230006 Enzymology and Experimental Biochemistry

Details
Department of Natural Sciences
Earliest Possible Year
DurationOne block
 
Credits7.5 (ECTS)
Course LevelMSc
 
ExaminationFinal 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 ExamSubmission of at least 75 % of project reports
 
Organisation of TeachingThe course consist of a combined theoretical part (lectures and theoretical exercises; approx. 6 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 PlacementBlock 2
Week Structure: A
 
Teaching LanguageEnglish
may be conducted in Danish
 
Optional Prerequisites230002 Biochemistry 1
Biochemistry 1
 
RestrictionsThe number of students per course is limited to 30 owing to limited space in the laboratories and the teaching in use of advanced instrumentation.
 
Areas of Competence the Course Will Address
Basic Science:
Knowledge to physico-chemical-biochemical properties of biomolcules, bioactive proteins, peptides.
Comprehends analytical biochemistry and enzymology.
Comprehends the changes in thermodynamic constants to actual or practical constants as function of compounds changing the properties of pure water and diluted solutions.
Evaluate the detection, quantification and linearity of experimental data in relation to published values (literature data).
Applied Science:
Knowledge to development of strategy in analytical biochemistry and enzymology based on structure and properties of analytes in complex matrix systems.
Understand the theoretical basis for changes of water as solvent, extraction and chromatographic systems in work with molecules of different polarity.
Expand the knowledge to biochemistry by use of mathematics and statistical evaluations
Ethics and Values
Is aware of environmental, health and disease risks related to bioactive biomolecules
 
Course Objectives
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.
 
Course Contents
The course comprises the theoretical and experimental work associated with studies and uses of biomolecules as bioactive proteins, peptides, and enzymes occurring in biological matrices of plant, animal, and microbial origin. It is especially molecules of relevance for quality of feed, food, and non-food products,as well as those involved in metabolic regulations associated with health and diseases, and enzymes used in analyses and bioprocessing technologies. Focus is placed on understandings of the relations between structure and properties of the molecules, as well as the effects of ions, organic molecules and surfactants on the properties of water as solvent, extraction, and chromatographic systems. 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. This give possibilities for knowledge to and experiences in applied biochemical research, quality assurance, Good Laboratory Practice (GLP) etc as required in basic research laboratories, in biotech companies, industries, applied sector research institutes and control laboratories. The course gives knowledge to:
· Quality assurance including GLP in enzymology and experimental biochemistry
· The theoretical and experimental based knowledge to changes in water as solvent, extraction and chromatographic systems, as function of ions, organic modifiers and surfactant type and concentration
· Thermodynamics and kinetics in enzymology and biochemical analyses
· Binding between molecules in equilibrium reactions and thermodynamic stable complexes.
· Native enzymes: holoenzymes, apoenzymes, co-factors, activation energy and kinetics
· Receptor and effector sites, positive (activators) and negative effectors (inhibitors) and their effects on the active sites
· 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
· Knowledge to new and traditional biochemical methods and experimental experiences in use of such methods
· Use of enzymes in analytical methods, in feed, food and bioprocess technologies, in xenobiotic metabolism, and diagnose of health and disease effects
The individual projects for each course participant include use of original scientific literature, its interpretation, evaluation and discussion in relation to results obtained in the project.
 
Teaching And Learning Methods
Lectures and theoretical exercises: lectures will be used to present the theoretical background for the subjects considered with at least 2 hours per week and folowing the progress in the study program and experimental work. The lectures will be followed by theoretical exercises 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. The last 2/3 of the course period will be devoted to a larger project focused on studies of a defined bioactive molecule. The project on such a defined molecule is chosen among a selection of high molecular weight biomolecules, and agreed on by the student and the teacher. 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, statistical analyses of obtained results, performance of good laboratory practise (GLP), quality assurance, and reporting with evaluation of own data in relation to literature data.
 
Learning Outcome
Stipulated in "Areas of Competence the Course Will Address"
 
Course Litterature
B.W. Wenclawiak, M. Koch, W. Hadjicostas (Eds) (2004): Quality Assurance in Analytical Chemistry. Training and Teaching. Springer - Verlag, Berlin, Heidelberg. ISBN 3-540-40578-X.

L Buckberry & P. Tessdale (2001): Essenstials of Biological Chemsitry (udvalgte afsnit). John Wiley & Sons Ltd. West Sussex, UK (ISBN 0-471-48906-9)

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 scientific literature relevant for projects
 
Course Coordinator
Hilmer Sørensen, hils@life.ku.dk, Department of Natural Sciences/Biochemistry & Natural Product Chemistry, Phone: 35332432
Keld Ejdrup Andersen, kea@life.ku.dk, Department of Natural Sciences/Biochemistry & Natural Product Chemistry, Phone: 35332461
Jens Christian Sørensen, jchs@life.ku.dk, Department of Natural Sciences/Biochemistry & Natural Product Chemistry, Phone: 35332435
 
Study Board
Study Committee NSN
 
Course Scope
lectures20
theoretical exercises30
practicals70
preparation84
examination2

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