Courses offered during Ist Semester

Course No.	Course Title	Credit hours
Biochem. 101	Introduction to Biochemistry	2+1
Biochem. 102	Nutritional Biochemistry-I	2+1
Biochem. 209	Introduction to Intermediary Metabolism 3+0 Sem. I	3+0
Biochem. 301	Introduction to Molecular Biochemistry 3+0 Sem. I	3+0
Biochem. 303	Introduction to Membrane Biochemistry 3+0 Sem. I	3+0
Biochem. 304	Enzymology and Enzyme Technologies	2+1
Biochem. 421	Fundamentals of Biochemistry 3+0 Sem. I	3+0
Biochem. 423	Fundamentals of Molecular Biochemistr	2+0
Biochem. 425	Fundamentals of Plant Biochemistry	2+0
Biochem.-501*	Basic Biochemistry	3+1
Biochem.-503*	Enzymology	2+1
Biochem.-505*	Techniques in Biochemistry	2+2
Biochem.-507*	Plant Biochemistry	2+1
Biochem.-509	Nutritional Biochemistry	2+1
Biochem.-511	Biochemistry on Xenobiotics	2+0
Biochem.-601	Advanced Enzymology	2+1
Biochem.-603	Biochemistry of Biotic and Abiotic stresses	3+0
Biochem.-607	Applications of techniques in Biochemistry	1+2
Biochem.-591	Master’s Seminar	1+0

*Core Courses/Compulsory Courses                                       Courses offered during 2ndSemester

Course No.	Course Title	Credit hours
Biochem. 103	Nutritional Biochemistry-II	3+0
Biochem. 104	Principles of Biochemistry	2+1
Biochem. 203	Structure and Function of Biomolecules	3+0
Biochem. 206	General Enzymology	2+0
Biochem. 207	Basic Biochemistry	3+1
Biochem. 208	Food Biochemistry and Nutrition	2+1
Biochem. 302	Basic Experiments in Biochemistry	0+3
Biochem. 424	Experiments in Biochemistry	0+3
Biochem. 426	Fundamentals of Animal Biochemistry	3+0
Biochem. 429	Biochemical and Biophysical Techniques	3+0
Biochem. 430	Fundamentals of Enzymology	3+0
Biochem. 431	Fundamentals of Membrane Biochemistry	2+0
Biochem. 432	Clinical Biochemistry	2+1
Biochem.-502*	Intermediary Metabolism	3+0
Biochem.-504	Molecular Biology	2+1
Biochem.-506	Immunochemistry	2+1
Biochem.-508	Animal Biochemistry	3+0
Biochem.-510	Nitrogen and Sulphur Metabolism	2+1
Biochem.-602	Advanced Molecular biology	3+0
Biochem.-591	Master’s Seminar	1+0

*Core Courses/Compulsory Courses

Course contents of the courses offered during Ist Semester

Biochem. 101 Introduction to Biochemistry (2+1) Sem. I Importance of Biochemistry. Properties of Water, pH and Buffer. Carbohydrate: Importance and classification. Structures of Monosaccharides, Reducing and oxidizing properties of Monosaccharides, Mutarotation; Structure of Disaccharides and Polysaccharides. Lipid: Importance and classification; Structures and properties of fatty acids; storage lipids and membrane lipids. Proteins: Importance of proteins and classification; Structures, titration and zwitterions nature of amino acids; Structural organization of proteins. Enzymes: General properties; Classification; Mechanism of action; Michaelis & Menten and Line Weaver Burk equation & plots; Introduction to allosteric enzymes. Nucleic acids: Importance and classification; Structure of Nucleotides, A, B & Z DNA; RNA: Types and Secondary & Tertiary structure. Metabolism of carbohydrates: Glycolysis, TCA cycle, Glyoxylate cycle, Electron transport chain. Metabolism of lipids: Beta oxidation, Biosynthesis of fatty acids. Practical: Preparation of solution, pH & buffers, Qualitative tests of carbohydrates and amino acids. Quantitative estimation of glucose/ proteins. Titration methods for estimation of amino acids/lipids/ Free fatty acids, Effect of pH, temperature and substrate concentration on enzyme action, Paper chromatography/ TLC demonstration for separation of amino acids/ Monosaccharides.

Biochem. 102 Nutritional Biochemistry-I (2+1) Sem. I Introduction to biochemistry – Definition, objectives, scope and inter relationship between biochemistry and other biological sciences.  Enzymes – Definition, types and classification of enzymes, definition and types of coenzymes, specificity of enzymes, isozymes, enzyme kinetics including factors affecting enzyme action, velocity of enzyme catalyzed reactions, enzyme inhibition. Intermediary metabolism. Carbohydrate metabolism- glycolysis, TCA cycle and energy generation, gluconeogenesis, glycogenesis, glycogenolysis, blood sugar regulation.  Lipid metabolism – oxidation and biosynthesis of fatty acids (saturated and mono-unsaturated), synthesis and utilization of ketone bodies, ketosis, fatty liver.  Protein metabolism – general reactions of amino acid metabolism, urea cycle, lipoproteins – types, composition, role and significance in disease. Practical: Handling of equipment and instruments, preparation of samples, solutions and buffers, blood constituents: Estimation of serum protein (Biuret method and Lowry method), blood glucose (Folin Wu method), serum inorganic phosphorus (Fiske and SubbaRow method), creatinine, Urine constituents: Estimation of protein levels, glucose levels in urine, ketone bodies in urine, urine constituents- Repeat.

