Biochemistry and Biochemical Analysis of Foods
A.Y. 2025/2026
Learning objectives
The course aims to provide students with the basic notions of the structure and function of proteins and basic knowledge of the main metabolic pathways of animal organisms. It also aims to provide the methodological principles of the biochemical approaches that can be used for the characterization and analysis of foods: enzymatic methods, immunochemical methods, separative techniques and molecular biology techniques.
Expected learning outcomes
At the end of the course the student will be able to understand the functioning of the main biological processes and the biochemical transformations that the main nutrients undergo in metabolism, also depending on the state of nutrition. Furthermore, the student will be able to critically evaluate, both in quantitative and qualitative terms, the results obtained by the main biochemical methodologies suitable for the characterization of foods.
Lesson period: First semester
Assessment methods: Esame
Assessment result: voto verbalizzato in trentesimi
Single course
This course cannot be attended as a single course. Please check our list of single courses to find the ones available for enrolment.
Course syllabus and organization
Single session
Responsible
Lesson period
First semester
Course syllabus
Biochemistry
Amino acids: general properties. Physical properties and chemical reactivity of side chains. Proteins: primary structure and post-translational modifications. The peptide bond. Secondary structure: alpha-helix and beta-sheet. Tertiary structure. Quaternary structure and its functional role. Collagen as an example. Quaternary structure and allosteric regulation: myoglobin and haemoglobin. Enzymes: enzymatically catalysed reactions. Michelis-Menten. Competitive and Uncompetitive inhibition of non-cooperative enzymes. Allosteric enzymes. Covalent regulation of enzymatic activity.
Introduction to metabolism: nature and role of cofactors. ATP, NAD and FAD. Glycolysis. Lactic and alcoholic fermentation. Metabolism of hexoses other than glucose. Gluconeogenesis. Control of glycolysis and gluconeogenesis. Role of fructose-2,6-bisphosphate. Hormonal regulation. Glycogen synthesis and brakedown. Pentose phosphate pathway. Pyruvate conversion to acetyl-CoA. Krebs cycle. Electron transport and oxidative phosphorylation. Energetic Balance of the total oxidation of glucose. Catabolism of fatty acids: beta oxidation. Catabolism of unsatured fatty acids. Fatty acid biosynthesis. Cholesterol biosynthesis. Plasma lipoproteins. Amino acid metabolism: protein digestion and transamination reaction. The urea cycle. Basis of amino acid carbon skeletons catabolism.
Biochemical Analysis of Food
Principles of UV-vis spectrophotometry. Enzymatic methods: principles of enzymology. Enzymatic assays: quantification of enzyme activity and its meaning for food quality. Thermal inactivation of enzymes. Use of enzymatic tests for the quantification of specific compounds in foods. Immunochemical methods: structure and properties of antibodies. Principles and application of quantitative immunochemical methods (ELISA). Rapid immunochromatographic assays (lateral flow tests). Application of molecular biology techniques to food safety issues. Classical and real-time PCR. Electrophoretic methods: principles of electrophoretic techniques. PAGE, SDS-PAGE, IEF, 2D-PAGE. Chromatographic methods: principles of chromatographic techniques. Gel-permeation chromatography, ionic exchange chromatography, reverse phase chromatography, affinity chromatography.
Amino acids: general properties. Physical properties and chemical reactivity of side chains. Proteins: primary structure and post-translational modifications. The peptide bond. Secondary structure: alpha-helix and beta-sheet. Tertiary structure. Quaternary structure and its functional role. Collagen as an example. Quaternary structure and allosteric regulation: myoglobin and haemoglobin. Enzymes: enzymatically catalysed reactions. Michelis-Menten. Competitive and Uncompetitive inhibition of non-cooperative enzymes. Allosteric enzymes. Covalent regulation of enzymatic activity.
Introduction to metabolism: nature and role of cofactors. ATP, NAD and FAD. Glycolysis. Lactic and alcoholic fermentation. Metabolism of hexoses other than glucose. Gluconeogenesis. Control of glycolysis and gluconeogenesis. Role of fructose-2,6-bisphosphate. Hormonal regulation. Glycogen synthesis and brakedown. Pentose phosphate pathway. Pyruvate conversion to acetyl-CoA. Krebs cycle. Electron transport and oxidative phosphorylation. Energetic Balance of the total oxidation of glucose. Catabolism of fatty acids: beta oxidation. Catabolism of unsatured fatty acids. Fatty acid biosynthesis. Cholesterol biosynthesis. Plasma lipoproteins. Amino acid metabolism: protein digestion and transamination reaction. The urea cycle. Basis of amino acid carbon skeletons catabolism.
Biochemical Analysis of Food
Principles of UV-vis spectrophotometry. Enzymatic methods: principles of enzymology. Enzymatic assays: quantification of enzyme activity and its meaning for food quality. Thermal inactivation of enzymes. Use of enzymatic tests for the quantification of specific compounds in foods. Immunochemical methods: structure and properties of antibodies. Principles and application of quantitative immunochemical methods (ELISA). Rapid immunochromatographic assays (lateral flow tests). Application of molecular biology techniques to food safety issues. Classical and real-time PCR. Electrophoretic methods: principles of electrophoretic techniques. PAGE, SDS-PAGE, IEF, 2D-PAGE. Chromatographic methods: principles of chromatographic techniques. Gel-permeation chromatography, ionic exchange chromatography, reverse phase chromatography, affinity chromatography.
Prerequisites for admission
The prerequisites for this course are the basic concepts of cell biology, and the ability to recognize the chemical reactivity of the major functional groups in molecules (-OH, -COOH, -SH, -NH2). Basic mathematics for quantitative approach to biochemistry.
Teaching methods
Frontal lessons and practical classes.
Teaching Resources
Biochestry
INTRODUZIONE ALLA BIOCHIMICA DI LEHNINGER (Nelson/Cox, Zanichelli). BIOCHIMICA (Campbell/Farrel, EdiSES).
Biochemical Analysis of Food
Slides presented in class, shared with students via the teaching myAriel site.
INTRODUZIONE ALLA BIOCHIMICA DI LEHNINGER (Nelson/Cox, Zanichelli). BIOCHIMICA (Campbell/Farrel, EdiSES).
Biochemical Analysis of Food
Slides presented in class, shared with students via the teaching myAriel site.
Assessment methods and Criteria
To verify learning achievements in the course in Biochemistry and Biochemical Analysis of Food students go through a final written exam, to be completed in 2 hours, in which open-ended questions are proposed. The achievement of the objectives established by the course will be evaluated taking into account the candidate's ability to accurately define the topics, to offer an overall systematic view of the topics, and familiarity with the specific language. The dates of the exams, and the registration deadline to take the exam, are communicated through the University application (UNIMIA). Evaluation is expressed in thirtieths. Results are communicated to the students by an automatically-generated e-mail.
Students with specific learning disabilities or other disabilities are requested to contact the Professor via email at least 15 days before the exam session to agree on any individualized measure. In the email addressed to the teacher, the respective University services must be registered in CC: [email protected] (for students with LD) and [email protected] (for students with disabilities).
Students with specific learning disabilities or other disabilities are requested to contact the Professor via email at least 15 days before the exam session to agree on any individualized measure. In the email addressed to the teacher, the respective University services must be registered in CC: [email protected] (for students with LD) and [email protected] (for students with disabilities).
BIO/10 - BIOCHEMISTRY - University credits: 8
Laboratories: 8 hours
Lessons: 60 hours
Lessons: 60 hours
Professor:
Barbiroli Alberto Giuseppe
Professor(s)