Logo UAB
2023/2024

Biochemistry I

Code: 103266 ECTS Credits: 6
Degree Type Year Semester
2501925 Food Science and Technology FB 1 2

Contact

Name:
Anna Maria Bassols Teixido
Email:
anna.bassols@uab.cat

Teaching groups languages

You can check it through this link. To consult the language you will need to enter the CODE of the subject. Please note that this information is provisional until 30 November 2023.

Teachers

Jorge Pérez Valle

Prerequisites


There are no official prerequisites. However, it is advisable to review the basic contents of Biology and Chemistry of the first semester and the Baccalaureate.


Objectives and Contextualisation

This subject should allow the student to understand that biological processes, especially those related to food and metabolism, have a chemical basis and that can be explained in these terms.
										
											
										
											The student must understand the structural bases of these processes, as well as the structural bases that explain the function in the different types of biological compounds: carbohydrates, lipids, proteins, vitamins and trace elements, and nucleic acids.
										
											
										
											Likewise, the student must understand the molecular basis of the transmission of genetic information and its regulation, as well as its applications in food biotechnology.
										
											
										
											The specific training objectives are to know and understand:
										
											
										
											- The structure and function of proteins, carbohydrates, lipids, nucleotides and vitamins.
										
											
										
											- The structure of nucleic acids and the processes of replication, transcription, translation and regulation of gene expression.
										
											
										
											- The foundations and applications of the main biochemical and molecular biology techniques and methodologies.

All aspects with an special focus on on Food Science and Technology

Competences

  • Adopt an ethical stance and attach importance to quality in work.
  • Analyse, summarise, resolve problems and make professional decisions.
  • Apply knowledge of the basic sciences to food science and technology.
  • Apply the scientific method to resolving problems.
  • Communicate effectively with both professional and non-professional audiences, orally and in writing, in the first language and/or in English.
  • Develop individual learning strategies and planning and organisation skills.
  • Display knowledge of nutrients, of their bioavailability and function in the organism, and the bases of nutritional balance.
  • Display knowledge of the physical, chemical, biochemical and biological properties of raw materials and foods.
  • Search for, manage and interpret information from different sources.
  • Stay abreast of new knowledge, adapt to new situations and develop creativity.
  • Use IT resources for communication, the search for information within the field of study, data processing and calculations.

Learning Outcomes

  1. Adopt an ethical stance and attach importance to quality in work.
  2. Analyse, summarise, resolve problems and make professional decisions.
  3. Apply the fundamental principles and the applications of biochemistry to food biotechnology.
  4. Apply the scientific method to resolving problems.
  5. Communicate effectively with both professional and non-professional audiences, orally and in writing, in the first language and/or in English.
  6. Describe mechanisms of transmission and regulation of genetic information in the cell.
  7. Describe the reactions of reaction, kinetics and enzyme regulation.
  8. Develop individual learning strategies and planning and organisation skills.
  9. Establish the metabolic role of vitamins, oligoelements and other essential nutrients.
  10. Explain the structures and properties of the principal biological molecules.
  11. Search for, manage and interpret information from different sources.
  12. Stay abreast of new knowledge, adapt to new situations and develop creativity
  13. Use IT resources for communication, the search for information within the field of study, data processing and calculations.

Content

PART 1. THE CHEMISTRY OF LIFE 

Unit 1.- Introduction to the chemistry of living beings. Biomolecules. Properties of water and importance of the aqueous environment for living organisms. 

Unit 2.- Constituents of proteins: amino acids. Structure and properties. 

Unit 3.- The amino acid sequence of proteins. The peptide bond. The primary structure of proteins. Sequencing of peptides.

Unit 4.- Three-dimensional structure of proteins. Secondary structure. The α-helix and the β-sheet. Tertiary structure. Quaternary structure. Structural domains. Native conformation and denaturalization. 

Unit 5.- Fibrous proteins. α-keratin, collagen and others.

