B.SC Bio Chemistry 2020 21

ADIKAVI NANNAYA UNIVERSITY :: RAJAHMAHENDRAVARAM
B.Sc Bio-Chemistry Syllabus (w.e.f: 2020-21 A.Y)
UG PROGRAM (4 Years Honors)

CBCS - 2020-21
SUBJECT
BIOCHEMISTRY
Members of BOS (Contact details)

Dr. D. Kalyani Department of Zoology
Assistant Professor Adikavi Nannaya University 9849419160
Rajahmahendravaram
Dr.K.Kamalakara Rao Department of iochemistry

9985062021
Assistant Professor Adikavi Nannaya University
Rajahmahendravaram
Syllabus and Model Question Papers
B Sc Bio-Chemistry Page 1 of 35
TABLE OF CONTENTS
S. No Particulars Page No.

1 Resolutions of the BOS 3
2 Details of Course titles & Credits 4
a. Proposed combination subjects: 4
b. Student eligibility for joining in the course: 4
c. Faculty eligibility for teaching the course 4
d. List of Proposed Skill enhancement courses with syllabus, if any 4
e. Any newly proposed Skill development/Life skill courses with 5
draft syllabus and required resources
f. Required instruments/software/ computers for the course 5
g. List of Suitable levels of positions eligible in the Govt/Pvt 6
organizations
h. List of Govt. organizations / Pvt companies for employment 7
opportunities or internships or projects
i. Any specific instructions to the teacher /Course setters/Exam- 8
Chief Superintendent
3 Program objectives, outcomes, co-curricular and assessment methods 8
4 Details of course-wise syllabus for Theory and Lab 8
5 Model Question Courses for Theory and Lab 26
6 Details of Syllabus on Skill Enhancement courses and Model 36
Question Courses for Theory and Lab
Note: BOS is to provide final soft copy in PDF and word formats and four copies of hard copies in
bounded form to the office of Dean Academic affairs.
1. Resolutions of the Board of Studies
Meeting held on: 22/01/2021………….Time: 10 AM – 4 PM

At: ANUR Convention Centre, Adikavi Nannaya University
Rajahmahendravaram
Agenda:
As per the directions and guidelines/modalities issued by the APSCHE for revising the curriculum
framework and updating the syllabus as out-come based B. Sc Bio-Chemistry programme to be effect
from 2020-21 academic year under CBCS for implementing in all affiliated colleges of AKNU
Members present:
Dr. D. Kalyani, Assistant Professor, Department of Zoology, Adikavi Nannaya University,

Rajahmahendravaram.
Dr. K. Kamalakara Rao, Assistant Professor, Department of Biochemistry, Adikavi Nannaya
University, Rajahmahendravaram.
Resolutions:
1. It was resolved to adopt revised common programme structure as per the guidelines issued by
APSCHE.
2. Resolved to adopt regulations and scheme of examinations and marks/grading system of the
university UG programs.
3. Resolved to prepare model question Courses in the given prescribed format.
4. Resolved to prepare a list of equipments/software required for each lab/practicals.
5. Resolved to give the eligibility criteria of students for joining the course.
6. Resolved to give the eligibility criteria of faculty for teaching the course.
7. Resolved to prepare a list of Course setters/Course evaluators/project evaluators in the given

prescribed format.
2. DETAILS OF COURSE TITLES & CREDITS
Hrs/Week Credits Max. Marks Max. Marks

Course
Type Count/Internal/ Sem- End
Sem Course No Course Name
(T/P/L) Science: 4+2 Science: 4+2
Mid Assessment Exam
Biomolecules T 4 4 25 75
BCH-1
I Biomolecules Lab L 2 1 - 50
Analytical
T 4 4 25 75
Techniques
BCH-II
II Analytical
L 2 1 - 50
Techniques Lab
Enzymology,
Bioenergetics and
T 4 4 25 75
Intermediary
Metabolism
BCH-III
III Enzymology,
Bioenergetics and
L 2 1 - 50
Intermediary
Metabolism Lab
Physiology,
Nutritional and T 4 4 25 75
Clinical Biochemistry
BCH-IV Physiology
Nutritional and
L 2 1 - 50
Clinical Biochemistry
Lab
Microbiology,
IV
Immunology and T 4 4 25 75
Molecular Biology
BCH-V Microbiology,
Immunology and
2 1 - 50
Molecular Biology L
Lab
Note: *Course type code: T: Theory, L: Lab, P: Problem solving
a. Proposed combination subjects: Biochemistry, Biotechnology, Microbiology

Biochemistry, Biotechnology, Chemistry
Biochemistry, Biotechnology, Zoology
b. Student eligibility for joining in the course: + 2/ Intermediate with Bi.P.C. and M.Bi.P.C.
c. Faculty eligibility for teaching the course: M.Sc. (Minimum Qualification)
M.Phil. and Ph.D. are desirable
d. List of Proposed Skill enhancement courses with syllabus, if any

Industrial Biochemistry
Environmental Biochemistry
Pharmaceutical Biochemistry
e. Any newly proposed Skill development/Life skill courses with draft syllabus and required
resources
f. Required instruments/software/ computers for the course (Lab/Practical course-wise required
i.e., for a batch of 15 students)
Sem. Lab/Practical Names of Instruments/Software/ Brand Name Qty

