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Course Unit Title Course Unit Code Type of Course Unit Level of Course Unit Year of Study Semester ECTS Credits
Basic Methods In Enzyme Purification KIM507 Elective Master's degree 1 Fall 8

Name of Lecturer(s)

Prof. Dr. Yonca DUMAN
Prof. Dr. Neslihan ŞAKİ
Associate Prof. Dr. Mustafa Oğuzhan KAYA

Learning Outcomes of the Course Unit

1) Making planning and strategy in enzyme purification.
2) Doing cell disintegration and extraction of intracellular enzymes,
3) Making enzyme purification with various chromatographic and electrophoretic methods.
4) Comment on some applications for enzyme purifications.
5) Discuss application areas of purified enzymes.

Program Competencies-Learning Outcomes Relation

  Program Competencies
1 2 3 4 5 6
Learning Outcomes
1 High High High High High High
2 High High High High High High
3 High High High High High High
4 High High High High High High
5 High High High High High High

Mode of Delivery

Face to Face

Prerequisites and Co-Requisites

None

Recommended Optional Programme Components

Enzymology

Course Contents

This course provides candidates with profound knowledge on planning and strategy in enzyme purification, methods for cell disintegration, methods for extraction of intracellular enzymes, methods for concentrations of enzyme extracts, principles of enzyme purification based on structural properties, adsorbtion techniques used on enzyme purification, ion exchange and hydrophobic interaction chromatographies, enzyme purification by affinity techniques, enzyme purification based on molecular size, other chromatographic techniques used in enzyme purification, electrophoretic methods in enzyme purification, establishment of enzyme purification profiles, and some applications for enzyme purifications.

Weekly Schedule

1) Planning and strategy in enzyme purification
2) Methods for cell disintegration
3) Methods for extraction of intracellular enzymes
4) Methods for fractionel precipitationof enzyme extracts,
5) Principles of enzyme purification based on structural properties
6) Principles of enzyme purification based on structural properties
7) Adsorbtion techniques used on enzyme purification
8) Midterm examination/Assessment
9) Ion exchange and hydrophobic interaction chromatographies
10) Enzyme purification by affinity techniques
11) Enzyme purification based on molecular size
12) Other chromatographic techniques used in enzyme purification
13) Electrophoretic methods in enzyme purification
14) Establishment of enzyme purification profiles
15) Some applications for enzyme purifications
16) Final examination

Recommended or Required Reading

1- D. Voet, J. G. Voet, Biochemistry, John Wiley & Sons, 3rd USA., 2004
2- E. L. V. Harrison & S. Angol Eds., Protein Purification Applications – A Practical Approach, IRL Press, 1990.
3- R. K. Skopes, Protein Purification – Principles & Practice, Springer Verlag, 1993.

Planned Learning Activities and Teaching Methods

1) Lecture
2) Discussion
3) Demonstration
4) Group Study
5) Problem Solving


Assessment Methods and Criteria

Contribution of Midterm Examination to Course Grade

40%

Contribution of Final Examination to Course Grade

60%

Total

100%

Language of Instruction

Turkish

Work Placement(s)

Not Required