Biochem. 209 Introduction to Intermediary Metabolism (3+0) Sem. I Bioenergetics: High energy compounds, chemical potential, electrochemical potential, electron transport chain and oxidative phosphorylation. Metabolism of carbohydrates: glycolysis, gluconeogenesis, tricarboxylic acid cycle, pentose phosphate pathway. Glycogen metabolism. Glyoxylate pathway. Oxidation of fatty acids. Biosynthesis of fatty acids. Cholesterol, phospholipid, and triglyceride metabolism. General reactions of amino acids – transamination, deamination and decarboxylation and urea cycle. Biosynthesis and degradation of purine and pyrimidine nucleotides. Biosynthesis of deoxyribonucleotides. Common diseases of metabolism.

Biochem. 301 Introduction to Molecular Biochemistry (3+0) Sem. I Introduction; Structure of DNA (A, B and Z) and RNA, DNA replication: semi-conservative mode of replication and its experimental verification. Enzymes involved in DNA replication. Differences between prokaryotic and eukaryotic replication. RNA biosynthesis: Initiation, elongation and termination, reverse transcriptase. Genetic code: Elucidation and general features.  Protein synthesis, enzymes involved in translation. Post-transcriptional processes. Introduction to operon concept (lac-operon) and regulation of gene expression.

Biochem. 303 Introduction to Membrane Biochemistry (3+0) Sem. I Chemical composition of biomembranes. Role of phospholipids and proteins, models of cell membranes. Functions of membranes: energy transduction, signal recognition and transduction. Nutrient transport across membranes. Active and passive transport. Pumps: examples and metabolic significance. Bacteriorhodopsin. Membrane fluidity and receptor functions.

Biochem. 304 Enzymology and Enzyme Technologies (2+1) Sem. I Classification and nomenclature of enzymes. General characteristics of enzymes. Active site. Cofactors and prosthetic groups. Metalloenzymes. Isolation, purification, characterization and assays of enzyme and international units. Criteria for purity. Enzyme kinetics- effect of pH, temperature, enzyme and substrate concentration. Determination of Km and Vmax. Regulation of enzyme activity. Enzyme inhibition- competitive, non-competitive and uncompetitive. Isoenzymes, schizomers and isoschizomers. Ribozymes, Immobilization of enzymes. Applications of enzymes in biotechnology, industry, environment, agriculture, food and medicine. Practical: Isolation, purification and assay of enzymes. Determination of optimum pH and optimum temperature of enzymes. Thermostability of enzymes. Activators and inhibitors of enzyme catalysis. Determination of kinetic parameters of enzymes. Immobilization of enzymes. Isoenzymes analysis.

Biochem. 421 Fundamentals of Biochemistry (3+0) Sem. I Cell structure and function. Structure and role of water in biological system. Acids, bases and buffers of living systems. The pK of biomolecules. Classification of enzymes. Effect of substrate, temperature, pH, activators and inhibitors on enzyme catalysis. Vitamins and hormones. Bio- membranes structure and function. Bioenergetics and oxidative phosphorylation. Metabolism of carbohydrates, lipids, proteins, nucleic acids. Photosynthesis and respiration. DNA replication, transcription and translation. Regulation of transcription. Recombinant DNA technology. Secondary plant products.

Biochem. 423 Fundamentals of Molecular Biochemistry (2+0) Sem. I Introduction. Structure and functions of nucleic acids. Nucleic acids as genetic material. DNA sequencing. DNA replication, mutations and repair mechanism. Transcription and post transcriptional modifications. Genetics code. Protein biosynthesis. Protein targeting. Regulation of gene expression at the level of transcription. Recombinant DNA and concepts of biotechnology.

Biochem. 425 Fundamentals of Plant Biochemistry (2+0) Sem. I Structure and function of cell wall and cell organelles. Photosynthesis and photorespiration. Sucrose transport. Biosynthesis of structural and storage carbohydrates, proteins and lipids. Biochemistry of seed development. Biological nitrogen fixation. Nitrogen and sulfur metabolism. Secondary plant products and their role. Growth regulators. Biochemistry of biotic and abiotic stresses. Carbohydrate and lipid metabolism during germination.

Biochem.-501* Basic Biochemistry  (3+1) Sem. I Unit I Biochemistry as modern science and its various divisions, Scope, and importance of Biochemistry in agriculture and allied sciences. Unit II Fundamental principles governing life, supramolecular structures, significance of weak non-covalent interactions in biology. Unit III Structure of water, ionization of water, acid base concept, pH and buffers, significance of structure-function relationship. Unit IV General introduction to physical techniques for determination of structure of biopolymers. Unit V Structure, classification, properties and function of carbohydrates, amino acids, proteins, lipids and nucleic acids. Unit VI Structure, formation and different forms of immunoglobulins, PR proteins and their classification. Unit VII Structure, classification, and function of plant secondary metabolites. Unit VIII Structure and biological functions of vitamins and coenzymes, enzymes: classification and mechanism of action; regulation, factors affecting enzyme action. Hormones: animal and plants. Unit IX Fundamentals of thermodynamic principles applicable to biological processes, Bioenergetics. Unit X Important and basic degradative metabolic pathways of carbohydrates, lipids and proteins and their regulation. Unit XI Formation of ATP, substrate level phosphorylation, electron transport chain and oxidative phosphorylation, chemiosmotic theory and proton motive force. Unit XII Overview of replication, transcription, and translation. Unit XIII Restriction enzymes, DNA cloning, applications of cloning, transgenics. Practical Preparation of standard and buffer solutions. Detection of carbohydrates, amino acids and proteins. Extraction and estimation of sugars. Extraction and estimation of amino acids. Extraction and estimation of proteins. Estimation of acid value of fat/oil. Estimation of peroxide value of fat/oil. Estimation of saponification value in fats and oils. Fatty acid composition in fat/oil by GC. Estimation of DNA and RNA by spectroscopic methods. Estimation of Ascorbic acid. Separation of biomolecules by TLC and Paper chromatography. Estimation of alpha amylase activity. Qualitative tests for secondary plant metabolites