No. Name computers required with Required
specifications
1 Biomolecules Weighing balance digital and Non 2
digital Mettler Toledo 2
PH Meter Coleparmer 2
Water bath Kemi 2
Vortex mixture Coleparmer 2
Magnetic stirrer IKA 2
Hot plate Remi 2
Hot air oven Remi 2
Autoclave Labline 2
Distillation unit Accumax India 2
Refrigerator 2
Ice flakes machine Labman 2
2 Analytical Homogenizer Remi 2
Techniques Centrifuge Thermo scientific 1
( Refrigerated and Non
refrigerated)
Gel documentation system Thermo Fisher 1
Chromatography chamber 2
Electrophoresis unit (Horizontal Major science 2
and vertical)
Colorimeter Equiptronic 2
UV Spectrophotometer Shimadzu 1
3 Enzymology, Soxhlet extractor Borosilicate 1
Bioenergetics Rotary evaporator Heidolph 1
and Dessicator Borosil 1
Intermediary Mortar and pestle Thermo scientific 2
metabolism Glass and micro pipettes Borosil Thermo scientific 15
Millipore unit Merck 1
4 Physiology, Simple microscope Olympus 2
Nutritional Compound microscope Leica 2
and Clinical
biochemistry
5 Microbiology BOD Incubator Kemi 1
Immunology COD Incubator Thermo Fisher 1
and Molecular Orbital shakers Coleparmer 1
biology Laminar air flow Bionics Scientific 1
Fume hood Coleparmer 1
ELISA reader Biorad 1
Neubarrs chamber Merck 2
g. List of Suitable levels of positions eligible in the Govt/Pvt organizations
Suitable levels of positions for these graduates either in industry/govt organization like.,
technical assistants/ scientists/ school teachers., clearly define them, with reliable justification
S.No Position Company/ Govt Remarks Additional skills
organization required, if any
1 Scientific Food Corporation of India Upgrade their skills Communication skills
assistant and get promoted Language skills
Computational skills
2 Scientific Central ware house Upgrade their skills Communication skills
assistant corporation and get promoted Language skills
3 Food safety State and central Upgrade their skills Communication skills
officers government organizations and get promoted Language skills
4 Technicians State and central Upgrade their skills Communication skills
government institutes and and get promoted Language skills
labs Computational skills
a. List of Govt. organizations / Pvt companies for employment opportunities or internships or projects
S.No Company/ Govt organization Position type Level of Position

1 Food Corporation of India Scientific assistant Basic
( can be upgraded)
2 Central ware house corporation Scientific assistant Basic
( can be upgraded)
3 State and central government organizations Food safety officers Basic
( can be upgraded)
4 State and central government institutes and Lab Technicians Basic
labs ( can be upgraded)
5 National Institute of Nutrition Lab assistant/project Basic
assistant ( can be upgraded)
6 Centre for Cellular and Molecular Biology Lab assistant/project Basic
7 National Centre for Biological Sciences Lab assistant/project Basic
8 Central Drug Research Institute Lab assistant/project Basic
9 Central Food Technological Research Lab assistant/project Basic
Institute assistant ( can be upgraded)
10 International Crops Lab assistant/project Basic
Research Institute for the assistant ( can beupgraded)
Semi-Arid Tropics
11 Indian Institute of Spices Lab assistant/project Basic
Research assistant ( can be pgraded)
12 Indian Institute of Lab assistant/project Basic
Integrative Medicine assistant ( can be pgraded)
13 National Institute of Lab assistant/project Basic
Virology assistant ( can beupgraded)
14 Institute of Life Sciences Lab assistant/project Basic
assistant ( can be pgraded)
15 National Institute of Lab assistant/project Basic
Immunology assistant ( can be pgraded)
16 Indian Institute of Lab assistant/project Basic
Chemical Biology (IICB) assistant ( can be upgraded)
17 Centre for Chronic Lab assistant/project Basic
Disease Control (CCDC) assistant ( can be upgraded)
18 Indian Institute of Immunologicals (IIL) Lab assistant/project Basic
19 National Institute of Animal Biology Lab assistant/project Basic
(NIAB) assistant ( can be upgraded)
b. Any specific instructions to the teacher /Course setters/Exam-Chief Superintendent
Course setter may strictly follow the given syllabus
Course evaluators may strictly follow the scheme of evaluation
3. Program objectives, outcomes, co-curricular and assessment methods
B.Sc. BIOCHEMISTRY
1. Aim and objectives of UG program in Subject:

Biochemistry is the study of biological phenomena at the molecular level. Its aim is to understand the
fundamental chemical principles that govern complex biological systems. The program aims to
provide an advanced understanding of the core principles and topics of biochemistry and their
experimental basis to enable students acquire a specialized biological and chemical knowledge. The
program also develops a foundation in the concepts and facts in modern cellular molecular biology
and biochemistry and be familiar with various ways of organizing and accessing scientific
knowledge
2. Learning outcomes of Subject:

1. Acquire knowledge and understanding of the molecular machinery of living cells;
2. Acquire knowledge and understanding of the principles that govern the structures of
macromolecules and their participation in molecular recognition;
3. Enrich with principles and basic mechanisms of metabolic control and molecular signaling
4. Use basic laboratory skills and apparatus to obtain reproducible data from biochemical
experiments;
5. Implement experimental protocols, and adapt them to plan and carry out simple investigations
6. Analyze, interpret, and participate in reporting to their peers on the results of their laboratory
experiments;
7. Participate in and report orally on team work investigations of problem-based assignments;
8. Build knowledge and understanding in tackling more advanced and specialised courses, and
more widely to pursue independent, self-directed and critical learning.
9. Recommended Skill enhancement courses: (Titles of the courses given below and details of the
syllabus for 4 credits (i.e., 2 units for theory and Lab/Practical) for 5 hrs class-cum-lab work
 Industrial Biochemistry
 Environmental Biochemistry
 Pharmaceutical Biochemistry
10. Recommended Co-curricular activities:(Co-curricular Activities should not promote copying
from text book or from others’ work and shall encourage self/independent and group learning)
A. Measurable:
1. Assignments on: Physiology
2. Student seminars (Individual presentation of Courses) on topics relating to:
Immunology
3. Quiz Programmes on: Molecular Biology
4. Individual Field Studies/projects: Nutritional Biochemistry
5. Group discussion on: metabolism topics
6. Group/Team Projects on: Enzymology
B General
1. Collection of news reports and maintaining a record of Course-cuttings relating to
topics covered in syllabus
2. Group Discussions on: New scientific approaches and Discoveries
3. Watching TV discussions and preparing summary points recording personal
observations etc., under guidance from the Lecturers
4. Any similar activities with imaginative thinking.
Organizing exhibitions
Preparation of charts and models
Science fairs
Science clubs
Essay writing
11. Recommended Continuous Assessment methods:
Slip test
Oral test
Assignments
Seminars
DETAILS OF COURSE WISE SYLLABUS

