| Responsible Department | Department of Basic Science and Environment | ||||||||||||||
| Duration | One block | ||||||||||||||
| Credits | 7.5 (ECTS) | ||||||||||||||
| Level of Course | MSc | ||||||||||||||
| Examination | Final Examination written examination and oral examination All aids allowed Description of Examination: Evaluation of reports of performed experiments supplemented with individual oral presentation and examination Weight: Oral examination in project report and pensum is judged by 100 % 7-point scale, internal examiner | ||||||||||||||
| Requirement for Attending Exam | Submission and approval of at least 75 % of project reports | ||||||||||||||
| Organisation of Teaching | The course consist of a combined theoretical part (lectures and theoretical exercises; approx. 4 h per week) and practical laboratory work (approx. 9 h per week) with traditional and new advanced methods of analyses used in work with biomolecules | ||||||||||||||
| Block Placement | Block 2 Week Structure: A | ||||||||||||||
| Language of Instruction | English | ||||||||||||||
| Optional Prerequisites | 230002 Biochemistry 1 | ||||||||||||||
| Restrictions | The number of students per course is limited to 30 owing to limited space in the laboratories and the teaching in use of advanced instrumentation. | ||||||||||||||
| Course Content | |||||||||||||||
| The course comprises the theoretical and experimental work on enzymes, proteins and peptides in biological matrices. Focus is placed on experimental and theoretical understanding of the relations between structure and properties of the molecules. Topics includes are: Extraction techniques Chromatographic systems Solvent and buffer relations where effects of ions, organic molecules, and surfactants play a significant role. The combinations of such knowledge give the students basis for understanding and development of a relevant strategy of methods as used in analytical biochemistry. The students will in selected projects work with both traditional and new actual /advanced biochemical methods and techniques. Strategies to efficient isolation, purification and characterisation of biomolecules, bioactive proteins, peptides, and enzymes from complex biological systems Determination of kinetic parameters, Vmax, KM and kcat, and interpretation of such data in relation to ideal catalytic effects Characterisation of antibodies and their use in immunochemical methods Thermodynamics and kinetics in enzymology and biochemical analyses Binding between molecules in equilibrium reactions and thermodynamic stable complexes Receptor and effector sites, positive (activators) and negative effectors (inhibitors) and their effects on the active sites Native enzymes: holoenzymes, apoenzymes, co-factors, activation energy and kinetics Design and use of enzymatic assays A project with individual final reporting is a part of the course where the students in a group of 2-3 persons perform purification of a selected enzyme or inhibitor. | |||||||||||||||
| Teaching and learning Methods | |||||||||||||||
| Lectures and theoretical exercises: lectures will be used to present the theoretical background for the subjects considered with at least 3 hours per week. The lectures will be followed by theoretical exercises (1 h per week) where the students in groups of three will work on answers of specific questions related to the theory and practical use of methods and technology. Laboratory work with knowledge to theory and practical use of the various instruments and biochemical methods are central parts of the course. The students will be in groups of three and spend about 9 hours per week with this part of the course. Three weeks will be devoted to the project focused on studies of a selected enzyme or inhibitor molecule. The combined theoretical and practical laboratory experiments with focus on strategies of methods in analytical biochemistry and enzymology will train the students in calculations on the produced data. | |||||||||||||||
| Learning Outcome | |||||||||||||||
| The course provides a thorough and fundamental theoretical and practical basis for knowledge to and work with biomolecules, especially bioactive proteins, peptides, and enzymes occurring in complex biological matrices, plant, animal and microbial based feed and food. Focus is placed on the relations between structure and properties of biomolecules, strategies in use of actual new and traditional biochemical methods and understanding of the descriptions in original scientific papers. After completing the course the student should be able to: Knowledge: Reflect about physico-chemical-biochemical properties of biomolcules and especially enzymes. Describe strategies to efficient isolation and purification of enzymes from complex biological systems Describe analytical techniques used in biochemistry and for enzyme characterisation. Understand the theoretical basis for changes of water as solvent, extraction and chromatographic systems in work with molecules of different polarity. Skills Evaluate the detection, quantification and linearity of experimental data in relation to published values (literature data). Design experimental stategies in analytical biochemistry and enzymology based on structure and properties of analytes in complex matrix systems. Apply theoretical principles of analytical biochemistry to carry out experimental isolation and purification of enzymes Evaluate the performance of applied techniques in an enzyme related project carried out in a group (preferably 2-3 persons). Competences Cooperate with a fellow student on laboratory reports and a project report Expand the knowledge to biochemistry by use of mathematics evaluations Utilise the obtained knowledge in more comprehensive projects within research, development or industry. | |||||||||||||||
| Course Literature | |||||||||||||||
| R.K. Scopes (1994): Protein purification. Principles and Practice. Springer-Verlag New York Berlin Heidelberg (ISBN 0-387-94072-3) H.Sørensen, S.Sørensen, C.Bjergegaard, S.Michaelsen (1999): Chromatography and Capillary Electrophoresis in Food Analysis. Royal Society of Chemistry, Cambridge, UK. (ISBN 0-85404-561-9)(selected parts will be copied for the students) Selected scientific literature relevant for projects | |||||||||||||||
| Course Coordinator | |||||||||||||||
| Jens Christian Sørensen, jchs@life.ku.dk, Department of Basic Sciences and Environment/Biochemistry & Natural Product Chemistry, Phone: 353-32435 | |||||||||||||||
| Study Board | |||||||||||||||
| Study Committee NSN | |||||||||||||||
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