|Teaching method||Contact hours|
|Course coordinator(s)||DC Swarts|
|dr. ir. JJM Vervoort|
|Lecturer(s)||dr. ir. JJM Vervoort|
|dr. MCR Franssen|
|dr. MCR Franssen|
|dr. ir. JJM Vervoort|
Language of instruction:
Assumed knowledge on:
BIC-10306 Practical Biological Chemistry; MIB-10306 Microbiology & Biochemistry.
Note: This course has a maximum number of participants. The deadline for registration is one week earlier than usual.
See Academic Year.(http://www.wur.nl/en/Education-Programmes/Current-Students/Agenda-Calendar-Academic-Year.htm) -> Registration for Courses.
The Enzymology course comprises: a) principles of enzymatic catalysis (20 lectures + ICT practical) and b) isolation, purification and initial characterization of enzymes (2-week intensive practical course).
The most important principles in homogenic and enzymatic catalysis are reviewed in 20 lectures. The following subjects are covered: biocatalysis, acid-base and nucleophilic catalysis, metal-ion catalysis, enzyme basic concepts, enzyme kinetics, enzyme inhibition, biocatalytic and regulatory strategies, cofactor-dependent catalysis and enzyme dynamics. These subjects are illustrated by a number of enzymes and enzymatic reactions. Principles of enzyme kinetics are explained in an ICT-practical (4 hours). This biocatalysis module is concluded with an exam; the mark for the exam is increased with 0.5 point, if the ICT-practical has been concluded successfully, provided the mark for the exam is 5.5 or higher.
Study of an enzyme catalytic mechanism requires a very high degree of purity of the respective enzyme. The practicals comprise isolation and purification of enzymes from cells or tissues, based on their physico-chemical properties. During the practicals, groups of 2 - 3 students purify 2 enzymes with precipitation methods and different chromatographic techniques (gel filtration, ion-exchange chromatography, bio-affinity chromatography, hydrophobic interaction chromatography). Initial characterization of the purified enzymes (size, subunit composition) is performed as well.
Principles of protein purification are explained in 5 lectures. At the end of the practical course, students present their results in PowerPoint presentations. The practicals are concluded with a practical test. The mark for the practicals is composed of a mark for performance during the practicals and the results obtained (judgments of assistants, PowerPoint presentations, 50%) and the mark for the practical test (50 %).
The maximal capacity for this course is 96 students, both in periods 3 and 6. Students for which this course is compulsory or restricted optional will be admitted with priority.
After successful completion of this course students are expected to:
- have knowledge on and insight into the chemical principles of enzyme catalysis, including cofactor chemistry;
- have insight in the action of enzymes as biocatalysts and in factors that influence enzyme activity;
- understand the kinetics of enzymatic reactions;
- be aware of the influence of enzyme structure on catalytic properties;
- have experience with purification, handling and characterization of proteins;
- have insight in the physico-chemical properties of proteins that underlie purification methods.
- attending lectures;
- studying readers;
- performing experiments and analysing results.
The final mark for Enzymology is composed of the following partial marks:
- a mark for the exam (open questions) on the Biocatalysis unit (50% of the final mark; minimal mark 5.5); this mark is increased with 0.5 bonus upon successful completion of the ICT-practical, provided the mark for the exam is 5.5 or higher
- a mark for performance and results obtained during the practicals on enzyme purification (judgments of assistants, PowerPoint presentation: 25% of the final mark; minimal mark 5.5)
- a mark for the test (open questions) on the theory of enzyme purification (25% of the final mark; minimal mark 5.5).
Reader Enzymology (available at WUR-shop).
Reader and manual for the practical course Enzymology (available at WUR-shop).
Berg, J.M.; Tymoczko, J.L.; Stryer, L.; [et.al]. (2012). Biochemistry. 7th ed. New York, NY [etc.], US: Freeman. (See Blackboard for chapters to be studied.)
PowerPoint presentations of the lectures will be made available on the Blackboard site.
|BML||Molecular Life Sciences||BSc||3WD|
|Compulsory for:||WUBIT||BSc Minor Biotechnology||6WD|