Subject Code & Name: BT25401 – Enzyme Technology
Regulation: R-2025
Semester: IV (Fourth Semester)
Branch: B.Tech. Biotechnology (Biotech)
Credits / L-T-P: 3 Credits | L-T-P: 2-1-0
Course Objectives
- To provide the fundamentals of enzymes, enzyme kinetics and inhibition as well as knowledge about the production, immobilization methods and application of enzymes.
Full Unit-wise Syllabus
Unit I – Overview of Enzymes and Their Action
Nature of enzymes – Features of active site – Peptide bond formation – Properties of enzymes – Classification of enzymes - Factors affecting enzyme Activities – Enzyme specificity – Cofactors and Coenzymes – Mechanisms of enzyme action – Monomeric and oligomeric enzymes.
Activities: Preparation of concept maps illustrating enzyme structure and active site interactions.
Unit II – Kinetics of Enzyme Catalysed Reactions
Kinetics of single-substrate enzyme catalysed reactions: Time course of enzymatic reactions - Relationship between initial velocity and substrate concentration – Derivation of Henri Michaelis-Menten equation – Derivation of Briggs-Haldane modification of Michaelis-Menten – Significance of Vmax, Km and Kcat – Linearized form of Michaelis-Menten equations (Lineweaver-Burk plot, Eadie- Hofstee plot, Hanes-Wolff plot and Eisenthal-Cornish- Bowden direct plot) – Kinetics of multi-substrate enzyme catalysed reactions: Ping- Pong bi-bi mechanism, Random order mechanism, Compulsory order mechanism.
Activities: Case study analysis on industrial relevance of enzyme kinetics.
Unit III – Enzyme Inhibition
Overview of reversible and irreversible inhibition – Competitive inhibition – Uncompetitive inhibition – Non-competitive inhibition – Mixed inhibition – Partial inhibition – Substrate inhibition – Allosteric inhibition - Monod Changeux Wyman model.
Activities: Group discussion on the significance of enzyme inhibitors in therapeutics and drug design.
Unit IV – Production, Purification and Applications of Enzymes
Production, purification and characterization of enzymes from microbial, plant and animal sources - Enzymes in food industry – Enzymes in organic synthesis – Enzymes in therapeutic; Enzymes in pharmaceutical and textile industries.
Activities: Case Study on production and applications of enzymes.
Unit V – Enzyme Immobilization and Biosensors
Overview of enzyme immobilization – Methods of reversible enzyme immobilization: Adsorption, Ionic binding, Affinity binding, Chelation or metal binding, Disulfide bonds - Methods of irreversible enzyme immobilization: Covalent binding, Entrapment (beads or fibres), Encapsulation, Cross linking – Multi-enzyme immobilization: Random co-immobilization, position co- immobilization and compartmentalization - Advantages and disadvantages of enzyme immobilization - Applications of immobilized enzymes in biosensor for healthcare (Biosensors for the detection of Glucose and Urea) and environment (Biosensors for the detection of Chromium and Arsenic).
Activities: Poster presentation on biosensors and Reproduction of research paper/Case Study
Course Outcomes (COs)
- CO1: Understand mechanisms of enzyme action in biological systems.
- CO2: Apply enzyme kinetics principles to analyze catalytic reactionsand determine enzyme activity.
- CO3: Analyze the different types of enzyme inhibition and their effects on biochemical reaction rates.
- CO4: Evaluate enzyme production methods and their industrial, medical, and biotechnological applications.
- CO5: Design enzyme immobilization systems and biosensor-based applications for solving biotechnology-related problems.
Assessment Pattern (Quick Note)
- Weightage: Continuous Assessment 40% | End Semester Examinations 60%
- Internal methodology: Assignments (20%), Solution to application-oriented problems (20%), Seminar/Poster presentation (20%), Internal Examinations (40%)
Source: Official Anna University – B.Tech. Biotechnology R-2025 Syllabus
Last Updated: October 2026
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