Unit 6.- Oxygen-transport proteins. Structure of myoglobin and hemoglobin. The center of oxygen binding. Cooperativity and allosterism. Allosteric effectors 

Unit 7.- Catalytic proteins: enzymes. General properties. Classification. Substrates and coenzymes or cofactors. Isoenzymes. Enzymatic catalysis. 

Unit 8.- Enzyme kinetics. The Michaelis-Menten equation. Meaning of Km and Vmax. Effects of pH and temperature on enzymatic activity. Enzyme inhibition. Main catalysis mechanisms.
Unit 9.- Mechanisms of regulation of enzymatic activity: Regulation of enzyme concentration. Allosteric enzymes. Reversible covalent modification. Protein-protein interaction. Changes in subcellular location. Irreversible covalent modification (proteolysis). 

Unit 10.- Vitamins and trace elements. Structure, function, requirements and avitaminosis.
Unit 11.- Biochemical study of carbohydrates. Generalities. Families of monosaccharides. Natural oligosaccharides. Reserve polysaccharides and structural polysaccharides.
										
											
										
											Unit 12.- Biochemical study of lipids. Fatty acids. Triglycerides. Phosphoglycerides. Sphingolipids and glucolipids. Cholesterol
										
											
										
											Unit 13.- Nucleotides and derivatives. Purines and pyrimidines and their nucleotides. The nucleotides as enzymatic cofactors. Cyclic AMP.

										
											PART 2. REPLICATION, TRANSCRIPTION, SYNTHESIS OF PROTEINS AND THEIR REGULATION
										
											
										
											Unit 14.- Nucleic Acids. DNA and its structure. Base equivalence. Double helix. Nucleosomes.
Unit 15.- DNA replication. Semiconservative replication. DNA polymerases. Okazaki fragments. DNA replication: initiation, elongation and termination. DNA repair.
										
											
										
											Unit 16.- RNA and transcription. RNA polymerase and synthesis of RNAs. Prokaryotes and eukaryotic promoters. Post-transcriptional modifications of rRNA and tRNA. Processing of mRNA in eukaryotes. Introns and splicing.
										
											
										
											Unit 17.- The genetic code. The nature of the code and its main features. The base triplets. tRNA as an adapter in protein synthesis.
Unit 18.- The synthesis of proteins. Activation of amino acids. Characteristics of aminoacyl tRNA synthase.  Initiation, elongation and termination. Introduction to the synthesis of proteins in eukaryotes.
										
											
										
											Unit 19.- Control of gene expression. Induction and gene repression. Lac operon. Control of gene expression in eukaryotes.
Unit 20.- Introduction to food biotechnology. Introduction to recombinant DNA techniques. Biotechnological applications of bacteria, yeasts, plants and animals. Analytical techniques: PCR, antibodies, biosensors.

 

LABORATORY PRACTICES.
										
											
										
											Practice 1. Separation of a mixture of amino acids by ion exchange chromatography and identification by thin layer chromatography.
										
											
										
											Practice 2. Enzymes: determination of the Km.
										
											
										
											Practice 3. Bioinformatic applications in bibliographic research.
										
											
										
											Practice 4 (2 days). Applications of PCR to food biotechnology.
										
											
										
											 
										
											SEMINARS
										
											
										
											Seminar 1: Chromatographic techniques.
										
											
										
											Seminar 2: Spectrophotometric techniques.
										
											
										
											Seminar 3: Enzymatic analysis.
										
											
										
											Seminar 4: Discussion of a scientific article.Seminar 5: PCR, cloning, recombinant protein expression.
										
											
										
											Seminar 6: Sequence of DNA,microarrays.