Biochem.-503* Enzymology (2+1) Sem. I Unit I Historic perspective, general properties of enzymes, enzyme compartmentalization in cell organelles, nomenclature and classification of enzymes, ribozymes, isozymes, abzymes. Unit II Extraction of soluble and membrane-bound enzymes, purification of enzymes, measurement of enzyme activity. Unit III Enzyme specificity, monomeric and oligomeric enzymes, catalytic mechanism, mechanism of enzyme action, pseudoenzymes, enzyme promiscuity. Unit IV Chemical nature and involvement of cofactors and coenzymes in enzyme catalyzed reactions, metal activated enzymes and metalloenzymes, mechanism of enzyme catalyzed reactions without cofactors. Unit V Active site, identification of binding sites and catalytic sites. Unit VI Relationship between initial velocity and substrate concentration, Michaelis-Menten equation, Lineweaver-Burk and Eadie-Hofstee plots, analysis of kinetic data, numerical exercises. Unit VII Reversible and irreversible enzyme inhibition, uses of enzyme inhibition. Unit VIII Nature of allosteric enzymes, sigmoidal kinetics, MWC model and allosteric regulation, KNF model and allosteric regulation. Unit IX Feedback regulation, regulatory enzymes, control of enzymatic activity, symmetry and sequential model, reversible covalent modification of enzymes. Unit X Industrial application of enzyme catalysis in sectors like food processing, detergents, biofuels, paper and pulp, biosensors, and clinical applications of enzymes. Unit XI Large scale production and purification of enzymes, immobilization of enzyme. Practical Soluble protein estimation. Enzyme assay by taking any model enzyme. Isolation and purification of any model enzyme. Study of the effect of enzyme and substrate concentrations on enzyme activity. Determination of Km and Vmax. Determination of pH and temperature optima. Effect of inhibitors on enzyme activity. Determination of pH and temperature stability of enzyme. Electrophoretic analysis of isozymes.

Biochem.-505* Techniques in Biochemistry (2+2) Sem. I  Unit I Principles and applications of paper, thin layer, gel filtration, ion-exchange, affinity, column & HPTLC, GC, HPLC and FPLC. Unit II General principles, paper, and gel electrophoresis, native and SDS-PAGE, 2D-PAGE, capillary electrophoresis. Unit III Hydrodynamic methods of separation of biomolecules such as viscosity and sedimentation velocity, – their principles. Unit IV Basic principles of sedimentation, type, care, and safety aspects of centrifuge preparative and analytical centrifugation. Unit V Principles and applications of UV-visible, Fluorescence, IR and FTIR, Raman, NMR and FTNMR, ESR and X-Ray spectroscopy. Unit VI MS/MS, LC-MS, GC-MS, MALDI-TOF, applications of mass spectrometry in biochemistry. Unit VII Principle, function and instrumentation of atomic absorption spectrophotometry. Unit VIII Principles and applications, light, UV, phase contrast, fluorescence, and electron microscopy, flow cytometry. Unit IX Tracer techniques in biology: concept of radioactivity, radioactivity counting methods with principles of different types of counters, concept of α, β and γ emitters, scintillation counters, γ-ray spectrometers, autoradiography, applications of radioactive tracers in biology. Unit X Principles and applications of phosphor imager, MRI, and CT scan. Unit XI Production of antibodies, immunoprecipitation, immunoblotting, immunoassays, RIA and ELISA. Unit XII Cryopreservation, polymerase chain reaction (PCR), FACS. Practical Expression of concentration in terms of dilution, molarity, normality, percent expression. pH measurement and buffer preparation. Determination of absorption maxima of biomolecules. Estimation of biomolecules through spectrophotometry and other methods. Separation of carbohydrates and amino acids by paper chromatography. Separation and analysis of fatty acids/lipids by GC. Separation/estimation of biomolecules through HPLC and FPLC. Separation of proteins using ion exchange, gel filtration and affinity chromatography. Electrophoretic separation of proteins and nucleic acids. Centrifugation- differential and density gradient. (NH4)2SO4 precipitation and dialysis. Use of radioisotopes in metabolic studies. PCR. ELISA. Western blotting/ Dot blotting

Biochem.-507* Plant Biochemistry (2+1) Sem. I  Unit I Structure and function of plant cell and its organelles, phytochromes, chloroplast morphology structure, structure and chemistry of photosynthetic pigments, light reaction of photosynthesis. Unit II Carbon reduction inC3, C4 and CAM plants, photorespiration, sucrose-starch interconversion. Unit III Biosynthesis of structural carbohydrates, storage proteins and lipids. Unit IV Basic concepts of nitrogen and sulphur metabolism: biological nitrogen fixation, nitrate assimilation in plants, sulphur chemistry and function, reductive sulphate assimilation pathway, sulphated compounds. Unit V Biochemistry of seed germination– stages, requirements, metabolism, and mobilization of storage material; Biochemistry of fruit ripening – ripening process, cell wall degrading enzymes, role of ethylene and regulation of ethylene production. Unit VI Different classes of phytohormones, their biosynthesis and mode of action. Unit VII Biochemistry and significance of plant secondary metabolites – phenolics, terpenoids, alkaloids, cyanogenic glycosides and glucosinolates, effect of biotic and abiotic factors on plant metabolism and plant defense system. Practical Fractionation of cell organelles. Estimation of starch. Assay of ADPG pyrophosphorylase/starch synthase. Assay of PAL/SOD. Assay of PPO/LOX. Estimation of individual amino acids. Qualitative tests of secondary metabolites (alkaloids, sterols etc.). Content and composition of carotenoids, anthocyanin, and chlorophylls. Determination of polyphenols/phenolics. Fractionation of storage proteins. Estimation of glucosinolates. Estimation of cyanogenic compounds

