Cow, Pig, Sheep, Goat, Bird, Insect.
Animal diseases need help of Biotechnology – Foot-and mouth disease, Coccidiosis,
Trypanosomiasis, Theileriosis.

UNIT III (10 Periods)

Animal propagation – Artificial insemination, Animal Clones. Conservation Biology – Embryo
transfer techniques. Introduction to Stem Cell Technology and its applications.
UNIT IV (10 Periods)
Genetic modification in Medicine - gene therapy, types of gene therapy, vectors in gene therapy,
molecular engineering, human genetic engineering, problems & ethics.

PRACTICALS
1. Sterilization techniques: Theory and Practical: Glass ware sterilization, Media sterilization,
Laboratory sterilization
2. Sources of contamination and decontamination measures.
3. Preparation of Hanks Balanced salt solution
4. Preparation of Minimal Essential Growth medium
5. Isolation of lymphocytes for culturing
6. DNA isolation from animal tissue
7. Quantification of isolated DNA.
8. Resolving DNA on Agarose Gel.

SUGGESTED READING

1. Brown, T.A. (1998). Molecular biology Labfax II: Gene analysis. II Edition. Academic Press,
California,USA.
2. Butler, M. (2004). Animal cell culture and technology: The basics. II Edition. Bios scientific
publishers.
3. Glick, B.R. and Pasternak, J.J. (2009). Molecular biotechnology- Principles and applications of
recombinant DNA. IV Edition. ASM press, Washington, USA.
4. Griffiths, A.J.F., J.H. Miller, Suzuki, D.T., Lewontin, R.C. and Gelbart, W.M. (2009). An
introduction to genetic analysis. IX Edition. Freeman & Co., N.Y., USA.
5. Watson, J.D., Myers, R.M., Caudy, A. and Witkowski, J.K. (2007). Recombinant DNAgenes
and genomes- A short course. III Edition. Freeman and Co., N.Y., USA.

DSE2 ENVIRONMENTAL BIOTECHNOLOGY

Paper Code (BBT 5004)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40

Course Objective(s)
 Recall knowledge on different environmental factors.
  To study concept of environmental pollution, bioremediation and its applications in
environmental clean up.
 To develops an attitude of concern for the environment and acquiring skills to help the
concerned individuals in identifying and solving environmental problems.

Course Outcome(s):
 They would understand and analyze environmental relationships with a better assessment
of the mechanisms of environmental components like atmosphere, hydrosphere and
lithosphere.
 Students will become skilled at basic theoretical concepts highlighting in the field of
ecology, and how these are applied to different ecological approaches.
 The studies of ecology, biogeography and ecosystem structure will provide the awareness
on ecological and historical foundations for understanding the distribution and abundance
of species and the changes in their distribution and abundance over time and climatic
impact.
 Student understood the concept of environmental pollution, types of pollutants and related
hazards. Acquire knowledge of bioremediation and its applications in environmental clean
up and various waste and disaster management methods and policies.
 Build awareness about environment conservation, environment protection acts. Studies on
current global environmental issues will make aware to students about their causes and
effect measure should be consider.

THEORY

UNIT I (10 Periods)

Conventional fuels and their environmental impact – Firewood, Plant, Animal, Water, Coal and
Gas. Modern fuels and their environmental impact – Methanogenic bacteria, Biogas, Microbial
hydrogen Production, Conversion of sugar to alcohol Gasohol

UNIT II (10 Periods)

Bioremediation of soil & water contaminated with oil spills, heavy metals and detergents.
Degradation of lignin and cellulose using microbes. Phyto-remediation. Degradation of pesticides
and other toxic chemicals by micro-organisms- degradation aromatic and chlorinates hydrocarbons
and petroleum products.

UNIT III (10 Periods)

Treatment of municipal waste and Industrial effluents. Bio-fertilizers Role of symbiotic and
asymbiotic nitrogen fixing bacteria in the enrichment of soil. Algal and fungal biofertilizers
(VAM)
UNIT IV (10 Periods)
Bioleaching, Enrichment of ores by microorganisms (Gold, Copper and Uranium). Environmental
significance of genetically modified microbes, plants and animals.

PRACTICALS

1. Calculation of Total Dissolved Solids (TDS) of water sample.

2. Calculation of BOD of water sample.
3. Calculation of COD of water sample.
4. Bacterial Examination of Water by MPN Method.

SUGGESTED READING

1. Environmental Science, S.C. Santra

2. Environmental Biotechnology, Pradipta Kumar Mohapatra
3. Environmental Biotechnology – Concepts and Applications, Hans-Joachim Jordening and Jesef
Winter
4. Waste Water Engineering, Metcalf and Eddy, Tata McGraw hill
5. Agricultural Biotechnology, S.S. Purohit
6. Environmental Microbiology: Methods and Protocols, Alicia L. Ragout De Spencer, John F.T.
Spencer
7. Introduction to Environmental Biotechnology, Milton Wainwright 8. Principles of
Environmental Engineering, Gilbert Masters 9. Wastewater Engineering – Metcalf &Edd

DSE3 MICROBIAL BIOTECHNOLOGY

Paper Code (BBT 5005)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40

Course Objective(s)
 Recall knowledge on medium formulation and strain improvement for enhanced
production of bioproducts.
 Develop fundamental knowledge to explore microbes for the production of industrially
relevant primary and secondary metabolites.
 Extend knowledge on the industrial method of fermentation processes for the production
of bioproducts.
Course Outcome(s):
 Understands importance of microorganisms in various milk and food processing.
  Understand the significance and activities of microorganisms in various food and factors
affecting on microbial growth in food leading to spoilage and understand the principles
underlying the preservation methods.
 Recognize and describe the characteristics of important food borne pathogens,
pathogenesis and prevention.
 Know the conceptual basis for understanding pathogenic microorganisms and mechanism
of their pathogenesis, treatment and prevention.
 Explains various aspects of wastewater treatment, also know various test to determine
potability of water.
 Acquire knowledge about application of microorganisms in bioleaching of metals,
agriculture, biosynthetic and biosynthetic material production.
 Understands norms and regulations of GMO and its responsible use.