Methodology

The methodology of the learning process combines the theoretical classes where the teacher exposes the most relevant aspects of each subject and the active self-learning by the student on topics of interest. The subject is based on the following activities:
  • Presential lectures with ICT support explaining the basic concepts of the subject.
  • Seminars and problem solving: Presentation by the teacher of specific topics and discussion in small groups.
  • Laboratory practices: Acquisition of work skills in the laboratory and experimental understanding of concepts explained in face-to-face classes and seminars.
  • Autonomous work of the student, individually or in groups, for the preparation of topics proposed by the teacher or the student. This work involves the search and selection of information in various sources of scientific databases. Presentations are public, they must include multimedia material and ICT support and are followed by a discussion.

Some of the lectures may be given as flipped classes, where the classroom is devoted to problem solving and discussion of difficult aspects of the topic

Several questions and activities may be proposed through the moodle classroom

 

Annotation: Within the schedule set by the centre or degree programme, 15 minutes of one class will be reserved for students to evaluate their lecturers and their courses or modules through questionnaires.


Activities

Title Hours ECTS Learning Outcomes
Type: Directed      
Laboratory practices 12 0.48 2, 4, 3, 1, 8, 10
Seminars and problem solving 6 0.24 2, 4, 3, 9, 10
Theoretical lectures 31 1.24 2, 4, 3, 1, 7, 6, 9, 10
Type: Supervised      
Self-learning preparation 22.5 0.9 3, 1, 11, 5, 7, 6, 8, 9, 10, 13
Type: Autonomous      
Study and bibliographic searching 74 2.96 2, 4, 3, 11, 7, 6, 8, 9, 10, 13

Assessment

The maximum score is 10 points. Students will pass the subject with an overall score of 5.0 or higher. The evaluation system is organized in three modules. The final qualification is obtained with the sum of the qualifications of the different modules, with the conditions described below.
 • Module 1. Theory, seminars and problems. - Evaluation system: test with multiple choice answers. - Weight in the global rating: 70%. - Competences evaluated: CE1, CE2, CE11, CT1, CT2, CT9 Students may opt for partial tests of the syllabus. 
There will be two partial tests throughout the semester. The first test includes from Topic 1 to Topic 12 (approx, depending on the specific calendar). Part 2 includes from topic 13 to 20. Each test will consist of approximately 25 type-test questions for each partial. Seminar questions will be included. 

The scheme includes the different possibilities: 

1) In the case of obtaining a minimum of 4,5 in each partial exam, the mean of the two scores will be calculated. The average mark must be equal to or greater than 5. In this case, the final mark will be obtained by the sum of the average of the two partials (weight 70%), the mark of the practice exam (weight 10%) and the note of self-learning (20% weight). 
If this number is equal to or higher than 5, the mark is Passed. If the sum is less than 5, the final grade will be Failed. in the case that the mark is Failed but the average grade of the two exams higher or equal 5, the student may retake the test to improve the mark and to approve the subject. The student will have to agree with the teacher which partial exam is to be retaken.

2) If the average of the two partial exams is less than 5, the student will have to retake the partial / partials with a score less than 5. In case that only a partial one should be retaken, the grade must be equal or higher than 4.5 (out of 10). 
The final mark will be calculated from the sum of the average of the two partials (weight: 70%), the mark of the practice exam (weight: 10%) and the mark of the self-study work (weight: 20%). If this number is equal to or higher than 5, the grade is Passed. If the sum is less than 5, the final grade will be Failed.
If in the retake of the partial exam the student obtains a mark less than 4.5 (out of 10), the partial exams will not compensate and therefore, the final qualification will be Failed.
										
											
										
											3) In case the student has to retake the two partial exams, the exam will be of all the subject (Module 1: theory + seminars). The exam will be corrected as a single test. The minimum mark in the recovery exam must be 4.5 (out of 10). A note lower than 4.5 represents a Failed as the final grade.
If the mark of the retake exam is equal to or higher than 4,5 (out of 10), the final mark will be obtained by the sum of the retake exam (weight: 70%), the mark of the Laboratory Practices exam (weight: 10%) and the mark of self-learning (weight: 20%). 
If this number is equal to or greater than 5, the final grade will be Passed. If the sum is less than 5, the final grade will be Failed.


