Thesis final - after defense-7 - Jacobs University

Chapter 4
additional understanding of the protein contaminants present in the yeast cell proteome
and is a valuable addition to the proteomics technology.
• Several important enzymes have been identified which were eluted at specific salt
concentrations. These enzymes can be purified by a single isocratic chromatography
without going through trial and error chromatographies to figure out the elution
position of any enzyme.
4.6. Recommendations for future work
• The average protein properties derived from the primary structure need to be explored
in reverse phase chromatography with the process proteomics approach.
• The average polarity parameter can be calculated from the surface residues of the three
dimensional structure of a protein. This average surface polarity can be used as an
alternative parameter to ASH.
• The adsorbent such as Toyopearl-Ether revealed an interesting chromatographic
behavior and can be used in future for the purification of the recombinant proteins of
highly hydrophobic nature.
• This approach can be extended to other hydrophobic adsorbents and expression
systems such as E.coli, mammalian cells and insect cells for the development of
downstream processing.
• This work involved the analysis of a real expression host instead of using model
proteins and the data obtained can be used to design a purification model for the
recombinant proteins utilizing an in silico approach.
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