THEORY

Unit 1: Microbial Biotechnology and its Applications (Lectures: 10)

Microbial biotechnology: Scope and its applications in human therapeutics, agriculture
(Biofertilizers, PGPR, Mycorrhizae), environmental, and food technology Use of prokaryotic and
eukaryotic microorganisms in biotechnological applications Genetically engineered microbes for
industrial application: Bacteria and yeast

Unit 2: Therapeutic and Industrial Biotechnology (Lectures: 10)

Recombinant microbial production processes in pharmaceutical industries - Streptokinase,
recombinant vaccines (Hepatitis B vaccine) Microbial polysaccharides and polyesters, Microbial
production of bio-pesticides, bioplastics Microbial biosensors

Unit 3: Applications of Microbes in Biotransformations (Lectures: 8)

Microbial based transformation of steroids and sterols Bio-catalytic processes and their industrial
applications: Production of high fructose syrup and production of cocoa butter substitute Unit 4
Microbial Products and their Recovery No. of Hours: 10 Microbial product purification: filtration,
ion exchange & affinity chromatography techniques Immobilization methods and their
application: Whole cell immobilization

Unit 5: Microbes for Bio-energy and Environment (Lectures: 08)

Bio-ethanol and bio-diesel production: commercial production from lignocellulosic waste and
algal biomass, Biogas production: Methane and hydrogen production using microbial culture.
Microorganisms in bioremediation: Degradation of xenobiotics, mineral recovery, removal of
heavy metals from aqueous effluents

Unit 6: RNAi (Lectures: 4)

RNAi and its applications in silencing genes, drug resistance, therapeutics and host pathogen
interactions

PRACTICALS

1. Study yeast cell immobilization in calcium alginate gels

2. Study enzyme immobilization by sodium alginate method
3. Pigment production from fungi (Trichoderma / Aspergillus / Penicillium)
4. Isolation of xylanase or lipase producing bacteria
5. Study of algal Single Cell Proteins

SUGGESTED READING

1. Ratledge, C and Kristiansen, B. (2001). Basic Biotechnology, 2nd Edition, Cambridge

University Press.
2. Demain, A. L and Davies, J. E. (1999). Manual of Industrial Microbiology and Biotechnology,
2nd Edition, ASM Press.
3. Swartz, J. R. (2001). Advances in Escherichia coli production of therapeutic proteins. Current
Opinion in Biotechnology, 12, 195–201.
4. Prescott, Harley and Klein’s Microbiology by Willey JM, Sherwood LM, Woolverton CJ
(2014), 9th edition, Mc Graw Hill Publishers.
5. Gupta PK (2009) Elements of Biotechnology 2nd edition, Rastogi Publications, 6. Glazer AN
and Nikaido H (2007) Microbial Biotechnology, 2nd edition, Cambridge University Press
7. Glick BR, Pasternak JJ, and Patten CL (2010) Molecular Biotechnology 4th edition, ASM Press,
8. Stanbury PF, Whitaker A, Hall SJ (1995) Principles of Fermentation Technology 2nd edition.,
Elsevier Science
9. Crueger W, Crueger A (1990) Biotechnology: A text Book of Industrial Microbiology 2nd
edition Sinauer associates, Inc.

SEMESTER 6
C13 RECOMBINANT DNA TECHNOLOGY
Paper Code (BBT 6001)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40
Course Objective(s)
 Recall different DNA modifying enzymes used in recombinant DNA technology
 Compare different vectors and their applications in recombinant DNA technology
 Illustrate different techniques used in genetic engineering
Course Outcome(s):
 Students will take practical training in the recent techniques of recombinant DNA technology
such as quantification of DNA, isolation of chromosomal DNA, isolation of plasmid DNA from
bacterial cells, restriction digestion of DNA and their separation using Agarose gel
electrophoresis, amplification of DNA fragment by PCR. With learning these techniques
students will gain expertise to work further in the area of recombinant DNA technology.

THEORY

UNIT I (10 Periods)

Molecular tools and applications- restriction enzymes, ligases, polymerases, alkaline phosphatase.
Gene Recombination and Gene transfer: Transformation, Episomes, Plasmids and other cloning
vectors (Bacteriophage-derived vectors, artificial chromosomes), Microinjection, Electroporation,
Ultrasonication, Principle and applications of Polymerase chain reaction (PCR), primer-design,
and RT- (Reverse transcription) PCR.

UNIT II (10 Periods)

Restriction and modification system, restriction mapping. Southern and Northern hybridization.
Preparation and comparison of Genomic and cDNA library, screening of recombinants, reverse
transcription, Genome mapping, DNA fingerprinting, Applications of Genetic Engineering
Genetic engineering in animals: Production and applications of transgenic mice, role of ES cells
in gene targeting in mice, Therapeutic products produced by genetic engineering-blood proteins,
human hormones, immune modulators and vaccines (one example each).

