BT2202 BIOORGANIC CHEMISTRY SYLLABUS | ANNA UNIVERSITY B.TECH. BIOTECHNOLOGY 3RD SEMESTER SYLLABUS REGULATION 2008 2011-2012 BELOW IS THE ANNA UNIVERSITY THIRD SEMESTER B.TECH. BIOTECHNOLOGY DEPARTMENT SYLLABUS IT IS APPLICABLE FOR ALL STUDENTS ADMITTED IN THE YEAR 2011-2012 (ANNA UNIVERSITY CHENNAI,TRICHY,MADURAI,TIRUNELVELI,COIMBATORE), 2008 REGULATION OF ANNA UNIVERSITY CHENNAI AND STUDENTS ADMITTED IN ANNA UNIVERSITY CHENNAI DURING 2009
BT2202 BIOORGANIC CHEMISTRY L T P C
3 0 0 3
AIM(S) OF THE COURSE
The course aims to develop skills of Students in the area of Organic Chemistry and its
applications in Biology. This will be a prerequisite to courses like Molecular Modelling,
Bioseparations etc.
UNIT I INTRODUCTION TO ENZYMES 9
Classification of enzymes. Mechanisms of enzyme action; concept of active site and
energetics of enzyme substrate complex formation; specificity of enzyme action;
Stereochemistry – R,S notation – re-si faces – e,z isomerism- conformers- ethane –
cyclopean - reactivates- mechanisms of sn1 sn2 reactions, e1 e2 reactions – ester
formation and hydrolysis, reaction rates - hammond's postulate – h/d effects. Catalysis –
general acid – base and covalent catalysis.
UNIT II KINETICS OF ENZYME ACTION 9
Allosteric regulation of enzymes, Monod changeux wyman model, ph and temperature
effect on enzymes & deactivation kinetics - Stereospecific enzymatic reactions –
Stereochemistry of nucleophilic reactions – chiral methyl group – chiral phosphate.
UNIT III ENZYME IMMOBILIZATION & CASE STUDIES OF ENZYME
STRUCTURE AND MECHANISM 9
Physical and chemical techniques for enzyme immobilization – adsorption, matrix
entrapment, encapsulation, cross-linking, covalent binding etc., - examples, advantages
and disadvantages. Case studies include dehydrogenases, proteases – - lysozymestability
of proteins
UNIT IV KINETICS OF PROTEIN FOLDING 9
Kinetics of single substrate reactions; estimation of Michelis – Menten parameters, multi
substrate reactions- mechanisms and kinetics; turnover number; types of inhibition &
models –substrate, product - folding of peptides.
UNIT V FOLDING PATHWAYS & ENERGY LANDSCAPES 9
Folding of ci2 – nucleation condensation mechanism – folding of barnase – time
resolution – insights from theory – optimization of folding rates – molecular chaperones.
Production and purification of crude enzyme extracts from plant, animal and microbial
sources; methods of characterization of enzymes; development of enzymatic assays
.
TOTAL: 45 PERIODS
TEXTS BOOKS
1. Harvey W. Blanch, Douglas S. Clark, “Biochemical Engineering”, Marcel Dekker, Inc.
2. James M. Lee, “Biochemical Engineering”, PHI, USA.
REFERENCES
26
1. Structure and Mechanism In Protein Science: A Guide To Enzyme Catalysis and
Protein Folding; A. R. Fersht, W.H. Freeman, 1999.
2. Bioorganic Chemistry; H. Dugas, Springer Verlag, 1999.
3. James. E. Bailey & David F. Ollis, “Biochemical Engineering Fundamentals”,
McGraw-Hill.
4. Wiseman, “Enzyme Biotechnology”, Ellis Horwood Pub.
BT2202 BIOORGANIC CHEMISTRY L T P C
3 0 0 3
AIM(S) OF THE COURSE
The course aims to develop skills of Students in the area of Organic Chemistry and its
applications in Biology. This will be a prerequisite to courses like Molecular Modelling,
Bioseparations etc.
UNIT I INTRODUCTION TO ENZYMES 9
Classification of enzymes. Mechanisms of enzyme action; concept of active site and
energetics of enzyme substrate complex formation; specificity of enzyme action;
Stereochemistry – R,S notation – re-si faces – e,z isomerism- conformers- ethane –
cyclopean - reactivates- mechanisms of sn1 sn2 reactions, e1 e2 reactions – ester
formation and hydrolysis, reaction rates - hammond's postulate – h/d effects. Catalysis –
general acid – base and covalent catalysis.
UNIT II KINETICS OF ENZYME ACTION 9
Allosteric regulation of enzymes, Monod changeux wyman model, ph and temperature
effect on enzymes & deactivation kinetics - Stereospecific enzymatic reactions –
Stereochemistry of nucleophilic reactions – chiral methyl group – chiral phosphate.
UNIT III ENZYME IMMOBILIZATION & CASE STUDIES OF ENZYME
STRUCTURE AND MECHANISM 9
Physical and chemical techniques for enzyme immobilization – adsorption, matrix
entrapment, encapsulation, cross-linking, covalent binding etc., - examples, advantages
and disadvantages. Case studies include dehydrogenases, proteases – - lysozymestability
of proteins
UNIT IV KINETICS OF PROTEIN FOLDING 9
Kinetics of single substrate reactions; estimation of Michelis – Menten parameters, multi
substrate reactions- mechanisms and kinetics; turnover number; types of inhibition &
models –substrate, product - folding of peptides.
UNIT V FOLDING PATHWAYS & ENERGY LANDSCAPES 9
Folding of ci2 – nucleation condensation mechanism – folding of barnase – time
resolution – insights from theory – optimization of folding rates – molecular chaperones.
Production and purification of crude enzyme extracts from plant, animal and microbial
sources; methods of characterization of enzymes; development of enzymatic assays
.
TOTAL: 45 PERIODS
TEXTS BOOKS
1. Harvey W. Blanch, Douglas S. Clark, “Biochemical Engineering”, Marcel Dekker, Inc.
2. James M. Lee, “Biochemical Engineering”, PHI, USA.
REFERENCES
26
1. Structure and Mechanism In Protein Science: A Guide To Enzyme Catalysis and
Protein Folding; A. R. Fersht, W.H. Freeman, 1999.
2. Bioorganic Chemistry; H. Dugas, Springer Verlag, 1999.
3. James. E. Bailey & David F. Ollis, “Biochemical Engineering Fundamentals”,
McGraw-Hill.
4. Wiseman, “Enzyme Biotechnology”, Ellis Horwood Pub.
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