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Module Specifications

Archived Version 2007 - 2008

Module Title Bioseparations
Module Code BE516
School School of Biotechnology

Online Module Resources

Module Co-ordinatorProfessor Ian W. MarisonOffice NumberX2 09
Level 5 Credit Rating 5
Pre-requisite None
Co-requisite None
Module Aims

The aim of this module is to

  • provide a detailed understanding of the behaviour of proteins in solution and how their properties may be altered by changing the physical surroundings.
  • provide an understanding of the theory and practical techniques involved in developing a purification process


Learning Outcomes

1. Understand the principles of protein chemistry in solution.

2. Design a DSP process which is readily integrated with the USP

3. Decide how to choose the correct separation and chromatographic techniques.

4. Understand the theory and practice of chromatography and how this can help in designing the DSP.

5. Comprehend the different types of chromatographic equipment and how they operate



Indicative Time Allowances
Hours
Lectures 18
Tutorials
Laboratories 2
Seminars
Independent Learning Time 55

Total 75
Placements
Assignments
NOTE
Assume that a 5 credit module load represents approximately 75 hours' work, which includes all teaching, in-course assignments, laboratory work or other specialised training and an estimated private learning time associated with the module.

Indicative Syllabus
This 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.
Assessment
Continuous Assessment100% Examination Weight0%
Indicative Reading List

Protein Purification – Principles & Practice – Robert K. Scopes 3rd Edition (1994)/Springer Verlag

Bioseparations Downstream Processing for Biotechnology – Paul Belter, E.L. Cussler, Wei-Shou Hu - (1988)/John Wiley & Sons

Lecturers Notes

Programme or List of Programmes
SMPSCSingle Module Professional Science
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