UNIT III (10 Periods)

Random and site-directed mutagenesis: Primer extension and PCR based methods of site directed
mutagenesis, Random mutagenesis, Gene shuffling, production of chimeric proteins, Protein
engineering concepts and examples (any two).

UNIT IV (10 Periods)

Genetic engineering in plants: Use of Agrobacterium tumefaciens and A. rhizogenes, Ti plasmids,
Strategies for gene transfer to plant cells, Direct DNA transfer to plants, Gene targeting in plants,
Use of plant viruses as episomal expression vectors.

PRACTICALS

1. Isolation of chromosomal DNA from plant cells

2. Isolation of chromosomal DNA from E.coli
3. Qualitative and quantitative analysis of DNA using spectrophotometer
4. Plasmid DNA isolation
5. Restriction digestion of DNA
6. Making competent cells
7. Transformation of competent cells.
8. Demonstration of PCR

SUGGESTED READING

1. Brown TA. (2006). Gene Cloning and DNA Analysis. 5th edition. Blackwell Publishing,
Oxford, U.K.
2. Clark DP and Pazdernik NJ. (2009). Biotechnology-Applying the Genetic Revolution. Elsevier
Academic Press, USA.
3. Glick, B.R., Pasternak, J.J. (2003). Molecular Biotechnology- Principles and Applications of
recombinant DNA. ASM Press, Washington
4. Primrose SB and Twyman RM. (2006). Principles of Gene Manipulation and Genomics, 7th
edition. Blackwell Publishing, Oxford, U.K.
5. Sambrook J, Fritsch EF and Maniatis T. (2001). Molecular Cloning-A Laboratory Manual. 3rd
edition. Cold Spring Harbor Laboratory Press.

C14 GENOMICS AND PROTEOMICS

Paper Code (BBT 6002)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40
Course Objective(s)
 Gaining a better understanding of the interactions between genes and the environment by
means of genomics is helping researchers find better ways to improve health and prevent
disease, Proteomics research permits the discovery of new protein markers for diagnostic
purposes and the study of novel molecular targets for drug discovery. The protein markers
identified have a broad range of potential applications. They may be used for clinical
diagnostic or prognostic purposes.
Course Outcome(s):
 Be able to describe the development of Omics technologies, with emphasis on genomics
and proteomics;
 Be able to synthesise information to discuss the key technological developments that
enabled modern genomic and proteomic studies;
  be able to describe advanced genomics and proteomics technologies and the ways in which
their data are stored;
 be able to use bioinformatics techniques to query examples of genomic and proteomic
databases to analyse cell biology;
 be able to describe the different types of genome variation and their relationship to human
diseases;
 be able to discuss how biological systems information relating to genes, proteins and
cellular structures can be used to model living cells, and even to create new synthetic cells.
 Genomics: an introduction to genomics, databases and sequence comparison techniques,
genes and the genome, principles and applications of DNA microarray technology,
transcriptional profiling, micro-array applications, SNP, QTL and genotyping, modern
genome sequencing, genome variation and phylogeny, biomes, and transcriptomics.
 Proteomics: early origins of proteomics, gel-based proteome profiling, the rise of different
mass spectrometry methods, modern high throughput mass spectrometry, protein data
bases

THEORY

UNIT I (10 Periods)

Introduction to Genomics, DNA sequencing methods – manual & automated: Maxam& Gilbert
and Sangers method. Pyrosequencing, Genome Sequencing: Shotgun & Hierarchical (clone
contig) methods, Computer tools for sequencing projects: Genome sequence assembly software.

UNIT II (10 Periods)

Managing and Distributing Genome Data: Web based servers and softwares for genome analysis:
ENSEMBL, VISTA, UCSC Genome Browser, NCBI genome. Selected Model Organisms'
Genomes and Databases.

UNIT III (10 Periods)

Introduction to protein structure, Chemical properties of proteins. Physical interactions that
determine the property of proteins. Short-range interactions, electrostatic forces, van der waal
interactions, hydrogen bonds, Hydrophobic interactions. Determination of sizes (Sedimentation
analysis, gel filteration, SDS-PAGE); Native PAGE, Determination of covalent structures –
Edman degradation.

UNIT IV (10 Periods)

Introduction to Proteomics, Analysis of proteomes. 2D-PAGE. Sample preparation, solubilization,
reduction, resolution. Reproducibility of 2D-PAGE. Mass spectrometry based methods for protein
identification. De novo sequencing using mass spectrometric data.
PRACTICALS

1. Use of SNP databases at NCBI and other sites

2. Use of OMIM database
3. Detection of Open Reading Frames using ORF Finder
4. Proteomics 2D PAGE database
5. Softwares for Protein localization.
6. Hydropathy plots
7. Native PAGE
8. SDS-PAGE

