Biochemistry

 

Promoters: Frans Ollevier, Ph.D. (KULeuven) and Johan Thevelijn, Ph.D. (KULeuven) Co-promoter: Elva Camba, M.Sc. (ESPOL) CENAIM Staff:Jenny Rodríguez, Ph.D., Nelson Montoya, M.Sc., Yela Paredes Theory = 52 hrs. Practical Training = 42 hrs.

Objectives and Description:

1. Understand the chemical nature and biological properties of biomolecules
2. Understand the role of enzymes
3. Understand the processes for energy production in living cells
4. At the completion of the course, students will be able to interpret function and regulation of metabolic pathways to maintain and propagate life

 

Content:

Part I: Introduction to Biochemistry

• Definition and relationships with other Sciences
• Main characteristics of living organisms. Chemical nature and properties of its principal components
• Water: physico-chemical properties and physiological and biochemical functions
• Essential biomolecules
• Homeostasis and regulatory mechanisms at the neuronal, hormonal and enzymatic levels
• Morphological biochemistry

Practical Training:

• General rules for working in the laboratory - Biosecurity
• Preparation of different types of solution

Part II: Biological Macromolecules - The Protein

• Structural unity of the protein. Composition and properties of the amino acids
• Definition and biological importance of proteins
• Biological value of proteins. Essential amino acids
• Protein classification based on size, shape, solubility, composition and biological function
• Protein organization and shape: importance for its functionality
• Protein denaturalization: denaturalizing agents and mechanisms of action

Practical Training:

• Determination of the isoelectric point of proteins
• Proteins denaturalization with different agents
• Protein electrophoresis
• Protein determination with the micro-Lowry method

Part III: Enzymes and Biological Catalysis

• Definition, chemical nature and biological importance of enzymes
• Main characteristics of the enzymes: efficiency and specificity
• Nomenclature and classification
• Enzymatic co-factors. Chemical nature of co-factors
• Mechanisms of enzymatic catalysis
• Enzymatic kinetic. Michaelis-Menten equation
• Lineweaver-Burck equation
• Factors affecting the speed of the reactions catalyzed by enzymes
• Enzymatic inhibitors. Mechanisms of inhibition
• Allosteric enzymes: Mechanisms of regulation. Allosteric modulators
• Zymogen: Mechanisms of activation
• Multi-enzymatic complexes. Isoenzyme conformation
• Regulation and control of the enzymatic activity
• Integration of the enzymes in metabolic pathways

Practical Training:

• Temperature effect on the speed of biochemical reactions
• Measure of the enzymatic activity: NADPH, oxidase and phenoloxidase.

Part IV: Structure and Chemistry of the Carbohydrates

• Definition, composition, properties and biological functions of the carbohydrates
• Origin of the glucids in the organism
• Monosaccharide derivatives of biological interest
• Oligosaccharides and polysaccharides: structure and classification
• Homopolysaccharides: starch, glycogen, cellulose, insulin, chitin and lignin. Types of glycoside links
• Heteropolysaccharides: Acid hyalurodic, chondroitin sulfate, keratin sulfate, heparin
• Polysaccharides hydrolysis. Types of hydrolysis and by-products

Practical Training:

• Identification reactions for carbohydrates
• Carbohydrates separation through thin layer chromatography
• Polysaccharides hydrolysis: measurement of the amylase activity

Part V: Structure and Chemistry of the Lipids

• Definition, composition, properties and biological functions of the lipids
• Lipids structure and classification
• Simple lipids: fatty acids, fatty alcohol and triglycerids
• Complex lipids: phospholipids, glycolipids, joined lipids
• Isoprenoid lipids: terpens, steroids, retinoles, carotenoids and tocopherol
• Prostaglandin and tromboxan

Practical Training:

• Glycogen determination

Part VI: Structure and Chemistry of the Nucleic Acids

• Definition, composition and chemical structure of the nucleic acids
• Types of nucleic acids: Function and cellular location
• Structural characteristics, size and shape of DNA
• Watson and Crick model
• DNA dynamic: denaturalization and renaturalization
• DNA in chromosomes
• Structural characteristics of RNA. RNA types: messenger, transfer and ribosomal
• Information fluxes in living organisms. Genetic code: characteristics

Practical Training:

• Amino acids separation through paper chromatography
• Amino acids profiles in shrimp and fish (HPLC technique)

Part VII: Metabolically Derived Energy

• Digestion of carbohydrates, lipids, proteins and nucleic acids. Digestion disturbance
• Absorption of carbohydrate, lipid and protein metabolites
• Energy metabolically derived
• Krebs cycle: metabolites, enzymes and co-enzymes involved. Function, energetic balance, control and regulation
• Respiratory chain: enzymatic complexes, organization and cellular location
• Oxidative phosphorilation. Desaccoupling and inhibitors
• Process control and global yield