Syllabus
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Course Code: BT-205 Course Name: Enzyme Technology |
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| MODULE NO / UNIT | COURSE SYLLABUS CONTENTS OF MODULE | NOTES |
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| 1 | History of Enzymology; General characteristics of enzymes; advantages of enzymes over chemical catalysts, Nomenclature and classification of enzymes, Significance of Enzyme Commission number; Determination of three dimensional structure of enzyme by X-ray crystallography and NMR spectrometry, importance of 3-D structure of an enzyme; Classification of enzyme structures, structures adopted by enzymes, principles that govern the 3-D structure adopted by enzymes; Forces for stability of 3-D structure; Denaturation and renaturation; Isoenzymes, enzyme specificity, monomeric and oligomeric enzymes, multienzyme complex, holoenzyme, apo-enzyme, cofactor, coenzyme, prosthetic group; enzyme activity unit, turn over number and specific activity, Ribozymes and Abzymes – A brief account. |
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| 2 | Enzyme action; effect of enzyme on the rate and equilibrium of a reaction; principles that explain catalytic power and substrate specificity of enzymes; enzyme substrate complex(Lock & Key Model, Induced Fit Theory, Substrate Strain Theory), factors responsible for catalytic efficiency of enzyme; proximity and orientation effect, acid-base catalysis, covalent catalysis, strain and distortion theory; Nature of active site, identification of functional groups at active sites; regulatory enzymes- covalently modulated enzymes, allosteric enzymes and their mode of action; regulation of enzyme activity in the living system. | |
| 3 | An introduction to enzyme kinetics and its importance, Methods used for investigating the kinetics of enzyme catalysed reactions; factors that influence the velocity of enzyme catalysed reaction(effect of substrate concentration, enzyme concentration, pH, temperature, presence of activator/inhibitor etc.); Michaelis-Menten equation, Vmax, Km and its significance; Lineweaver Burk plot- its advantages and limitations, Eadie- Hofstee and Hanes plots; enzyme inhibition, types of enzyme inhibitions- competitive, uncompetitive, non-competitive, mixed type inhibition and determination of Ki, Determination of Km and Vmax in the presence and absence of inhibitor; feed- back inhibition; Bisubstrate reactions- brief introduction to sequential and Ping-Pong mechanism with examples. | |
| 4 | Strategies used for enzyme production, isolation and purification at laboratory and industrial scale from plant, animal and microbial sources , method of calculating the purification fold; estimation of enzyme activity; characterization of an enzyme, criteria of enzyme purity, determination of the molecular weight (MW) and the number of sub-units of an enzyme; enzyme immobilization and its importance; protein engineering; enzyme therapy, enzyme inhibitors and drug design; enzymes as biosensors, enzyme reactors; Applications of enzymes in medicine, textile, leather, detergent, paper, bakery, dairy industry, beverage and fruit processing, food processing and preservation, clinical applications of enzyme estimation. | |