SUGGESTED READING

1. Genes IX by Benjamin Lewin, Johns and Bartlett Publisher, 2006.

2. Modern Biotechnology, 2nd Edition, S.B. Primrose, Blackwell Publishing, 1987.
3. Molecular Biotechnology: Principles and Applications of Recombinant DNA, 4th Edition, B.R.
Glick, J.J. Pasternak and C.L. Patten, 2010.
4. Russell, P. J. (2009). iGenetics- A Molecular Approach. III Edition. Benjamin Cummings.
5. Molecular Cloning: A Laboratory Manual (3rd Edition) Sambrook and Russell Vol. I to III,
1989.
6. Principles of Gene Manipulation 6th Edition, S.B.Primrose, R.M.Twyman and R.W. Old.
Blackwell Science, 2001.
7. Snustad, D.P., Simmons, M.J. (2009). Principles of Genetics. V Edition. John Wiley and Sons
Inc.
8. Klug, W.S., Cummings, M.R., Spencer, C.A. (2009). Concepts of Genetics. IX Edition.
Benjamin Cummings.
9. Glick, B.R., Pasternak, J.J. (2003). Molecular Biotechnology- Principles and Applications of
recombinant DNA. ASM Press, Washington. 6. Pevsner, J. (2009). Bioinformatics and Functional
Genomics. II Edition. John Wiley & Son

DSE4 PLANT BIOTECHNOLOGY

Paper Code (BBT 6003)
(Credits: Theory-4, Practicals-2)
 THEORY Lectures: 40
Course Objective(s)
 Explain the developmental processes operating in plants
 Demonstrate plant tissue culture methods
 Analyze biotechnological tools for engineering plants in agriculture and industry
Course Outcome(s):
 Learning outcomes for this course include detailed understanding of metabolic processes
specific for plants such as nitrate assimilation, photosynthesis, respiration, nitrogen
fixation and the role of different metabolic pathways in plant growth and development.
 Students will also gain insight to various stressful conditions of the environment that affect
plant growth and productivity as well as the defense mechanisms in plants due to which
plants survive under stresses.
THEORY

UNIT I (10 Periods)

Introduction, Cryo and organogenic differentiation, Types of culture: Seed, Embryo, Callus,
Organs, Cell and Protoplast culture. Micropopagation Axillary bud proliferation, Meristem and
shoot tip culture, cud culture, organogenesis, embryogenesis, advantages and disadvantages of
micropropagation.

UNIT- II (10 Periods)

In vitro haploid production Androgenic methods: Anther culture, Microspore culture
andogenesisSgnificance and use of haploids, Ploidy level and chromosome doubling,
diplodization, Gynogenic haploids, factors effecting gynogenesis, chromosome elimination
techniques for production of haploids in cereals.

UNIT - III (10 Periods)

Protoplast Isolation and fusion Methods of protoplast isolation, Protoplast development, Somatic
hybridization, identifiation and selection of hybrid cells, Cybrids, Potential of somatic
hybridization limitations. Somaclonal variation Nomenclautre, methods, applications basis and
disadvantages.

UNIT – IV (10 Periods)

Plant Growth Promoting bacteria. Nitrogen fixation, Nitrogenase, Hydrogenase, Nodulation,
Biocontrol of pathogens, Growth promotion by free-living bacteria.

PRACTICALS

1. Preparation of simple growth nutrient (knop’s medium), full strength, half strength, solid and
liquid.
2. Preparation of complex nutrient medium (Murashige& Skoog’s medium)
3. To selection, Prune, sterilize and prepare an explant for culture.
4. Significance of growth hormones in culture medium.
5. To demonstrate various steps of Micropropagation.

SUGGESTED READING
1. Bhojwani, S.S. and Razdan 2004 Plant Tissue Culture and Practice.
2. Brown, T. A. Gene cloning and DNA analysis: An Introduction. Blackwell Publication.
3. Gardner, E.J. Simmonns, M.J. Snustad, D.P. 2008 8th edition Principles of Genetics. Wiley
India.
4. Raven, P.H., Johnson, GB.,Losos, J.B. and Singer, S.R. 2005 Biology. Tata MC Graw Hill.
5. Reinert, J. and Bajaj, Y.P.S. 1997 Applied and Fundamental Aspects of Plant Cell, Tissue and
Organ Culture. Narosa Publishing House.
6. Russell, P.J. 2009 Genetics – A Molecular Approach. 3rdedition. Benjamin Co.
7. Sambrook& Russel. Molecular Cloning: A laboratory manual. (3rd edition)
8. Slater, A., Scott, N.W. & Fowler, M.R. 2008 Plant Biotechnology: The Genetic Manipulation
of Plants, Oxford University Press.

DSE5 BIOINFORMATICS
Paper Code (BBT 6004)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40
Course Objective(s)
 Recall the basic practical techniques of bioinformatics.
 Extend the knowledge of bioinformatics and biological databases to solving real
research problems.
 Formulate the use of a wide variety of tools, servers, biological databases and apply them
in appropriate fields.
Course Outcome(s):
 By studying this course, the students completing B.Sc. Biotechnology will have an
understanding of the tools of bioinformatics and computational biology and will be in a
position to access biological data bases and softwares which will be helpful in
understanding sequence alignments and predicting the structures of biomolecules such
as proteins. Students will be exposed to available bioinformatics tools and databases.
 They will be in a position to comprehend the fundamental aspects of in-silico protein
structure prediction.
 They will understand application of theoretical approaches to biological systems.
Students will get trained in the application of programs used for database searching,
protein and DNA sequence analysis, and prediction of protein structures.
THEORY

UNIT I (10 Periods)

History of Bioinformatics. The notion of Homology. Sequence Information Sources, EMBL,
GENBANK, Entrez, Unigene, Understanding the structure of each source and using it on the web.
UNIT II (10 Periods)
Protein Information Sources, PDB, SWISSPROT, TREMBL, Understanding the structure of each
source and using it on the web. Introduction of Data Generating Techniques and Bioinformatics
problem posed by them- Restriction Digestion, Chromatograms, Blots, PCR, Microarrays, Mass
Spectrometry.