Biochem.-509  Nutritional Biochemistry (2+1) Sem. I Unit I Fundamentals of human nutrition, concept of balanced diet, biochemical composition, energy, and food value of various food grains (including cereals, pulses, oilseeds), fruits and vegetables. Physico-chemical, functional, and nutritional characteristics of carbohydrates, proteins and fats and their interactions (emulsions, gelation, browning etc.). Digestion and absorption, digestive secretions, their characteristic features and control, protection of microflora of the GI tract. Unit II Biochemical functions of nutrients, macro- and micronutrients- carbohydrates, fats and proteins, vitamins, water soluble and fat-soluble vitamins, mineral, and phytonutrients, prebiotics and probiotics, enzymes and metabolic protein factors, cofactor role, electrolytic function, constituents of skeletal tissues, interrelationship in nutrient functions, mineral deficiency diseases; nutraceuticals, antinutritional factors, biochemistry of postharvest storage. Unit III Factors affecting bioavailability of nutrients, biological value of proteins; effect of cooking, processing, and preservation of different food products on nutrients, energy- and micronutrient malnutrition, deficiency diseases of macro and micronutrients. Unit IV Food sensitivity: immunologically mediated food sensitivity, nature, and properties of antigens in foods, mechanism of induction of all allergic reactions, diagnostic tests for food, hypersensitivity, non-immunologically mediated food sensitivity, food sensitivity due to metabolic diseases, gastrointestinal diseases, food additives, pharmacologic agents, food toxins and poisonous and psychological factors. Practical Estimation of amylose and amylopectin. Estimation of resistant starch. Estimation of ω3, ω6 and trans fatty acid. Estimation of phenols in plant tissue/sample. Estimation of carotenoids. Estimation of amylase, trypsin, and chymotrypsin inhibitor activities. Estimation of Vitamin C in fruits. Estimation of reducing & non reducing sugar in fruits. Estimation of protein contents. Estimation of dietary fibre. Determination of limiting amino acids. Estimation of phytate/ oxalate. Estimation of total antioxidant activity by different methods. Estimation of curcumin.

Biochem.-511 Biochemistry on Xenobiotics (2+0) Sem. I Unit I  Xenobiotics: classification and their effects on biological systems, Problems related to xenobiotics degradation, potential effects of toxic agents on immune system function, biotic metabolism of xenobiotics – biodegradation/biotransformation. Unit II Mode of degradation – Enzymatic and Non-enzymatic, Metabolism of toxic compounds with reference to role of detoxifying enzymes, Mechanism of xenobiotics detoxification – in animal using the enzymes of Phase I and Phase II, Role of microbes in xenobiotics degradation and co-metabolism, Biodegradation and its genetics, manipulation of xenobiotic degradative genes. Unit III Plant metabolism of xenobiotics – transformation, conjugation, and compartmentation, Metabolic responses of pesticides in plants, Impact, metabolism, and toxicity of heavy metals in plants, Regulation of xenobiotics in higher plants: signalling and detoxification. Unit IV Phytoremediation, Advances in development of transgenic plants for remediation of xenobiotic pollutants, safety assessment of xenobiotics.

Biochem.-601 Advanced Enzymology (2+1) Sem. I Unit I Theory of enzymatic catalysis, Specificity and editing mechanisms, concept of active site and enzyme substrate complex, active site mapping, factors associated with catalytic efficiency, mechanism of enzyme reactions, detection of intermediates in enzymatic reactions. Unit II Transition state theory, Arrhenius equation, Determination of energy of activation, effect of pH and temperature on enzyme kinetics, pre-steady state and steady state kinetics, single substrate kinetics, allosteric enzymes and mixed inhibition, substrate and product inhibition, numerical exercises. Unit III Mechanism determination by radioisotope exchange, role of enzymes in regulation of metabolism, bifunctional enzymes, pseudoenzyme and enzyme promiscuity, extremozymes, catalytic nucleic acids (ribozymes, catalytic DNA). Unit IV Advantages and disadvantages of biocatalysis in technology driven processes, stabilization and regeneration of enzyme systems used in biotechnology, protein engineering of enzymes, creation of chimeric, bifunctional, immobilization of enzymes, semisynthetic enzymes and their use as industrial biocatalysts, and their practical significance, modern information technologies in enzyme engineering. Practical Purification and characterization of some model enzymes (peroxidise, α-amylase, lipase). Study kinetics of inhibited and uninhibited enzyme catalysed reactions. Determination of Km values of single substrate reactions. Determination of enzyme activity by coupled assay. Electrophoretic separation of isozymes. Enzyme immobilization.