4. Details of course-wise Syllabus
B.Sc. Semester - I Credits: 4

Course: 1 BIOMOLECULES Hrs/Wk: 4
Aim and objectives of Course (Biomolecules):
The student gains knowledge in the chemistry of biomolecules such as water, carbohydrates, lipids,
proteins and nucleic acids which make up all the living organisms including humans.
Learning outcomes of Course
This course will enable the student to understand the importance of biomolecules in living organisms
and effects of their alterations in diseases occurring in plants, animals and humans.
The practical will give the expertise to the student for analysis of any biological or non-biological
sample for identification of its chemical composition.
3∙Detailed Syllabus: (Five units with each unit having 12 hours of class work)
UNIT I: 12 hours
Carbohydrates: Carbohydrates: Classification, monosaccharides, D and L designation, open chain
and cyclic structures, epimers and anomers, mutarotation, reactions of carbohydrates (due to
functional groups - hydroxyl, aldehyde and ketone. Amino sugars, Glycosides. Structure and
biological importance of disaccharides (sucrose, lactose, maltose, isomaltose, trehalose), tri-
saccharides (raffinose, melezitose), structural polysaccharides (cellulose, chitin, pectin) and storage
polysaccharides (starch, inulin, glycogen). Glycosaminoglycans, Bacterial cell wall polysaccharides.
Outlines of glycoproteins, glycolipids and blood group substances.
UNIT II: 12 hours
Lipids: Classification, saturated and unsaturated fatty acids, structure and properties of fats and oils
(acid, saponification and iodine values, rancidity). General properties and structures of
phospholipids. Prostaglandins- structure, types and biological role. Lipoproteins- types and functions,
Bio-membranes-formation of micelles, bilayers, vesicles, liposomes. Membrane composition and
organization - Fluid mosaic model.
UNIT III: 12 hours
Amino Acids: Amino Acids: Classification, structure, stereochemistry, chemical reactions of amino
acids due to carbonyl and amino groups. Titration curve of glycine and px values. Essential and non-
essential amino acids, non-protein amino acids. Peptide bond -Nature and conformation. Naturally
occurring peptides - glutathione, enkephalin.
UNIT IV: 12 hours
Proteins: Proteins Classification based on solubility, shape and function. Determination of amino
acid composition of proteins. General properties of proteins, denaturation and renaturation of
proteins. Structural organization of proteins- primary, secondary, tertiary and quaternary structures
(Eg. Hemoglobin and Myoglobin).
UNIT V: 12 hours
Nucleic acids and porphyries: Types of RNA and DNA. Structure of purines and pyrimidines,
nucleosides, nucleotides. Stability and formation of phosphodiester linkages. Effect of acids, alkali
and nucleases on DNA and RNA. Structure of Nucleic acids- Watson-Crick DNA double helix
structure, denaturation and renaturation kinetics of nucleic acids-, Tm-values and their significance,
cot curves and their significance.Structure of porphyrins: Identification of Porphyrins,
Protoporphyrin, porphobilinogen properties, Structure of metallo-porphyrins–Heme, cytochromes
and chlorophylls.
RECOMMENDED BOOKS:
1. The biochemistry of Nucleic acids; Adams et al., Chapman and Hall, 1986.
2. Proteins: A guide to study by physical & chemical methods, Haschemeyer and Haschemeyer,
3. Proteins: Structure, function and evolution. Dickerson & Geis, 2nd Edn, Benjamin/Cummings.
4. Biochemistry - Zubay C, Addison – Wesley, 1986.
5. Biochemistry, A problem Approach, 2nd Edn. Wood, W.B. Addison Wesley 1981.
6. Biochemistry, Lehninger A.H.
7. Textbook of Biochemistry West, E.S., Todd, Mason & Vanbruggen, Macmillian&Co.
8. Principles of Biochemistry White-A, Handler, Pand Smith E.L. Mc Grew Hill.
9. Organic chemistry, I.L. Finar, ELBS. (1985).
10. Organic Chemistry by Morrison and Boyd (2000) Prentice Hall.
11. Fundamentals of Biochemistry by Donald Voet (1999).
4∙ Details of Lab/Practical/Experiments/Tutorials syllabus:

B.Sc. Semester - I Credits: 1
Course: 1(L) BIOMOLECULES LAB Hrs/Wk: 2
List of practical Experiments:

1. Qualitative identification of carbohydrates- glucose, fructose, ribose/xylose, maltose, sucrose,
lactose, starch/glycogen.
2. Qualitative identification of amino acids-histidine, tyrosine, tryptophan, cysteine, arginine.
3. Qualitative identification of lipids- solubility, saponification, acrolein test, Salkowski test,
Lieberman-Burchard test.
4. Preparation of Osazones and their identification.
5. Absorption maxima of colored substances-p-Nitrophenol, Methyl orange.