UNIT III (10 Periods)

Sequence and Phylogeny analysis, Detecting Open Reading Frames, Outline of sequence
Assembly, Mutation/Substitution Matrices, Pairwise Alignments, Introduction to BLAST, using it
on the web, Interpreting results, Multiple Sequence Alignment, Phylogenetic Analysis.

UNIT IV (10 Periods)

Searching Databases: SRS, Entrez, Sequence Similarity Searches-BLAST, FASTA, Data
Submission. Genome Annotation: Pattern and repeat finding, Gene identification tools.

PRACTICALS

1. Sequence information resource

2. Understanding and use of various web resources: EMBL, Genbank, Entrez, Unigene, Protein
information resource (PIR)
3. Understanding and using: PDB, Swissprot, TREMBL
4. Using various BLAST and interpretation of results.
5. Retrieval of information from nucleotide databases.
6. Sequence alignment using BLAST. 7. Multiple sequence alignment using Clustal W.

SUGGESTED READING

1. Ghosh Z. and Bibekanand M. (2008) Bioinformatics: Principles and Applications. Oxford

University Press.
2. Pevsner J. (2009) Bioinformatics and Functional Genomics. II Edition. Wiley-Blackwell.
3. Campbell A. M., Heyer L. J. (2006) Discovering Genomics, Proteomics and Bioinformatics. II
Edition. Benjamin Cummings.
 DSE6 BIOPROCESS TECHNOLOGY
Paper Code (BBT 6005)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40
Course Objective(s)

 To teach the concept and application bioprocess technology

 To develop understanding bioformulation and fermentation techniques.
 To provide knowledge recycling and quality control.

Course Outcome(s):
 This paper presents the basics of fermentation technology, media components as applied
to lab scale, pilot scale and industrial scale upstream and downstream processing.
 This paper is introduced to acquire requisite skills for the design and development of
bioreactors, production optimization, and preparation of sterile base materials for
downstream processing.
 On successful completion of the course the students should have understood the basics
of fermentation technology and learnt the concept of screening, optimization and
maintenance of cultures.

THEORY
UNIT I (10 Periods)
Introduction to bioprocess technology. Range of bioprocess technology and its chronological
development. Basic principle components of fermentation technology. Types of microbial culture
and its growth kinetics– Batch, Fed batch and Continuous culture.

UNIT II (10 Periods)

Design of bioprocess vessels- Significance of Impeller, Baffles, Sparger; Types of
culture/production vessels- Airlift; Cyclone Column; Packed Tower and their application in
production processes. Principles of upstream processing – Media preparation, Inocula
development and sterilization.

UNIT III (10 Periods)

Introduction to oxygen requirement in bioprocess; mass transfer coefficient; factors affecting KLa.
Bioprocess measurement and control system with special reference to computer aided process
control.

UNIT IV (10 Periods)

Introduction to downstream processing, product recovery and purification. Effluent treatment.
Microbial production of ethanol, amylase, lactic acid and Single Cell Proteins.

PRACTICALS

1. Bacterial growth curve.

2. Calculation of thermal death point (TDP) of a microbial sample.
3. Production and analysis of ethanol.
4. Production and analysis of amylase.
5. Production and analysis of lactic acid.
6. Isolation of industrially important microorganism from natural resource.
SUGGESTED READING

1. Casida LE. (1991). Industrial Microbiology. 1st edition. Wiley Eastern Limited.
2. Crueger W and Crueger A. (2000). Biotechnology: A textbook of Industrial Microbiology. 2nd
edition. Panima Publishing Co. New Delhi.
3. Patel AH. (1996). Industrial Microbiology. 1st edition, Macmillan India Limited.
4. Stanbury PF, Whitaker A and Hall SJ. (2006). Principles of Fermentation Technology. 2nd
edition, Elsevier Science Ltd.

SEMESTER 7
C15 APPLIED BIOTECHNOLOGY
Paper Code (BBT 7001 [A])
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 20

Course Objective(s)

 To study microbial growth and its maintenance.

 To develop understanding different bioreactors.
 To provide knowledge biochemistry of different industrial chemicals

Course Outcome(s):
 Learn basics of fermentation technology, bioreactors, production optimization, and
downstream processing.
  On successful completion of the course the students should have understood the basics
of fermentation technology and learnt the concept of different metabolite production by
microbes in industrial setup.

THEORY

Unit-I Microbial Cell Growth and Death Kinetics: (10 Lectures)

Screening and Improvement of industrially important microorganisms, Microbial Growth and
Death Kinetics, Media for Industrial Fermentation, Air and Media Sterilization.

Unit-II Operation and Control of Bioreactors: ( 10 Lectures)

Types of Fermentation Processes: Analysis of batch, fed-batch and continuous bioreactors,
stability of microbial bioreactors, analysis of mixed populations, specialized bioreactors-pulsed,
fluidized, photo bioreactors, etc. Measurement and Control of bioprocess parameters. Downstream
processing, Whole cell immobilization and their industrial applications.

