Module Specifications..
Current Academic Year 2023 - 2024
Please note that this information is subject to change.
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Repeat examination Repeat MCQ exam in August. |
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Description The aim of this module is three-fold: 1. To provide the student with a thorough understanding of analytical and prep scale chromatography in both the characterisation and purification of biologics and biotherapeutics. 2. To provide a detailed understanding of the behaviour of proteins in solution and how their properties may be altered by changing the physical surroundings. 3. To provide an understanding of the theory and practical techniques involved in developing a purification process. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Learning Outcomes 1. Gain advanced knowledge of the principles of protein chemistry in solution. 2. By using specialised tools and techniques of enquiry, design a DSP process which is readily integrated with the USP 3. Gain systematic understanding to choose the correct separation and chromatographic techniques. 4. Demonstrate a systematic understanding of the theory and practice of chromatography and other separation methods and how this can help in designing the DSP. 5. Gain critical awareness of the different types of chromatographic equipment and how they operate | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
All module information is indicative and subject to change. For further information,students are advised to refer to the University's Marks and Standards and Programme Specific Regulations at: http://www.dcu.ie/registry/examinations/index.shtml |
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Indicative Content and Learning Activities
BioseparationsThis module is built on the fundamental concepts of protein structure and function, physical chemistry of solutions and electrolytes/acids/bases and pH to understand how proteins behave in solution and how their properties may be altered by changing the physical surroundings. Using examples, descriptions will be given as to how to isolate proteins from inclusion bodies or culture medium using a range of chemical and physical separation processes. The principles of developing a purification process, including theory, will be defined using a wide range of chromatographic techniques including, but not exclusive to; gel filtration, ion-exchange, hydrophobic interaction, reverse phase, metal chelate, immunoaffinity and other affinity- based techniques, microfiltration and others. The different types of equipment, fluidized versus packed-beds and how these may be scaled-up will be discussed. This module will provide the student with (1) a thorough understanding of analytical and prep scale chromatography in both the characterisation and purification of biologics and biotherapeutics, (2) a detailed understanding of the behaviour of proteins in solution and how their properties may be altered by changing the physical surroundings, and (3) an understanding of the theory and practical techniques involved in developing a purification process. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Indicative Reading List
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Other Resources None | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Programme or List of Programmes
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| Date of Last Revision | 10-MAR-11 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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