Biochem.-603  Biochemistry of Biotic and Abiotic stresses (3+0) Sem. I Unit I Molecular mechanisms of fungal and bacterial infection in plants; changes in metabolism, cell wall composition and vascular transport in diseased plants. Unit II Role of secondary metabolites, Plant defence response, antimicrobial molecules; genes for resistance, hypersensitive response and cell death; systemic and acquired resistance, pathogen derived resistance. Unit III Plant viruses, host-virus interactions, disease induction, virus movement, and host range determination; viroids. Unit IV Biochemical basis of abiotic stresses namely osmotic (drought, salinity), temperature, heavy metals, air and water pollutants, synthesis and functions of proline and glycine betaine in stress tolerance interaction between biotic and abiotic stresses; stress adaptation. Unit V Reactive oxygen species and biotic and abiotic stress, antioxidants, enzymes of defense system. Role of calcium, nitric oxide, and salicylic acid in plant development. Molecular strategies for imparting tolerance against biotic and abiotic stress

Biochem.-607  Applications of techniques in Biochemistry (1+2) Sem. I Unit I Isolation and purification of important metabolites from microbial/plant/animal source, Applications of paper, thin layer and gas liquid chromatography, PAGE, FPLC and HPLC in the separation of biomolecules. Determination of molecular weight of protein using PAGE/ gel filtration method. Unit II Electrophoretic separation of protein, Experiments on DNA: Isolation, agarose gel electrophoresis and restriction analysis of DNA. Techniques in DNA-protein and protein-protein interaction. Unit III Isolation of chloroplast and mitochondria by differential centrifugation and their purification by density gradient centrifugation. Unit IV Isolation, purification, and characterization of enzymes, isozymic analysis and enzyme immobilization. Unit V Application of PCR, yeast 2 hybrid system, Antigen-Antibody interaction, ELISA, Chromatin immunoprecipitation, gel based and gel free proteasome tools. Practical Isolation and purification of important metabolites from microbial/plant/animal source. Paper chromatography and thin layer chromatography. gas liquid chromatography. PAGE. FPLC and HPLC. Determination of molecular weight of protein using PAGE/ gel filtration method. Electrophoretic separation of protein. Isolation, agarose gel electrophoresis and restriction analysis of DNA. Techniques in DNA-protein and protein-protein interaction. Isolation of chloroplast and mitochondria by differential centrifugation and their purification by density gradient centrifugation. Isolation, purification, and characterization of enzymes. isozymic analysis. enzyme Immobilization. PCR. yeast 2 hybrid system. Antigen-Antibody interaction. ELISA. Chromatin immunoprecipitation. Gel based and gel free proteasome tools.

Biochem.-591 (1+0) Master’s Seminar

Course contents of the courses offered during 2nd Semester

Biochem. 103 Nutritional Biochemistry-II   (3+0) Sem. II Role of major biomolecules in nutrition. Introduction to nucleic acids-DNA, RNA and their structure, replication, transcription, genetic code and biosynthesis of proteins. Vitamins -chemistry and biochemical role of fat-soluble vitamins – A, D, E and K, water soluble vitamins – B1, B2, B6, niacin and vitamin C.  Biochemical role of minerals in nutrition- macrominerals- calcium, iron, magnesium, sodium, potassium, chloride, phosphorus and sulphur, microminerals – iodine, zinc, copper, chromium, selenium, cobalt, fluoride and manganese. Anti-nutrients and antioxidants in human health. Digestion and absorption of carbohydrates, lipids, proteins, vitamins and iron. Bile acid metabolism. Molecular aspects of transport, passive diffusion, facilitated diffusion, active transport of sugars and amino acids.  Basal metabolism and caloric requirements. Balanced diet.  Metabolic disorders of macromolecules- glycogen storage diseases, lipidosis, dyslipidemias and atherosclerosis.  Evaluation of protein quality by chemical and biological methods. Protein energy malnutrition- marasmus and kwashiorkor and their management.  

Biochem. 104   Principles of Biochemistry (2+1) Sem. II Recapitulation of basic chemistry and biology. Water. pH and buffers. Acid-base balance. Cellular constituents and their structure and function- amino acid and proteins, carbohydrates, lipids and bio-membranes, nucleic acids. Dissolved molecules– vitamins and minerals. Enzymes-function, properties and mechanism. Metabolism of cellular constituents- basic concepts of bioenergetics. Carbohydrate metabolism-glycolysis and glycogenolysis, HMP pathway, TCA cycle and gluconeogenesis. Electron transport chain. Photosynthesis. Lipid metabolism-β-oxidation, ketone bodies, fatty acid synthesis.  Amino acid metabolism – general reactions of nitrogen assimilation and excretion. Biosynthesis of DNA, RNA and protein- replication, transcription, translation and genetic code. Regulation of gene expression.  Practical: Preparation of buffers and pH determination. Preparation of colloids. Qualitative and quantitative tests of carbohydrates, lipids and proteins. Tests of enzyme action- potato oxidase, urease, salivary amylase. Paper chromatography of amino acids or carbohydrates ascending and descending. Determination of starch and sugar. Analysis of proximate constituents in food.

Biochem. 203 Structure and Function of Biomolecules (3+0) Sem. II Development and scope of Biochemistry. Biochemical composition of living organisms. Water as a solvent of life. Buffers and Henderson-Hasselbalch equation. Structure and functions of simple and complex carbohydrates. Lipids: classification, structure and functions; Proteins: structures of amino acids, concept of peptide bond, levels of protein structure and protein functions. Nucleic acid: nucleoside, nucleotides, structure of DNA and RNA and their functions. Vitamins and coenzymes.

Biochem. 206 General Enzymology (2+0) Sem. II Classification and nomenclature of enzymes. General characteristics of enzymes. Active site, cofactors, prosthetic groups; metallo-enzymes. Enzyme assays and international units. Enzyme kinetics: significance of Km and Vmax and their determination using Lineweaver-Burk plots. Enzyme inhibition: Reversible and irreversible, competitive, non-competitive and uncompetitive with graphical representations. Brief mention of allosteric enzymes and isoenzymes. Biotechnological and clinical applications of enzymes.