Unit-III Fermentation Technology: (10 Lectures)

Industrial production of chemicals: Ethanol, Acids (citric, acetic and gluconic acid), Solvents
(glycerol, acetone, butanol), Antibiotics (penicillin, streptomycin, tetracyclin), Semi-synthetic
antibiotics, Amino acids (lysine, glutamic acid), Single cell protein.

Unit-IV Applications of Bioprocess Engineering: (10 Lectures)

Agitation and aeration: requirement in industrial processes, concept of volumetric oxygen transfer
coefficient and its determination (Kla), Factors affecting Kla values; Uses of microbes in mineral
beneficiation and oil recovery. Introduction to food technology; Elementary idea of canning and
packaging, Sterilization and pasteurization of food products.

PRACTICALS

1. To plot Microbial growth curve for shake flask culturing using turbidity method.
2. Prepare a standard curve of reducing sugar by 3,5-Dinitrosalicylic acid method
3. To produce invertase enzyme and find its activity from Baker’s Yeast
4. Preparation of standard curve of Ethanol.
5. Quantitative estimation of ethanol produced during Yeast fermentation
6. Production of Penicillin and assaying its activity.
7. To get familiarized with the lab scale fermenter (bench top fermenter)
8. To determine dissolved oxygen concentration in tap and aerated water.
9. To determine the volumetric transfer coefficient (K la)
10. Estimation of BOD in a given waste water sample.
11. Centrifugation studies during settling of yeast cells.
12. Yeast cell disruption by mechanical methods.

SUGGESTED BOOKS

1. Bioprocess Engineering, Shular M &Kargi F, Prentice Hall

2. Biochemical Engineering Fundamentals, Bailey JE &Ollis DF
3. Bioprocess Engineering Principles, Doran, PM, Academic Press, California

CC 15 APPLIED BIOCHEMISTRY
Paper Code (BBT 7001 [B])
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 40

Course Objective(s)
 To develop understading for the application of applied biochemistry.
 To train students in emerging field of applied biochemistry.

Course Outcome(s):
 Students will learn basics and application of radiochemistry, immunochemistry, and
immunoassay.

THEORY

Unit I- (10 Lectures)

Experimental systems in biochemical studies: in vivo and in vitro models. Cell cultures.
Microbial cultures. Cel count techniques. Basic principles of FACS analysis and applications of
flow cytofluorimetry. UV-VIS spectroscopy: first elements, applications and instrumentation.
Spectrofluorimetry: first elements, applications and instrumentation. Sedimentation and
centrifugation: physical laws, preparative and analytical applications. Preparation and
fractionation of cell and tissue homogenates. Assay methods for protein measuring.

Unit II- (10 Lectures)

Aminoacid composition and primary structure of proteins: analysis methods. Protein
fragmentation and peptide production: first elements of mass spectrometry in the proteome
analysis. Electrophoresis: first elements and physical laws. Electrophoresis in liquid and semisolid
media: agarose gels and polyacrilamide gels. SDS-PAGE and molecular mass determination of
proteins. Native PAGE. Gradiente gels. Isoelectrofocusing and protein pI. Detection, evaluation
and recovery of protein from gel. Western and South-Western blotting. Agarose and
polyacrilamide gel electrophoresis of nucleic acids. Pulsed field gel electrophoresis (PFGE) DNA
sequencing: Sanger and Maxam-Gilbert methods. Chromatography: first elements and theoretical
principles. TLC chromatography. Column low pressure chromatography. High performance liquid
chromatography (HPLC, FPLC). Adsorption chromatography. Partition chromatography. Normal
phase and reversed phase (RPC) chromatography. Ion pair RPC. Hydrophobic interaction
chromatography (HIC). Ion exchange chromatography (IEX). Gel filtration chromatography.
Affinity chromatography. Working out of protein purification protocols.
Unit III- (10 Lectures)
Radiochemistry: nuclear reactions, radioisotopes, radioactive decay. Matter-radiation
interactions: safety elements in radioprotection. Detection and measuring of radioactivity:
autoradiography, gas ionization methods, scintillation methods. Practical aspects in radioactivity
counting and data analysis. Uses of radioisotopic tracers in biochemical, biomolecular and
biomedical analyses.

Unit IV- (05 Lectures)

Immunochemistry: monoclonal (mAb) and polyclonal (pAb) antibodies production. In vivo and
in vitro radiolabeling of proteins and nucleic acids. Purification and fragmentation of
immunoglobulins. Immunoprecipitation. Antibody labeling.

Unit V- (05 Lectures)

Immunoassays: RIA, IRMA, ELISA. Nucleic acids analysis:Northern and Southern analyses,
restriction enzymes, modification enzymes and their applications. Polymerase chain reaction
(PCR). Sensitivity and general applications of PCR. Cloning vectors and molecular cloning.
Production of recombinant proteins.

PRACTICALS
*(Wherever wet lab experiments are not possible the principles and concepts can be demonstrated
through any other material or medium including videos/virtual labs etc.)
1. Differential leucocytes count
2. Total leucocytes count
3. Blotting
4. Haemagglutination assay
5. Haemagglutination inhibition assay
6. Separation of serum from blood
7. Double immunodiffusion test using specific antibody and antigen.
8. ELISA.