A.
Measurable:
1.
Assignments on: Amino Acids
2.
Student seminars (Individual presentation of Courses) on topics relating to: Syllabus
3.
Quiz Programmes on: Nucleic acids and porphyrins
4.
Individual Field Studies/projects: relating to Syllabus
5.
Group discussion on: Carbohydrates
B.
Group/Team Projects: qualitative and quantitative Analysis of Biomolecules General
topics covered in syllabus.
2. Group Discussions on: new scientific approaches and Discoveries
Science fairs
Science clubs
Essay writing
 Slip test
 Oral test
 Assignments
 Seminars
B.Sc. Semester - II Credits: 4
Course-2 ANALYTICAL TECHNIQUES Hrs/Wk: 4
Aim and objectives of Course: Analytical Techniques
The knowledge in the analytical techniques will enable the student for isolation, purification and chemical
characterization of compounds from plants and microbes which will have medical or commercial importance.
1. The student will learn the various analytical techniques and their applications in separation
and isolation of cells and tissues for studying their functional abnormalities
2. The practicals will provide the expertise to the student for quantification of electrolytes and other
metal ions, hormones and identification of bacteria.
3. The expertise gained by the student in this course can be useful in food industries, pharma industries,
clinical and microbiological labs.
UNIT I: 12 hours
Biophysical Concepts & Cell disruption methods:Water as biological solvent, Buffers,
measurement of pH, electrodes, Biological relevance of pH, pKa value, Electrical conductivity,
analysis of drinking water and pond water, Total dissolved salts (TDS), BOD, COD, soil analysis
(texture, organic matter, elements), Methods of tissue homogenization: (Potter-Elvejham, mechanical
blender, sonicator and enzymatic).
UNIT II: 12 hours
Microscopy and Centrifugation: Basic principles of light microscopy, phase contrast, electron
microscope and fluorescent microscope and their applications. Centrifugation techniques, principles
and applications- differential, density gradient. Ultra-centrifugation- preparative and analytical.
UNIT III: 12 hours
Chromatographic techniques: Chromatography - Principle and applications, Types of
chromatographic techniques - Course chromatography- solvents, Rf value, applications; Thin layer
chromatography- principle, choice of adsorbent and solvent, Rf value, applications; Gel filtration,
Ion- exchange- principle, resins, action of resins, experimental techniques, applications, separation of
metal ions; Affinity chromatography.
UNIT IV: 12 hours
Spectroscopy and tracer techniques: Electromagnetic radiation, Beer-Lambert’s law. Colorimetry
and Spectrophotometry, spectrofluorimetry, flame photometry. Tracer techniques: Radio isotopes,
units of radio activity, half-life, β and γ- emitters, use of radioactive isotopes in biology, ELISA.
UNIT V: 12 hours
Electrophoresis: Electrophoresis- principles and applications of Course, polyacrylamide (native and
SDS) and agarose gel electrophoresis, isoelectric focusing, immune-electrophoresis-types and
applications.
RECOMMENDED TEXT BOOKS:
1. Principles and Techniques of practical Biochemistry. Eds. Williams and Wilson.
2. Techniques in Molecular biology Ed. Walker & Gastra, Croom Helm, 1983.
3. Principles of instrumental analysis, 2nd Ed, Holt-Sanders, 1980.
4. An introduction to spectroscopy for Biochemistry. Ed. Brown S.N., Academic press
5. Analytical Biochemistry, Holmes and Hazel peck, Longman, 1983.
6. An introduction to practical biochemistry. David T. Plummer, Tata Mac Grew-Hill
7. Biophysical chemistry, Edshall & Wyman, Academic press Vol. II & I.
8. A textbook of quantitative inorganic analysis including elementary instrumental analysis,
Vogel ELBS.
9. Biochemical calculations Seigel, IH, 2nd Edit, John Wiley & sons Inc., 1983.
10. Analytical Biochemistry by Friefelder David.
B.Sc. Semester - II Credits: 1
Course-2(L) ANALYTICAL TECHNIQUES LAB Hrs/Wk: 2
Details of Lab/Practical/Experiments/Tutorials syllabus:
1. Preparation of Buffers
2. Sub cellular fraction using Centrifuge
3. Isolation of RNA and DNA from tissue/culture.
4. Qualitative Identification of DNA, RNA and Nitrogen Bases
5. Isolation of egg albumin from egg white.
6. Isolation of cholesterol from egg yolk.
7. Isolation of starch from potatoes.
8. Isolation of casein from milk.
9. Separation of amino acids by Course chromatography.
10. Determination of exchange capacity of resin by titrimetry.
11. Separation of serum proteins by Course electrophoresis.
1. Recommended Co-curricular activities: (Co-curricular Activities should not promote copying

A. Measurable:
1. Assignments on: Microscopy and Centrifugation
2. Student seminars (Individual presentation of Courses) on topics relating to: Tracer
techniques
3. Quiz Programmes on: Spectroscopy
4. Individual Field Studies/projects: Chromatographic techniques
5. Group discussion on: Spectroscopy and tracer techniques
6. Group/Team Projects on: Isolation and characterization of compounds from different
sources using above techniques.
B. General
Science fairs
Science clubs
Essay writing
 Slip test
 Oral test
 Assignments
 Seminars
B.Sc. Semester - III Credits: 4

Course: 3 ENZYMOLOGY, BIOENERGETICS AND INTERMEDIARY Hrs/Wk: 4
METABOLISM
Aim and objectives of Course (Enzymology, Bioenergetics and Intermediary Metabolism):
The student will get knowledge in enzymes, their physiological importance and other applications. They also
understand the metabolism of biomolecules like carbohydrate, lipid and aminoacids.

a) The student will know how the biomolecules such as carbohydrates, lipids and proteins get
metabolized for the purpose of energy and other physiological functions in the body.
b) The course will enable the student to understand the pathophysiology of metabolic diseases
such as diabetes, atherosclerosis etc. which occur due to alterations in metabolism.
c) The practicals will provide the expertise for quantification of enzymes’ activities, glucose,
proteins and lipid levels in blood which will have clinical applications
UNIT I: 12 hours
Enzymology: Introduction to Biocatalysis, differences between chemical and biological catalysis.
Nomenclature and classification of enzymes. Definition of holo-enzyme, apo-enzyme, coenzyme,
cofactor. Active site, Enzyme specificity. Principles of energy of activation, transition state.
Interaction between enzyme and substrate-lock and key, induced fit models. Fundamentals of
enzyme assay, enzyme units. Outlines of mechanism of enzyme action, factors affecting enzyme
activity. Commercial application of enzymes.
UNIT II: 12 hours

Bioenergetics and Biological oxidation: Bioenergetics: Thermodynamic principles – Chemical
equilibria; free energy, enthalpy (H), entropy (S). Free energy change in biological transformations in
living systems; High energy compounds. Energy, change, oxidation-reduction reactions.Organization
of electron carriers and enzymes in mitochondria. Classes of electron-transferring enzymes,
inhibiters of electron transport. Oxidative phosphorylation. Uncouplers and inhibitors of oxidative
phosphorylation. Mechanism of oxidative phosphorylation.
UNIT III: 12 hours

Carbohydrate Metabolism: Concept of anabolism and catabolism. Glycolytic pathway, energy
yield. Fate of pyruvate-formation of lactate and ethanol, Citric acid cycle, regulation, energy yield,
amphipathic role. Anaplerotic reactions. Glycogenolysis and glycogenesis. Pentose phosphate
pathway. Gluconeogenesis. Photosynthesis- Light and Dark reactions, Calvin cycle, C4 Pathway.
Disorders of carbohydrate metabolism- Diabetes Mellitus.
UNIT IV: 12 hours