Biochem. 207   Basic Biochemistry (3+1) Sem. II Introduction and importance. Cell structure. Bio molecules – structure, functions and properties of carbohydrates, lipids, proteins and nucleic acids.  Enzymes – classification and factors affecting activity.  Structure and role of water in biological system. Acids, bases and buffers of living systems. The pK of biomolecules.  Vitamins- chemistry, classification, biochemical role and deficiency diseases. Hormones – classification, general mode of action and role in metabolism. Bioenergetics. Metabolism – basic concept, Glycolysis, Citric acid cycle, Pentose phosphate pathway, Oxidative phosphorylation, Fatty acid oxidation. General reactions of amino acid degradation-transamination, deamination, decarboxylation and urea cycle. Biosynthesis – carbohydrates, lipids, proteins and nucleic acids. Secondary metabolites – terpenoids, alkaloids, phenolics and their applications in food and pharmaceutical industries. Practical: Qualitative tests for carbohydrates, amino acids, proteins and lipids. Extraction and characterization of lipids by thin layer chromatography. Determination of acid, iodine and saponification values of oil. Extraction, quantitative estimation and separation of sugars by paper chromatography.  Determination of phenols. Determination of free amino acids and proteins.

Biochem. 208      Food Biochemistry and Nutrition (2+1) Sem. II Biochemistry and its scope. Occurrence, classification, structures, physicochemical and metabolic functions of carbohydrates, proteins and lipids. Nucleic acids – properties, structure and metabolism.  Enzymes – chemical nature, nomenclature, classification, sources and properties, mechanism of action, coenzyme and prosthetic groups, regulation of enzymatic activity, enzyme kinetics, inhibition, effects of pH, allosteric enzymes, derivation of Michaelis‐Menten equation. Concepts and content of nutrition – water and energy balance, water intake and losses, basal metabolism. Formulation of diets – classification and preparation of balanced diet, recommended dietary allowances for various age groups. Malnutrition – assessment of nutritional status, food fad and faddism. Potentially toxic substance in human food. Basic food groups and nutrients supplied by food. Digestion, absorption, assimilation and transport of carbohydrates, proteins and fats in human beings. Metabolism of carbohydrates – glycolysis and respiration, production of ATP, brief description of electron transport chain, oxidative and substrate phosphorylation. Metabolism of Lipids- β‐oxidation of fatty acids, ketosis, fatty acid synthesis. Metabolism of proteins- breakdown of proteins, transamination, deamination, decarboxylation and urea cycle. Minerals – functions, sources and effects of deficiency. Factors affecting absorption of minerals, promoters and inhibitors. Vitamins and hormones – classification, functions, sources and effects of deficiency. Fat soluble and water-soluble vitamins. Physico-chemical and nutritional changes during food processing – drying and dehydration, irradiation, freezing, fermentation, canning, restoration, enrichment, fortification and supplementation of foods. Practical:  Preparation of various solutions and buffers. Qualitative and quantitative determination of carbohydrates, amino acids, proteins and lipids. Isolation of enzymes from various sources.  Determination of pKa of acid and pI for casein. Separation of amino acids using paper chromatography, thin layer chromatography and electrophoresis. Estimation of phosphorus, calcium and iron in food samples. Estimation of β-carotene using column chromatography.  Vitamins -Estimation of ascorbic acid using dye method. Effects of acids and alkali on pigments.

Biochem. 302 Basic Experiments in Biochemistry (0+3) Sem. II Practical: Qualitative tests for carbohydrates, lipids, proteins and amino acids. Determination of acid, iodine and saponification values of fats and oils. Extraction of total lipids and total sugars. Estimation of total sugars, reducing sugars and starch. Starch hydrolysis by amylase. Preparation of buffers. Determination of acid phosphatase from mungbean. Separation of sugars by paper chromatography and lipids by thin layer chromatography.

Biochem. 424 Experiments in Biochemistry (0+3) Sem. II Practical: Concepts of pH and buffers. Determination of total sugars, reducing and non-reducing sugars, starch, free fatty acids, cholesterol and phospholipids. Determination of free amino acids and proteins. Separation of sugars by paper chromatography. Extraction of lipids, separation of polar and non-polar lipids by TLC. Fatty acid composition by GLC. Estimation of Vitamin C and tocopherols. Isolation and purification of acid phosphatase. Estimation of chlorophyll, carotenoids and phytic acid. Extraction and estimation of nucleic acids.

Biochem. 426 Fundamentals of Animal Biochemistry (3+0) Sem. II Composition and secretion of digestive juices. Digestion and absorption of lipids, proteins, carbohydrates and nucleic acids. Role of lipoproteins in transport of lipids. Acid base balance in kidney and lung functions. Composition of blood and blood clotting. Metabolism and functions of hemoglobin. Biochemistry of specialized tissues like muscles, eyes, nerves and connective tissues. Hormones and their mechanism of action. Role of thyroid, pituitary and calcium metabolizing hormones. Detoxification of xenobiotics. Introduction to immune system and immune cells. Antibodies: classes and functions. Antigen-antibody interactions. Production of monoclonal and polyclonal antibodies.

Biochem. 429 Biochemical and Biophysical Techniques (3+0) Sem. II Separation techniques like salt and organic solvent fractionation; dialysis, osmosis and ultra-filtration. Chromatographic techniques- partition, adsorption, ion exchange, thin layer, molecular sieve, affinity, high pressure liquid chromatography and GLC. Electrophoresis and isoelectric focusing. X-ray diffraction, ORD and circular dichroism and their application. Lyophilization. Centrifugation techniques: basic principles of sedimentation; centrifuges of various types; Rotors: differential centrifugation, density gradient centrifugation, applications of the analytical ultracentrifuge. Instrumentation methods-IR, UV and visible spectrophotometry, spectrofluorimetry, ESR, NMR spectroscopy. Atomic spectroscopy, Radioactive counters. Radioisotopes in biology: Applications and precautions.