• Module 2. Laboratory practices:Laboratory practices are mandatory. The student who has not completed them or does not present the poster will be qualified as Not Presented or Failed, depending on their situation, regardless of the grade that they have obtained in the exam.
. - Assessment system:Design and construction of a poster about one or more laboratory practices (the choice will be made by the professor). - Weight in the global rating: 10% (Maximum score: 1,0) - Competences evaluated: CE1, CE2, CE11, CT2, CT8,CT9 


• Module 3. Self-learning. Theself-learning work is compulsory and, therefore, the student who does not take it will be graded as Not Presented or Failed, depending on their situation and regardless of the grade that they have obtained in the exam. 
- Evaluation system: papers presented. - The written and oral presentation will be evaluated, as well as the competence when discussing the topic. - Weight in the global rating: 20% (Maximum score: 2.0) - Skills evaluated: CE1, CE2, CE11, CT4, CT5, CT6, CT8, CT10

 Retake exam In the retake exam the student will be able to take the failed partial exam or both (obligatory or voluntarily) corersponding to Module 1. The obtained mark, which will represent 70% of the note mark, will be added to the marks obtained in Modules 2 and 3 as indicated above. 
Any student regardless of the score obtained in the partial tests may choose to examine the entire program in the retake exam to obtain a higher mark. In this case, the mark will be the one from the last exam.  Non-gradable: A student is not gradable if he has participated in assessment activities that represent ≤ 15% of the final grade
 Single assessment: Students who take the single assessment must do the laboratory practices in the in-person sessions at the time set in the calendar. Attendance and in-person presentation of the work corresponding to Module 3 (Self-Learning Work) is also mandatory, and the student will have to attend the entire session on the indicated day. 
The single assessment test will coincide with the same date fixed in the calendar for the last continuous assessment test and the same assessment and recovery system will apply as for the continuous assessment. The presentation of the poster as an evaluation system for the practices and the evaluation of module 3 will take place on the day 
of the single assessment.

Assessment Activities

Title Weighting Hours ECTS Learning Outcomes
Exam of laboratory practices 10 0 0 2, 4
Partial and final exams 70 2 0.08 2, 3, 1, 7, 6, 8, 9, 10
Presentation and discussion of self-learning project 20 2.5 0.1 2, 4, 3, 11, 5, 7, 6, 9, 10, 12, 13

Bibliography

Basic bibliography:

Qualsevol llibre de Química General, 

Main textbooks:

1.- Stryer, L., Berg, J.M. & Tymoczko, J.L.  BIOQUIMICA. CURSO BASICO. 1ª edició. Ed. Reverté 2014

2.- Stryer L. Biochemsitry, 5th edition 2015. https://www.ncbi.nlm.nih.gov/books/NBK21154/?term=stryer%20biochemistry

3.- Nelson, D.L., & Cox, M.M. Lehninger Principles of Biochemistry. 5ª edició. Freeman ed. 2009.

4.- Fennema, O.R. Química de los Alimentos. 4a edición. Ed. Acribia. 2019.

5.- Fennema's Food Chemistry, 5th edition, 2017. By: Srinivasan Damodaran; Damodaran, Srinivasan; Kirk L. Parkin. CRC Press. https://app.knovel.com/web/toc.v/cid:kpFFCE001G/viewerType:toc/root_slug:fennemas-food-chemistry?kpromoter=federation

6.- Sanchez de Medina F. Tratado de Nutrición. Tomo I: Bases fisiológicas y bioquímicas de la nutrición. 3ª edición. Ed. Panamericana. 2017

 


Software

1) Páginas de Bioquimica y Biologia Molecular:

http://biomodel.uah.es/

2) Protein Purification (Dr Andrew Booth, University of Leeds, UK)

http://www.agbooth.com/pp_ajax/