Lipid Metabolism: Catabolism of fatty acids (β- oxidation) with even and odd number of carbon
atoms, Ketogenesis, de novo synthesis of fatty acids, elongation of fatty acids in mitochondria and
microsomes, Biosynthesis and degradation of triacylglycerol and lecithin. Biosynthesis of
cholesterol. Disorders of lipid metabolism.
UNIT V: 12 hours
Metabolism of Amino acids: General reactions of amino acid metabolism- transamination,
decarboxylation and deamination, Urea cycle and regulation, Catabolism of carbon skeleton of amino
acids- glycogenic and ketogenic amino acids. Metabolism of glycine, serine, aspartic acid,
methionine, phenylalanine and leucine. Biosynthesis of creatine. Inborn errors of aromatic and
branched chain amino acid metabolism.
RECOMMENDED BOOKS:
1. Understanding enzymes: Palmer T., Ellis Harwood ltd., 2001.
2. Enzyme structure and mechanism. Alan Fersht, Freeman & Co. 1997
3. Principles of enzymology for food sciences: Whitaker Marc Dekker 1972.
4. Principles of Biochemistry, White. A, Handler, P and Smith.
5. Biochemistry, Lehninger A.L.
6. Biochemistry, Lubert Stryer.
7. Review of physiological chemistry, Harold A. Harper.
8. Text of Biochemistry, West and Todd.
9. Metabolic pathways – Greenberg.
10. Mitochondria, Munn.
11. Biochemistry, 2nd Edition, G. Zubay.
B.Sc. Semester - III Credits: 1

ENZYMOLOGY, BIOENERGETICS AND INTERMEDIARY Hrs/Wk: 2
Course: 3(L) METABOLISM LAB
1. Details of Lab/Practical/Experiments/Tutorials syllabus:

1. Assay of amylase.
2. Assay of urease.
3. Assay of catalase
4. Effect of pH, temperature and substrate concentration on enzyme activity.
5. Estimation of glucose by DNS method.
6. Estimation of glucose by Benedict’s titrimetric method.
7. Estimation of total carbohydrates by Anthrone method.
8. Tests for lipids- Salkowski test, Lieberman-Burchard test.
9. Estimation of amino acid by Ninhydrin method.
10. Estimation of protein by Biuret method.

C. Measurable:
1. Assignments on: Enzymology.
2. Student seminars (Individual presentation of Courses) on topics relating to: Metabolic
pathways.
3. Quiz Programmes on: Bioenergetics and Biological oxidation.
4. Individual Field Studies/projects: metabolism of biomolecules in healthy and diseased
condition.
5. Group discussion on: Lipid Metabolism
6. Group/Team Projects on: Bioenergetics and Biological oxidation
7. General .
1. Collection of news reports and maintaining a record of Course-cuttings relating to topics
covered in syllabus.
3. Watching TV discussions and preparing summary points recording personal observations
etc., under guidance from the Lecturers.
Science fairs
Science clubs
Essay writing
Slip test
Oral test
Assignments
Seminars
B.Sc. Semester - IV Credits: 4

Course:4 PHYSIOLOGY, NUTRITIONAL AND CLINICAL Hrs/Wk: 4
BIOCHEMISTRY
Aim and objectives of Course (Physiology, Nutritional and Clinical Biochemistry):
The student will get knowledge on different physiological systems and their functions in the
human body. By studying blood, its composition and its functions the student will understand the
importance of blood.
Learning outcomes of Course:
a) This course will also provide knowledge on hormones, their functions and the diseases
occurring due to alterations in the levels of hormones.
b) By studying this course the student will know the nutritional importance of proteins,
carbohydrates, lipids, vitamins and minerals.
c) Clinical biochemistry unit along with practicals will enable the student to do diagnostic tests
for liver diseases, Gastro intestinal diseases, renal diseases and nutritional deficiencies.
UNIT I: 12hours
Digestion and Blood:Digestion and absorption of carbohydrates, lipids and proteins. Role of
enzymes and gastrointestinal hormones in digestion. Composition of blood, Blood groups,
coagulation of blood and disorders of blood coagulation (haemophilia). Hemoglobin and transport of
gases in blood (oxygen and CO2). Types of anemias, haemoglobinopathies-sickle cell anemia.
UNIT II: 12hours

Nervous system and excretory system: Introduction to nervous system, general organization of
nervous system, Neurons-structure, types, properties and functions; Neurotransmitters, Cerebrospinal
fluid-composition and functions, Reflex-types and properties. Introduction to excretory system.
Organization of kidney, Structure and functions of nephron, Urine formation, Role of kidneys in
maintaining acid-base and electrolyte balance in the body.
Unit III: 12 hours

Endocrinology: Endocrinology- organization of endocrine system. Classification of hormones.
Outlines of chemistry, physiological role and disorders of hormones of thyroid, parathyroid, pituitary
and hypothalamus. Introduction of gastrointestinal hormones. Mechanism of hormonal action- signal
transduction pathways for glucocorticoids and insulin. Adrenalin, estrogen and progesterone.
UNIT IV: 12hours

Nutritional Biochemistry: Balanced diet. Calorific values of foods and their determination by bomb
calorimeter. BMR and factors affecting it. Specific dynamic action of foods. Energy requirements
and recommended dietary allowance (RDA) for children, adults, pregnant and lactating women.
Sources of complete and incomplete proteins. Biological value of proteins. Malnutrition-
Kwashiorkor, Marasmus and PEM. Vitamins- sources, structure, biochemical roles, deficiency
disorders of water and fat soluble vitamins. Introduction to nutraceutical and functional foods. Bulk
and trace elements-Ca, Mg, Fe, I, Cu, Mo, Zn, Se and F.
UNIT V: 12hours
Clinical Biochemistry: Plasma proteins in health and disease. Liver diseases-jaundice. Liver
function tests- conjugated and total bilirubin in serum, albumin: globulin ratio, Serum enzymes in
liver diseases-SGOT, SGPT, GGT, CPK, Acid and alkaline phosphatases. Serum lipids and
lipoproteins. Normal and abnormal constituents of urine. Renal function tests-Blood urea, creatinine,
GFR, creatinine clearance. GTT and gastric and pancreatic function tests.
RECOMMENDED BOOKS:
1. Essentials of Food and Nutrition, Vol. I & II, M.S. Swaminathan.
2. Text Book of Biochemistry with clinical correlations. Thomas M. Devlin (John Wily)
3. Harper’s Review of Biochemistry, Murray et al (Longman).
4. Biochemical aspects of human disease – R.S. Elkeles and A.S. Tavil. (Blackwell Scientific
Publications).
5. Clinical chemistry in diagnosis and treatment–Joan F.Zilva and P.R.Pannall (Lloyd-Luke
Medical Books, 1988).
6. Varley’s Practical clinical Biochemistry – Ed. Alan W. Gowenlock (Heinemann Medical
Books, London, 1988).
PHYSIOLOGY NUTRITIONAL AND CLINICAL
Course:4(L) Hrs/Wk: 2
BIOCHEMISTRY LAB
1.Estimation of calcium by titrimetry

