Unit-1
Bio-technology-an overview
Origin and definition: Old Vs New biotechnology
Scope of importance of biotechnology
Tissue Culture, Gene technology, Medicine, Protein engineering, Metabolic engineering, Agriculture, Industrial Microbiology, Environmental Problems
Biotechnology in India
Bio informatics, Plant molecular biology, Service oriented infrastructural facilities
Training and manpower development, areas of research

Unit-II
Chemical Constituents of life:
A brief Introduction to Chemistry of Biomolecules in the cell.
Carbohydrates:
Definition, function, source
Classification & Nomenclature:(With eg)
1. Sugars
Monosaccharides-Type of Carbonyl group, number of Carbon atoms.
Oligo saccharides-Disaccharides, Trisaccharides, Tetra Saccharides
2. Non Sugars or Poly saccharides-Configuration of Monosaccharides, Asymmetric carbon atom,Stereoisomers(Succinic acid and fumeric acid) enantiomers, optical isomers. Cyclic(ring) structure of sugars. Muta roration. Haworth formula, Conformational formulas, Glycosides.

Disaccharides and Polysaccharides of biological importance, Maltose, Lactose, Sucrose, Cellulose, Starch (Amylose & Amylopectin) & Glycogen.

Lipids:
Biological functions.
Classification: Simple lipids, fats and oils (saturated & unsaturated fats), waxes
and their importance, compound lipids, Phospholipids, Glycolipids, derived lipids.
Nomenclature of fats
Fatty acids-essential fatty acids
Trigylcerols-Hydrolysis of fats-saponification
Glycerol, Formation of esters, Dehydration.
Phospholipids (Phosphatides)
Functions of phospholipids, classification, Lecithins, Cephalins, Plasmalogens-
Sphingomyclins, Glycolipids (Carbosides & Gangliosides)
Steroids-Cholesterol, Stigmasterol

Proteins and aminoacids:
Definition, examples of Proteins,
Chemical Nature of Proteins, Hydrophilic and laevorotatory nature, Iso
electric point, Denaturation, renaturation or annealing, Hydrolysis, Colour reactions, Biuret, xanthoproteic, Millons & Ninhydrin test.
Biological value of proteins, Functions of Proteins.
Aminoacids-
Neutral aminoacids, Acidic aminoacids, Basic aminoacids, Properties of aminoacidsZwitter ions & iso electric point.
Structure of Proteins:
Primary, Secondary, tertiary and Quaternary structure of Proteins.
Eg: Insulin (Quaternary structure), egg albumin for denaturation
Nucleic Acids:
Chemistry, Nucleo proteins, Nucleic acids, Nitrogen base-Purines and
Pyrimidine with structure and (eg). Sugars-Pentose and deoxypentose with (eg) Phospheric acid, Proteins, histone and protamines.
Nucleosides and Nucleotides, Biologically important Nucleotides, (ATP) Nucleotides & Nuleic acids as Coenzymes.
RNA-rRNA,tRNA,mRNA

Unit III

Biological Oxidation
Bio energetics- Definition, enthalopy, entropy and the coupling of endergonic to exergonic process free energy. High energy Compounds.
Energy-rich bonds in important biochemical Compounds.
Linkage, formula and occurrence of Low energy and high energy type
Compounds. Electron transport and Oxidation phosphorylation energy –Conservation sites. Respiration chain – flow of energy from Carbohydrates to TCA cycle- flow electrons in mitochondria.
Electron transport system of the respiration chain showing the site of formation of 3ATP molecules.
Biological membranes
Fluid mosaic model-Singer Nicolson, Plasma membrane showing amino acids and Carbohydrates in RBC. Shematic representation of Proteins in membrane.
Transport across membranes:
Simple diffusion, passive transport, active transport, secondary transport and Ion channels with carrier, Energy dependent, source of energy along with examples. Stematic representation of simple diffusion, facilitated diffusion of cl- and Hco3, active transport of ATP(primary), Na+/K+ ATPase, and Lactose(secondary) uniport, Symport, Antiport & Co transport.

Unit IV

Biological Catalysis-
Historical background – Nomenclature and Classification of enzymes. The major features of the IUB system. The major six classes of the enzymes. Chemical nature and properties. Holoenzyme, Apoenzyme and Co enzyme, Efficiency, specificity (stereo reaction). Substrate and Enzyme(all with eg) of enzymes.
Factors affecting the enzyme activity.
Temperature, pH, Concentration of oter ions, Substrate Concentration and enzyme Concentration.
Enzyme Kinetics and Km value-
Michaelis & Menten explanation Michaelis plot. Line weaver – burk equation plot.

Active site-Lock-and Key relationship. Positionary site, catalytic site.
Inhibitions-
Definition, Competitive, non-Competitive and allosteric inhibition with examples showing stematically.
Mechanism of Enzyme action –
Fischers Lock-Key theory & its Draw backs. Koshland induces fit mechanism with figures explaining them.
Regulation of enzyme synthesis
Inductive, Constitutive, inducer, adaptives, examples with organism, Enzyme and Inducer, Pacemaker enzymes, units of Enzyme activity-definition.
Co enzymes-
Coenzymes explanation, Coenzymes involved in hydrozen transfer and those involved in transfer of groups or atom other than hydrogen.
Immobilized Enzymes-
Advantages of immobilized enzymes, Techniques for immobilization, adsorption, Covalent binding, Cross binding and antrapping method its draw backs. Entrapping by Micro encapsulation. Application of immobilized enzyme.
Iso enzymes-
LDH, Diagnostic importance of enzymes, Functional and non-functional enzymes, Enzymes of diagnostic value.
Therapentic uses of Enzymes.