SUGGESTED READING
1.Wilson, Keith & Walker, John -Principles and Techniques of Biochemistry and Molecular
Biology - 6th ed. Cambridge University Press, 2005 (Italian edition: WILSON Keith &
WALKER, John - Biochimica e BiologiaMolecolare: Principi e Tecniche - Raffaello Cortina
ed. (ISBN 88-6030-066-5))
C 15 APPLIED MIICROBIOLOGY
Paper Code (BBT 7001 [C])
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 50

Course Objective(s)
 Recall necessary information related to all microorganisms and their application in various
sectors Elaborate on laboratory safety and specialized microbiological laboratory skills

Course Outcome(s):
 Learn the structure, diversity, classification, and application of microorganisms.
 Relate the role of microbes in the fields of food, agriculture, medicine and biotechnology.

THEORY

Unit 1- (10Lectures)
Agriculture Microbiology: Role of microorganisms in soil fertility. Interactions between
microbes and plants - rhizosphere, phyllosphere, mycorrhizae. Biofertilizer for sustainable
agriculture Rhizobium, Azospirillium, Azotobacter, Azolla, BGA - mass production methods -
applications methods of biofertilizers - significance of biofertilizers. Microorganisms used as
biocontrol agents against microbial plant pathogens (Trichoderma sp. and Pseudomonas
fluorescens), Bacterial, fungal and viral bio-insecticides and bio-herbicides

Unit 2- (10Lectures)
Food Microbiology: Factors influencing microbial growth in foods - extrinsic and intrinsic.
Principles of food preservation - preservation methods - irradations - drying, heat processing,
chilling and freezing, and chemical preservatives. Microbial production of Dairy Cheese, Yogurt,
Butter, Buttermilk. Prebiotics, probiotics-health benefits and types of microorganisms used.
Cultural and rapid detection of food borne pathogens.

Unit 3- (10 Lectures)

Industrial Microbiology: Introduction to fermentation. Industrially important organisms –
Isolation, preservation and strain improvement. Types of fermentation processes - Solid-state and
liquid-state (stationary and submerged) fermentations; batch, fed-batch and continuous
fermentations. Components of a typical bio-reactor, types of bioreactors, downstream processing.
Microbial productions: Wine and ethyl alcohol, citric acid, glutamic acid, penicillin Recombinant
products: vaccine.

Unit 4- (10 Lectures)

Medical and Pharmaceutical Microbiology: History and Importance of Medical Microbiology,
Significance of Microbiome: Normal microflora, True pathogen Opportunistic Pathogens.
Bacterial, Viral, Fungal and Protozoan Diseases of various human body systems, Disease
associated clinical samples for diagnosis. Antimicrobial Chemotherapy: General Characteristics
and model of action of different classes of Antibiotics, Antiviral, Antifungal and Anti protozoal
Agents.

Unit 5- (05 Lectures)

Microbiology of waste management: Determination of water quality: BOD, COD,
bacteriological examination of water (Presumptive, confirmed, completed test, SPC, MPN,
Membrane filter technique). Waste treatment: Types of wastes, Effluent treatment - Primary,
secondary (aerobic and anaerobic) and tertiary Methods, Disinfection, Biogas production. Solid
waste management - Composting, vermicomposting, and Mushroom cultivation.

Unit 6- (05 Lectures)

Microbial Applications and ethical issues: Bioremediation strategies (environment
modification, microbial application), Enhanced metal recovery; Transgenic plants (BT crops,
golden rice), transgenic animals, advantages, social and environmental aspects. Advances and
trends, ethical issues, quality control, legislation, FDA & FPO, (India), safety and security at
workplace

PRACTICALS

*(Wherever wet lab experiments are not possible the principles and concepts can be
demonstrated through any other material or medium including videos/virtual labs etc.)
1. Screening of antibiotics producing microbes from soil.
2. Isolation of rhizobia from root nodules.
3. Ascertaining microbial quality of milk by MBRT
4. General techniques for bacterial isolation – MPN test, Total coliform
5. Passive monitoring of microbial air quality
6. Determination of resistance/sensitivity of bacteria using disc diffusion method
7. Detection of biological oxygen demand of given water sample.
SUGGESTED READINGS
1. Ananthanarayan R. and Paniker C.K.J. (2009) Textbook of Microbiology. 8th edition,
University Press Publication.
2. Atlas RM and Bartha R. (2000). Microbial Ecology: Fundamentals & Applications. 4th
edition. Benjamin/Cummings Science Publishing, USA
3. Bare Act, 2007.Indian Patent Act 1970 Acts & Rules, Universal Law Publishing Co. Pvt. Ltd.,
New Delhi.
4. Coyne MS. (2001). Soil Microbiology: An Exploratory Approach. Delmar Thomson Learning.
5. Crueger W, Crueger A (1990) Biotechnology: A text Book of Industrial Microbiology 2nd
edition Sinauer associates, Inc.
6.Demain, A. L and Davies, J. E. (1999). Manual of Industrial Microbiology and Biotechnology,
2nd Edition, ASM Press.
7.Goel D &Prashar S (2013).IPR, Biosafety and Bioethics. Pearson.
8.Goering R., Dockrell H., Zuckerman M. and Wakelin D. (2007) Mims’ Medical Microbiology.
4th edition. Elsevier.

C15 APPLIED FOOD TECHNOLOGY

Paper Code (BBT 7001 [D])
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 20

Course Objective(s)
 To impart knowledge in areas of food science and technology.
 To understand the food composition along with physicochemical properties.
 To learn the basis of food processing and packaging

Course Outcome(s):
 Understand the process of food preservation and packaging requirements of food
categories.
 Understand the material handling in food industry, thermal processing.