2.Estimation of iron by Wong’s method.
3.Estimation of vitamin C by 2, 6 -dichlorophenol indophenol method.
4.Determination of iodine value of an oil.
5.Estimation of hemoglobin in blood.
6.Total count - RBC and WBC. Differential count.
7.Determination of blood group and Rh typing.
8.Visualization of antigen antibody reactions (Ouchterlony technique).
9.Urine analysis for albumin, sugars and ketone bodies.
10.Estimation of urinary creatinine.
11.Estimation of blood Glucose.
12.Estimation of serum total cholesterol.

A. Measurable:
1. Assignments on: Endocrinology
2. Student seminars (Individual presentation of Courses) on topics relating to: syllabus
B. Quiz Programmes on: Digestion and Blood
1. Individual Field Studies/projects: Clinical Biochemistry
2. Group discussion on: Nutritional Biochemistry
3. Group/Team Projects on: Clinical Biochemistry
C. General
1. Collection of news reports and maintaining a record of Course-cuttings relating to topics
covered in syllabus
3. Watching TV discussions and preparing summary points recording personal observations
etc., under guidance from the Lecturers
4.Any similar activities with imaginative thinking.
Science fairs
Science clubs
Essay writing
Slip test
Oral test
Assignments
Seminars
MICROBIOLOGY, IMMUNOLOGY AND
Course:5 Hrs/Wk: 4
MOLECULAR BIOLOGY
Aim and objectives of Course (Microbiology, Immunology and Molecular biology):
a) This course will enable the student to know various microbes such as bacteria, fungi and
viruses, their structures and other properties and diseases caused by them.
b) The student will also get knowledge in their commercial applications by making use of
their beneficial effects such as fermentation in alcohol production, nitrogen fixation in
agriculture etc.
Learning outcome of Course:
a) The student will get knowledge in immune system, vaccines and also understand the
pathogenesis of auto immune diseases and immune deficiency diseases.
b) This course will provide knowledge and expertise in molecular biology such as genes, their
structure and importance. This will also enable the student to know the applications of PCR in
cloning and diagnosis of genetic and viral diseases.
c) The practicals will provide the expertise to the student to work in microbiology laboratory, food and
pharma industries, and biotech companies for production of vaccines and other life-saving drugs.
UNIT I: 12hours
Microbiology: Introduction to microbiology and microbial diversity. Classification of
microorganisms- prokaryotic and eukaryotic microorganisms. Bacterial structure, growth curve and
kinetics of growth. Introduction to viruses-plant and animal viruses, structure, life cycle, Food and
dairy microbiology. Nitrogen Fixation Nitrogen cycle, Non-biological and biological nitrogen
fixation, photosynthetic and non-photosynthetic systems, Nitrogenase system. Utilization of nitrate
ion, Ammonia incorporation into organic compounds
UNIT II: 12 hours
Microbial techniques: Preparation of different growth media, isolation and culturing and preservation
of microbes, Gram’s staining- Gram positive and Gram-negative bacteria, motility and sporulation,
Sterilization techniques -Physical methods, chemical methods, radiation methods, ultrasonic and
antibiotic resistance.
UNIT III: 12 hours
Applied Biochemistry : Fermentation Technology: Batch, continuous culture techniques, principle,
types of fermentors. Pasteur Effect. Industrial production of chemicals- alcohol, acids (citric acid),
solvents (acetone), antibiotics (penicillin), Enzyme Technology: Immobilization of enzymes and
cells, industrial applications, enzymes in Bioremediation.
UNIT IV: 12hours
Immunology: Organs and cells of immune system. Innate and acquired immunity, Cell mediated and
humoral immunity (T-cells and B-cells). Classification of immunoglobulins, structure of IgG.
Epitopes / antigenic determinants. Concept of haptens. Adjuvants. Monoclonal antibodies. Antigen-
antibody reactions- agglutination, immunoprecipitation, immunodiffusion. Blood group antigens.
Immunodiagnostics- ELISA, RIA. Vaccines and their classification. Traditional vaccines-live and
attenuated. Modern vaccines- recombinant and peptide vaccines. Outlines of hypersensitivity
reactions.
UNIT V: 12 hours
Molecular biology: Types of RNA and DNA, DNA replication-leading and lagging strands, Okazaki
fragments, inhibitors of DNA replication. Genetic code, Protein synthesis-transcription, translation,
inhibitors of protein synthesis. Outlines of cloning technology, vectors, restriction enzymes, PCR,
applications of cloning in agriculture, industry and medical fields.
RECOMMENDED BOOKS:
1. Willey MJ, Sherwood, LM &Woolverton C J (2013) Prescott, Harley and Klein’s
Microbiology by. 9th Ed., McGraw Hill.
2. Atlas RM. (1997). Principles of Microbiology. 2nd edition. W. M. T. Brown Publishers.
3. Pelczar MJ, Chan ECS and Krieg NR. (1993). Microbiology. 5th edition. McGraw Hill Book
Company.
4. Fermentation Technology (2nd ed.) Standury (Pergman press)
5. Biotechnology: Textbook of Industrial microbiology 2nd Edit. by Crueger and
Crueger (2000).
6. Principles of Biochemistry, White. A; Handler P and Smith.
7. Ivan M. Roitt; Essential Immunology (Latest Edition). Blackwell Scientific Publication
8. Goldsby RA, Kindt TJ, Osborne BA. (2007). Kuby’s Immunology. 6th edition
9. W.H. Freeman and Company, New York.
10. Richard C and Geiffrey S. (2009). Immunology. 6th edition. Wiley Blackwell Publication.
11. Watson JD, Baker TA, Bell SP, Gann A, Levine M and Losick R (2008) Molecular Biology
of the Gene, 6th edition, Cold Spring Harbour Lab. Press, Pearson Publication
12. Molecular biology by David Freifelder.
MICROBIOLOGY, IMMUNOLOGY AND
Course:5(L) Hrs/Wk: 2
MOLECULAR BIOLOGY LAB