Biochem. 430 Fundamentals of Enzymology (3+0) Sem. II Introduction to enzymes. Naming and classification of enzymes. Enzymes specificity, cofactors, coenzymes and prosthetic groups. Isozymes, nature of active site, concept of pKa of amino acids. Identification of functional groups of active site. Factors responsible for catalytic efficiency of enzymes. Concept of initial velocity, enzyme units, specific activity, Michaelis-Menten equation, concept of Km and Vmax. Enzyme inhibition and activation, bi-substrate reactions, regulation of enzyme activity. Allosteric enzymes. Enzyme isolation and purification. Enzyme immobilization. Biotechnological applications of enzymes.

Biochem. 431 Fundamentals of Membrane Biochemistry (2+0) Sem. II Membrane composition and functions. Various models of unit membrane structure. Comparison of membranes of cells and organelles. Distribution of membrane compounds and their role in organization of membrane and cellular recognition. Membrane transport mechanisms. Membrane channels and pumps. Gap junctions and tight junctions. Transport of different nutrients. Membrane mediated processes and membrane receptors. Signal recognition and transduction.

Biochem. 432 Clinical Biochemistry (2+1) Sem. II Role of Biochemistry in diagnosis of diseases. Composition of blood: serum, plasma proteins, RBC, WBC, and platelets. Disorders of carbohydrate metabolism; glucose level in normal blood, renal threshold, hyper and hypoglycemia, qualitative tests for sugars in diagnosis of diabetes mellitus. Glycogen storage diseases. Disorders of amino acid metabolism: phenyl alanemia, homocystinuria, tyrosinemia, maple syrup urine disease, alkaptonuria and aminoacidurias. Disorders of lipid metabolism: Plasma lipoproteins, cholesterol, phospholipid and triglyceride in health and diseases, ketosis, fatty lever, lipidosis. Disorders of nucleic acid metabolism. Diagnostic enzymes related to GIT, liver and kidney function tests. Hemoglobin metabolism, hemoglobinopathies, thalessmia, anemias and porphyrias. Disorders of mineral metabolism. Hormonal disturbances: steroid and protein hormone, thyroid function.  Practical: Separation of serum and plasma from blood, Estimation of hemoglobin blood sugar, cholesterol, phospholipids and triglycerides, Estimation of calcium, phosphorus, sodium, potassium, urea, uric acid, and creatinine in serum. Assay of aminotransferases (SGOT and SGPT), amylase, phosphatases, and lipase in serum. Albumin/globulin ratio. Separation of plasma proteins by electrophoresis. ELISA. Thyroid function test: T3 and T4 assay.

Biochem.-502*  Intermediary Metabolism (3+0) Sem. II Unit I The living cell – a unique chemical system, biochemical reaction types, bioenergetics, bioavailability of nutrients, transport mechanism, signal transduction. Unit II Catabolism and anabolism, compartments of metabolic pathways, experimental approaches to study metabolism, metabolic profiles of major organs. Unit III Major catabolic and anabolic pathways of carbohydrate metabolism, the glyoxylate pathway. Unit IV Fatty acid oxidation, ketone bodies, fatty acid biosynthesis, synthesis of triacylglycerols, cholesterol, eicosanoids. Unit V General reactions of amino acid metabolism, degradative and biosynthetic pathways of amino acids, urea cycle, amino acids as metabolic precursors. Unit VI Mechanisms of energy transduction, electron transport system, oxidative phosphorylation, control of ATP production. Unit VII Sulphate reduction and incorporation of sulphur into amino acids. Unit VIII Synthesis and degradation of purine and pyrimidine nucleotides.  Unit IX Regulation of carbohydrate, lipid, protein, nucleotide metabolism and oxidative phosphorylation. Unit X Disorders of carbohydrates, lipids, amino acids, and nucleic acid metabolism, and inborn errors of metabolism. Metabolic pathway engineering. Biochem.-504  Molecular Biology (2+1) Sem. II Unit I Historical development of molecular biology, nucleic acids as genetic material. Unit II Nucleic acid structure, chemical and physical properties of nucleic acids, spectroscopic and thermal properties of nucleic acids, DNA supercoiling. Unit III Concept of genes and genome, genome complexity, genome organization in prokaryotes and eukaryotes, chromatin structure and function, repetitive and non-repetitive DNA, satellite, DNA central dogma, genome editing. Unit IV Modes of replication, DNA polymerases, topoisomerases, DNA ligase, model of replisome, semi conservative replication in prokaryotes and eukaryotes, inhibitors of replication, DNA damage and repair. Unit V Basic principles of transcription, transcription initiation, elongation and termination, RNA processing, RNA interference, siRNAs, miRNAs and other ncRNAs, DNA/RNA editing, regulation of transcription, reverse transcription. Unit VI Ribosomes structure and function, organization of ribosomal proteins and RNA genes, genetic code, aminoacyl tRNA synthases. Unit VII Initiation, chain elongation and termination of translation, energetics, inhibitors of translation. Unit VIII Post translational modifications of nascent polypeptide, protein targeting and turnover, regulation of gene expression in prokaryotes and eukaryotes, nucleases, and restriction enzymes. Unit IX Importance, Sanger method, High-Throughput Sequencing (HTS) techniques, applications of DNA sequencing. Unit X Vectors, isolation of genes, recombinants vector, selection of recombinants, characterization and expression of cloned DNA, transformation, transgenesis, mutation, molecular mechanism of mutation, site directed mutagenesis, in vitro mutagenesis. Unit XI Polymerase chain reaction (PCR), expression cloning, gel electrophoresis, molecular markers, macromolecule blotting and probing, arrays (DNA array and protein array) – principles and application. Practical Isolation and purification of DNA and RNA. To check the purity of isolated DNA and RNA. Restriction fragmentation of genomic DNA. Separation of oligos by agarose gel electrophoresis. Southern blotting experiments. Northern blotting experiments. Cloning of DNA fragment in vector. Selection of recombinant. SSR analysis of DNA. cDNA synthesis using RT- PCR. Basic tools in bioinformatics analysis. Biochem.-506 Immunochemistry (2+1) Sem. II Unit I History and scope of immunology, antigens, adjuvants, immune system, organs, tissues and cells, immunoglobulins, molecular organization of immunoglobulin. haptens, Ag-Ab interaction, plant immunity, proteasome mediated process, plantibodies. Unit II Classes of antibodies, antibody diversity, theories of generation of antibody diversity, vaccine, monoclonal and polyclonal antibodies, hybridoma, recombinant antibodies, complement system – classical and alternate. Unit III Cellular interactions in immune response, major histocompatibility complex, cell mediated immune response, cytokines. Unit IV Immunoregulation, immunological tolerance, hypersensitivity, mechanisms of immunity, innate resistance and specific immunity, current immunological techniques– ELISA, RIA, immunoblotting, FACS; basics of PCR and hybridization-based methods of detection, microarray-based detection, multiplexing. Practical Handling, inoculation, and bleeding of laboratory animals. Preparation of antigens and antisera, natural antibodies. Carbon clearance test. Lymphoid organs of the mouse. Morphology of the blood leucocytes. Separation of lymphocytes from blood, viable lymphocyte count. Antigen-antibody interaction. Precipitation and agglutination. Direct and indirect haemagglutination. Immunoelectrophoresis. Complement fixation. Quantitation of immunoglobulins by zinc sulphate turbidity and single radial immunodiffusion. ELISA. Western blotting. Fluorescent Ab test. Hybridoma technique. Biochem.-508  Animal Biochemistry (3+0) Sem. II Unit I Digestion and absorption of food, Detoxification, biochemistry of specialized tissues –connective tissue, skin, muscle, nervous tissue and blood and other body fluids. Unit II Water, electrolyte and acid-base balance, structure, function, and mechanism of major trace elements, vitamins, energy nutrients and biochemistry of respiration, bioactive peptides, and functional oligosaccharides. Unit III Hormones of thyroid, hypothalamus, pituitary, pancreas, adrenals, and sex hormones, Membrane receptors of hormones, signal transduction.  Unit IV Immune systems, immunoglobulins, monoclonal antibodies, formation of antibody, antibody diversity, complement system – classical and alternate, major histocompatibility complexes, cell mediated immune response, mechanisms of immunity.