THEORY

Unit I- (10 Lectures)

Low temperature storage: Freezing and chilling, requirements of refrigerated storage - controlled
low temperature, air circulation and humidity, changes in food during refrigerated storage,
progressive freezing, changes during freezing –concentration effect and ice crystal damage, freezer
burn and types of freezers.

Unit II- (10 Lectures)

Thermal processing: Introduction, classification of thermal Processes, Principles of thermal
processing, Thermal resistance of microorganisms, Thermal Death Time, Thermal process
Calculations, Drying curve , effect of food properties on dehydration , change in food during drying
,drying methods and equipments used for drying and dehydration.

Unit III- (10 Lectures)

Food irradiation and microwave heating: Ionizing radiation and sources, unit of radiations,
direct and indirect radiation effects, safety and wholesomeness of irradiated food. Microwave
heating and application, Infra-red and ultrasonic radiation for processing and their mechanism.

Unit IV-(05 Lectures)

Advanced technologies: Extrusion: Theory and applications, extrusion cookers and cold
extrusion, single and twin screw extruders, design considerations, Supercritical gas extraction, Non
thermal Processing: High pressure processing, Pulsed electric processing and Ohmic heating.

Unit V- (06 Lectures)

Packaging of foods: Packaging: Properties of packaging material, factors determining the
packaging requirements of various foods, brief introduction of various packaging materials used
in food sector, Advanced packaging techniques- MAP, CAP, Smart packaging.

PRACTICALS

1. Estimation of reducing sugar by Fehlings procedure.

2. Determination of acidity of water
3. Demonstration of the Soxhlet method for determination of fat content
4. Estimation of gluten content of flour.
5. Demonstration of the Kjeldahl’s method for estimation of protein content
6. Determination of pH of different foods using pH meter.

SUGGESTED READINGS

1. WimJongen- Fruit and vegetable processing improving quality, WoodheadPublishing

Limited.
2. A. Chakraverty- Post harvest Technology of cereals, pulses and oilseeds, Oxford & IBH
Publishers
3. SukumarDey- Outlines of Dairy Technology, Oxford Publishers.
4. William J. Stadelman, V. M. Olson, G. A. Shemwell, S. Pasch- Egg and Poultry-Meat
Processing, VCH Publishers.

C16 RESEARCH METHODOLOGY

Paper Code (BBT 7002)
(Credits: Theory-4, Practicals-2)
THEORY Lectures: 20
Course Objective(s)
 Understand some basic concepts of research and its methodologies.
 To identify appropriate research topics and select and define appropriate research problem
and parameters.

Course Outcome(s):
 Students will learn how to prepare a project proposal (to undertake a project).
 Organize and conduct research (advanced project) in a more appropriate manner
 Will write a research report and thesis • write a research proposal (grants)

THEORY

Unit 1 Introduction to Research Methodology (Lectures: 4)

Objectives and motivation in research.

Unit 2 Defining the Research Problem (Lectures: 4)

Selecting and defining a research problem, Reviewing and conducting literature search,
Developing a research plan.

Unit 3 Designing of Experiment (Lectures: 4)

Different experimental designs – single and multifactorial design, Making measurements and
sources of error in measurements, Methods of data collection and record keeping.
Unit 4 Data Processing and Statistical Analysis (Lectures: 8)
Processing operations, tabulation, and graphical representation, Statistics in research: Concepts of
sample and population, Measure of central tendency, dispersion, asymmetry (skewness, kurtosis),
Normal distribution (p-value), Statistical tests and hypothesis (Standard error, t-test, chi-square
test), and regression analysis, Report writing, Writing a research paper - abstract, introduction,
methodology, results and discussion.
Based on the teaching above, each student will undertake the following exercises.
1. A teacher (adviser) who would guide the student will discuss with student and identify a topic
of mutual interest.
2. The student will collect the literature, collate the information and write the same in the form of
a term paper with proper incorporation of references using appropriate software such as EndNote.
3. The student will identify scope of research on the topic and will frame objectives to be addressed
in the project through a work plan.
4. The student will write standard operating protocols (SOPs) and identify requirement for
equipment and reagents.
5. Each student will be asked to make presentation about the project including literature available,
objective sought and work plan including methodologies as described above.

SUGGESTED READINGS

1. Research in Education (1992) 6th ed., Best, J.W. and Kahn, J.V., Prentice Hall of India Pvt. Ltd.
2. At the Bench: A Laboratory Navigator (2005) Barker, K., Cold Spring Harbor Laboratory Press
(New York), ISBN: 978-087969708-2. 51
3. Research Methodology - Methods and Techniques (2004) 2nd ed., Kothari C.R., New Age
International Publishers.
4. Research Methodology: A Step by Step Guide for Beginners (2005) 2nd ed., Kumar R., Pearson
Education.
5. Biostatistics: A Foundation for Analysis in the Health Sciences (2009) 9th ed., Daniel W.W.,
John Wiley and Sons Inc.
6. Statistics at the Bench: A Step-by-Step Handbook for Biologists (2010) Bremer, M. and Doerge,
R.W., Cold Spring Harbor Laboratory Press (New York), ISBN: 978-0-879698- 57-7.

C17 PROJECTS
Paper Code (BBT 8001)
(Credits: Practicals-4)

Course Objective(s)

Course Outcome(s):