List of Practical Experiments
1. Biosafety and good laboratory practices (GLP) of Microbiology.
2. Sterilization of microbial media by autoclave.
3. Isolation of pure cultures: (i) Streak plate method. (ii) Serial dilution method.
4. Demonstration of alcohol fermentation.
5. Antibiotic sensitivity by Course disc method.
6. Effect of nitrogen sources on growth of E. coli
7. Immunodiffusion by Ouchterlony method.
8. Blood group analysis.
9. Isolation of DNA from plant tissues.
10. Spotters.

A .Measurable:. Assignments on: Immunology
1. Student seminars (Individual presentation of Courses) on topics relating to:
Microbiology & Molecular Biology.
2. Quiz Programmes on: Molecular biology
3. Individual Field Studies/projects: Microbiology
4. Group discussion on: Applied Biochemistry
5. Group/Team Projects on: Microbial techniques
B. General
Science fairs
Science clubs
Essay writing
Slip test
Oral test
Assignments
Seminars
BLUE PRINT FOR MODEL QUESTION COURSE - THEORY
Time: 3 hours Max marks: 75M

SECTION A
Answer any 5 questions. Each question carries 5 marks. (5 x 5 =25M)
(Questions 1-5, one question from each unit & questions 6, 7 & 8 can be from any of the
5 units)
1. Unit - I
2. Unit-II
3. Unit-III
4. Unit-IV
5. Unit-V
6.
7.
8.
SECTION B
Answer all the questions. Each question carries 10 marks. (5X10 =50M)
9.a) from unit 1

(OR)
b) from unit 1
11.a) from unit II

(OR)
b) from unit II
12.a) from unit III

(OR)
b) from unit III
13.a) from unit IV

(OR)
b) from unit IV
14.a) from unit V

(OR)
b) from unit V
BLUE PRINT FOR MODEL PRACTICAL COURSE
Experiment/ problem solving: 40 marks (Major/Minor/Principles/Spotters)
Record/report submission: 5 marks
Viva/inter- active questioning in lab exam: 5 marks
MODEL QUESTION COURSE
B. Sc DEGREE EXAMINATION
SEMESTER: I
Course 1: BIOMOLECULES
Time: 3Hrs. Max. Marks: 75
SECTION A
Answer any 5 questions. Each question carries 5 marks 5 x 5 =25M
1. Mutarotation
2. Prostaglandins
3. Enkephalin
4. General properties of proteins
5. Heme
6. Types of RNA and DNA
7. Peptide bond
8. Fluid mosaic model
SECTION B
Answer all the questions. Each question carries 10 marks 5X10 =50M
9. a) Write about classification of carbohydrates.

(OR)
b) Write about structure and biological importance of disaccharides and trisaccharides
10. a) Write about lipids classification

(OR)
b) Write about prostaglandins- structure, types and biological role.
11. a) Write about amino acid classification

(OR)
b) Write about titration curve of glycine and px values
12. a) Write about protein classification

(OR)
b) Write about structural organization of myoglobin
13. a) Write about Watson-Crick DNA double helix structure

(OR)
b) Write about denaturation and renaturation kinetics of nucleic acids
BIOMOLECULES LAB
MODEL PRACTICAL QUESTION COURSE

Time: 3hrs Max. Marks: 50M
Major experiment 15M

1. Qualitative identification of carbohydrates- glucose, fructose, ribose/xylose, maltose,
sucrose, lactose, starch/glycogen
Minor experiment 10M
2. Absorption maxima of colored substances-p-Nitrophenol, Methylorange
Principles 5M
3. Qualitative identification of amino acids
4. Lieberman-Burchardtest
Record/report submission 5M
Viva/inter- active questioning in lab exam 5M
SEMESTER: II
Course 2: ANALYTICAL TECHNIQUES
SECTION A
Answer any 5 questions. Each question carries 5 marks 5 x 5M =25M
1. Biological relevance of pH
2. Basic principles of light microscopy
3. Thin layer chromatography
4. Beer-Lambert’s law
5. Isoelectric focusing
6. ELISA
7. Gel filtration
8. BOD
SECTION B
Answer all the questions. Each question carries 10 marks 5X10M =50M
9. a) Write about methods of tissue homogenization

(OR)
b) Write about buffers and their role in maintenance of pH
10. a) Write about ultra-centrifugation and its working principle.

(OR)
b) Write about fluorescent microscope and their applications.
11. a) Write about affinity chromatography

(OR)
b) Write about ion- exchange chromatography
12. a) Write about radio-isotopes and their use in biology

(OR)
b) Write about spectrofluorimetry
13. a) Write about immune-electrophoresis-types and applications.

(OR)
b). Write about isoelectric focusing
ANALYTICAL TECHNIQUES Lab
Time:3hrs Max. Marks:50M
1. Separation of amino acids by Course chromatography
2. Determination of exchange capacity of resin by titrimetry
Principles 5M
3. Isolation of cholesterol from egg yolk

4. Isolation of casein from milk
SEMESTER: III
Course 3: ENZYMOLOGY, BIOENERGETICS AND NTERMEDIARY METABOLISM
SECTION A
1. Enzyme specificity
2. Enthalpy (H)
3. Diabetes Mellitus
4. Lecithin
5. Urea cycle
6. Cholesterol
7. C4 Pathway
8. Inhibitors of electron transport
SECTION B
9.a) Write about nomenclature and classification of enzymes

(OR)
b) Write about lock and key, induced fit models
10. a) Write about high energy compounds.

(OR)
b) Write about mechanism of oxidative phosphorylation
11. a) Write about pentose phosphate pathway
(OR)
b) Write about citric acid cycle
12. a) Write about disorders of lipid metabolism.