Biochem.-510  Nitrogen and Sulphur Metabolism (2+1) Sem. II Unit I Nitrogen cycle, assimilation of inorganic nitrogen, nitrate uptake and transporters, enzymology of nitrate reduction – Nitrate reductase (NR) and Nitrite reductase (NiR), NR regulation, nitrate signaling. Assimilation of inorganic nitrogen and N-transport amino acids- glutamine synthetase (GS), glutamate synthase (GOGAT), glutamate dehydrogenase (GDH), aspartate amino transferase (AspT) and asparagine synthetase (AS), interaction between carbon metabolism and amino acid synthesis, biosynthesis of amino acids. Nitrogen fixation – an overview, enzymology of nitrogen fixation – nitrogenase, nif genes and their regulation, symbiotic nitrogen fixation – biochemical basis of rhizobial infection, nodule development. Mechanism of creation of microaerobic environment for nitrogen fixation. metabolic exchange between host plant and bacteroids. Unit II Overview of sulfate assimilation, sulfur chemistry and function, sulfate uptake and transport, reductive sulfate assimilation pathway, synthesis and function of sulfur containing amino acids, glutathione and its derivatives, role of sulfated compounds in metabolism. Practical Estimation of nitrite content. Estimation of nitrate content. In vivo assay of nitrate reductase activity. In vitro assay of nitrate reductase activity. In vitro assay of nitrite reductase activity. In vitro assay of glutamine synthetase activity. In vitro assay of glutamate synthase and glutamate dehydrogenase activity. Estimation of ureides and amides. Assay of nitrogenase activity by acetylene reduction method. Estimation of hydrogen evolution by legume nodules. Estimation of cysteine, methionine, pyruvate, and glutathione. Assay of APS activity. Biochem.-602  Advanced Molecular biology (3+0) Sem. II Unit I Genes, their relationship with chromosomes, gene number hypothesis; Genome – definition, variation and organization in plants and animals, structure of organelle genomes; concept of epigenome, genome size and genome evolution. Unit II Prokaryotic and eukaryotic gene regulation, transcriptional and posttranscriptional regulation. regulation at genome level, role of histones, riboswitches. Unit III Genome sequencing technologies, Sanger sequencing, next generation sequencing, nanopore sequencing; genome mapping – genetic map construction, physical mapping. Unit IV Methods of gene isolation and transfer in plants and animals, agrobacterium mediated and direct transfer of genes in plants and animals; gene silencing technologies: virus induced gene silencing, RNA interface; genome editing -TALENs, CRISPR/cas, ZFN and their application, site directed mutagenesis, Application of genetic engineering in different fields, gene therapy.  Unit V Genome browsing, primer design, marker application for breeding, application of MAS in case studies. Bioethics and bio safety guidelines, IPR in recombinant DNA research.

Biochem.-591 Master’s Seminar (1+0)