BIOMOLECULAR INTERACTIONS

Academic year
2019/2020 Syllabus of previous years
Official course title
BIOMOLECULAR INTERACTIONS
Course code
CM0539 (AF:316518 AR:170152)
Modality
On campus classes
ECTS credits
6
Degree level
Master's Degree Programme (DM270)
Educational sector code
BIO/13
Period
2nd Semester
Course year
2
This course is opened to understand and discuss bioseparation engineering of pharmaceutical proteins in downstream process of bioindustry. Production of biopharmaceuticals including monoclonal antibodies are currently recognized as key technologies in bioindustry and especially, in their purification processes, it would be essential to understand complicated phenomena of proteins, such as mass transfer, conformational change, diffusion and adsorption. Therefore, both theoretical and practical approaches would be necessary to establish robust, efficient and economical downstream process. Here, this course introduces basic and practical knowledges of protein separation at downstream process. Especially, chromatographic separation technologies of proteins based on biochemical engineering principle would be pointed out. The attendees of this course could understand how to operate chromatographic separation of proteins in industrial processes and handle several empirical equations for designing processes.
1. Knowledge and understanding
i) Knowing basis and role of bioprocess engineering, especially downstream processing of protein.
ii) Knowing theory and application of chromatographic separation of proteins.
iii) Knowing theory and application of biosensing of biomacromolecules using specific interacrtion.

2. Applying knowledge and understanding
i) Knowing how to calculate retention time on the basis of the knowledge of equilibration model in gel permeation chromatography
ii) Knowing how to calculate HETP and reduced HETP from the knowledge of chromatographic theory, and design a column for industrial use.

3. Making judgements
i)Being able to evaluate the logical consistency of the results to which the application of the learned bioseparation engineering knowledge and law is applied, both in the theoretical field and in the case of experimental data.
ii) Knowing how to recognize errors through a critical analysis of the applied method.

4. Communication
i) Knowing how to communicate the knowledge learned and the result of its application using appropriate terminology, both in oral and written form.
ii) Knowing how to interact with the teacher and with the classmates in a respectual and constructive way, especially during the experimental work carried out in a group.

5. Lifelong learning skills
i) Knowing how to take notes, selecting and collecting information according to their importance and priority.
ii) Being able to be sufficiently autonomous in the collection of experimental data.
For this course is not necessary to have any prerequisite
1. Introduction of bioseparation
Basis and importance of separation technologies in downstream processing of proteins are introduced. Separation technologies including membrane filtration, centrifugation and chromatography are explained. Also advantages and disadvantages of these technologies would be discussed.

2. Properties of biomacromolecules in downstream processing
Characteristics of biomacromolecules, especially, proteins regarding downstream processing are introduced. Basic properties, such as isoelectric point (pI), thermal stability, folding/unfolding, are explained.

3. Principles of protein chromatography
Basis and principle of chromatography for protein separation are explained. Retention mechanisms of gel-permeation chromatography, ion-exchange chromatography, hydrophobic interaction chromatography and affinity chromatography are introduced.

4. Size-exclusion chromatography
 Size-exclusion chromatography which is a separation method by difference of penetration ability into porous particles. In this class, theory and application of size-exclusion chromatography are introduced. The theory of equilibration model to estimate retention time and retention volume is explained, and this model would be applied to some examples of chromatograms.

5. Ion-exchange chromatography
Ion-exchange chromatography is widely utilized for separation between charged molecules by changing pH or concentration of electrolytes. Ion-exchange chromatography of proteins has been studied on the basis of mechanistic model with linear gradient elution (LGE). In this class, this mechanistic model is introduced to design operational condition in ion-exchange chromatography process.

6. Hydrophobic interaction chromatography
Hydrophobic interaction chromatography is one of popular chromatography for separation of proteins that were in middle of process. Proteins could be bound to the resins by van der Waals attraction at high concentration of salts, and the interaction become lower by decreasing salt concentration gradually. In this class, the basis and application of hydrophobic interaction chromatography is introduced.

7. Affinity chromatography
Affinity chromatography utilizing specific interactions of biomolecules such as DNA-DNA, DNA-RNA, antigen-antibody and ligand-receptor is a significantly important technique in downstream processing of proteins. In this class, affinity chromatographic methods using antibody-immobilized resins as well as protein A-immobilized resins are introduced. Also, advantages and disadvantages of affinity chromatography are discussed.

8. Biosensor and bioanalysis
Biosensing and bioanalysis of proteins are very important in bioprocess monitoring as well as
1. Biochemical Engineering 2nd edition: Shigeo Katoh, Jun-ichi Horiuchi, Fumitake Yoshida, Wiley
2. Protein Chromatography: Alois Jungbauer, Georgio Carta, Wiley


The expected method of verification of learning is written exams including some reports. Problems and some reports would be provided in each class, and scores taken in each class would be summated.
The professor will use face to face lessons.
English
written
Definitive programme.
Last update of the programme: 23/01/2020