BIC-20806 Enzymology


Studiepunten 6.00

Independent study0
Course coordinator(s)DC Swarts
dr. ir. JJM Vervoort
Lecturer(s)DC Swarts
dr. ir. JJM Vervoort
dr. MCR Franssen
Examiner(s)DC Swarts
dr. ir. JJM Vervoort
dr. MCR Franssen

Language of instruction:


Mandatory knowledge:

ZSS06100 Laboratory Safety

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.( -> 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.

Learning outcomes:

After successful completion of this course students are expected to able to:
- understand the chemical principles of enzyme catalysis, including cofactor chemistry;
- show insight in the action of enzymes as biocatalysts and in factors that influence enzyme activity;
- understand the kinetics of enzymatic reactions;
- show awareness of the influence of enzyme structure on catalytic properties;
- show experience with purification, handling and characterization of proteins;
- show 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.; []. (2012). Biochemistry. 7th ed. New York, NY [etc.], US: Freeman. (See Brightspace for chapters to be studied.)
PowerPoint presentations of the lectures will be made available on Brightspace.

Verplicht voor: BBTBiotechnologyBSc6WD
BMLMolecular Life SciencesBSc3WD
Verplicht voor: WUBITBSc Minor Biotechnology6WD