(OR)
b) Write about catabolism of fatty acids (β- oxidation) with even number of carbon atoms
13. a) Write about inborn errors of aromatic and branched chain amino acid metabolism.
(OR)
b) Write about catabolism of glycogenic amino acids
ENZYMOLOGY, BIOENERGETICS AND INTERMEDIARY METABOLISM Lab
Time: 3hrs Max. Marks: 50M
1. Estimation of amino acid by Ninhydrin method
2. Assay of amylase
Principles 5M
3. Estimation of glucose by DNS method
4. Assay of catalase
SEMESTER: IV
Course 4: PHYSIOLOGY, NUTRITIONAL AND CLINICAL BIOCHEMISTRY
SECTION A
1. Sickle cell anemia.
2. Neurotransmitters
3. Gastrointestinal hormones
4. Kwashiorkor
5. SGOT
6. BMR
7. Physiological role of hormones
8. Role of kidneys in acid-base balance
SECTION B
9. a) Write about blood coagulation

(OR)
b) Write about Digestion and absorption of carbohydrates
10. a) Write about nephron.

(OR)
b) Write about Cerebrospinal fluid-composition and functions
11. a) Write about Classification of hormones
(OR)
b) Write about signal transduction pathways for glucocorticoids
12. a) Write about recommended dietary allowance (RDA) for children and adults.
(OR)
b) Write about sources, structure, biochemical roles of vitamins.
13. a) Write about Liver function tests

(OR)
b) Write about pancreatic function tests
Physiology, Nutritional and Clinical Biochemistry Lab

Time: 3hrs Max. Marks. 50M
1. Determination of blood group and Rh typing
2. Estimation of calcium by titrimetry
Principles 5M
3. Estimation of hemoglobin in blood
4. Estimation of serum total cholesterol
SEMESTER: IV
Course 5: MICROBIOLOGY, IMMUNOLOGY AND MOLECULAR BIOLOGY
SECTION A
1. Nitrogenase system.
2. Gram’s staining
3. Enzymes in Bioremediation
4. Haptens
5. Okazaki fragments
6. RIA
7. Pasteur effect
8. Antibiotic resistance.
SECTION B
9.a) Write about non-biological and biological nitrogen fixation.

(OR)
b) Write about bacterial growth curve and kinetics of growth.
10. a) Write about Physical methods and chemical methods of Sterilization.

(OR)
b) Write about isolation culturing and preservation of microbes.
11. a) Write about industrial production of antibiotics

(OR)
b) Write about Immobilization of enzymes.
12. a) Write about Vaccines and their classification.

(OR)
b)Write about Classification of immunoglobulins
13. a) Write about DNA replication in prokaryotes

(OR)
b) Write about PCR
MICROBIOLOGY, IMMUNOLOGY AND MOLECULAR BIOLOGY LAB

Time: 3hrs Max. Marks. 50M
1. Isolation of DNA from plant tissues.

1. Antibiotic sensitivity by Course disc method
Spotters 5M

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ADIKAVI NANNAYA UNIVERSITY :: RAJAHMAHENDRAVARAM

B.Sc Bio-Chemistry Syllabus (w.e.f: 2020-21 A.Y)

UG PROGRAM (4 Years Honors)

Members of BOS (Contact details)

Dr.K.Kamalakara Rao Department of iochemistry

Syllabus and Model Question Papers

S. No Particulars Page No.

Meeting held on: 22/01/2021………….Time: 10 AM – 4 PM

Dr. D. Kalyani, Assistant Professor, Department of Zoology, Adikavi Nannaya University,

3. Resolved to prepare model question Courses in the given prescribed format.

4. Resolved to prepare a list of equipments/software required for each lab/practicals.

7. Resolved to prepare a list of Course setters/Course evaluators/project evaluators in the given

Hrs/Week Credits Max. Marks Max. Marks

a. Proposed combination subjects: Biochemistry, Biotechnology, Microbiology

d. List of Proposed Skill enhancement courses with syllabus, if any

Sem. Lab/Practical Names of Instruments/Software/ Brand Name Qty

S.No Company/ Govt organization Position type Level of Position

b. Any specific instructions to the teacher /Course setters/Exam-Chief Superintendent

Course setter may strictly follow the given syllabus

Course evaluators may strictly follow the scheme of evaluation

1. Aim and objectives of UG program in Subject:

2. Learning outcomes of Subject:

DETAILS OF COURSE WISE SYLLABUS

B.Sc. Semester - I Credits: 4

4∙ Details of Lab/Practical/Experiments/Tutorials syllabus:

List of practical Experiments:

2. Qualitative identification of amino acids-histidine, tyrosine, tryptophan, cysteine, arginine.

3. Qualitative identification of lipids- solubility, saponification, acrolein test, Salkowski test,

4. Preparation of Osazones and their identification.

5. Absorption maxima of colored substances-p-Nitrophenol, Methyl orange.

12. Recommended Co-curricular activities:(Co-curricular Activities should not promote copying

1. Recommended Co-curricular activities: (Co-curricular Activities should not promote copying

B.Sc. Semester - III Credits: 4

Learning outcomes of Course

UNIT II: 12 hours

UNIT III: 12 hours

UNIT IV: 12 hours

B.Sc. Semester - III Credits: 1

1. Details of Lab/Practical/Experiments/Tutorials syllabus:

2. Recommended Co-curricular activities: (Co-curricular Activities should not promote copying

B.Sc. Semester - IV Credits: 4

UNIT II: 12hours

Unit III: 12 hours

UNIT IV: 12hours

Details of Lab/Practical/Experiments/Tutorials syllabus:

List of practical Experiments:

1.Estimation of calcium by titrimetry

7. Recommended Co-curricular activities: (Co-curricular Activities should not promote copying

Details of Lab/Practical/Experiments/Tutorials syllabus:

1. Recommended Co-curricular activities:(Co-curricular Activities should not promote copying

BLUE PRINT FOR MODEL QUESTION COURSE - THEORY

Time: 3 hours Max marks: 75M

9.a) from unit 1

11.a) from unit II

12.a) from unit III

13.a) from unit IV

14.a) from unit V

BLUE PRINT FOR MODEL PRACTICAL COURSE