Rafik Hariri philanthropic and developmental contributions are countless. The most remarkable being the multifaceted support to educate more than 36,000 Lebanese university students within Lebanon, and beyond.
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HYDROPHOBIC BEHAVIOR OF FIVE MODEL PROTEINS IN CHROMATOGRAPHY, PRECIPITATION, AND AQUEOUS TWO-PHASE SYSTEMS
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Fatima M. HACHEM
|
Univ. |
Reading |
Spec. |
Food Science |
Deg. |
Year |
#Pages |
|
Ph.D. |
1992 |
189 |
Proteins are used in many different industries such as the food, feed, pharmaceutical, cosmetics, paints to mention just a few. The level of purity of a protein is determined by the function it is going to play with some applications being more stringent in purity requirements than others. As proteins are normally present in mixtures, some separation and purification steps are necessary in their isolation. Over the years, methods to separate and purify proteins have improved which made it possible for the pharmaceutical industry, for instance, to obtain protein of high purity. Separation techniques vary among those exploiting the size of proteins, to those exploiting their density, solubility, charge, hydrophobicity or a combination of some of them.
In one of the promising separation techniques; aqueous two‑phase systems (ATPS), partitioning of a protein between two phases depends on factors related to the protein itself and to the system employed. Although over the last two decades our understanding of factors affecting separation in ATPS has improved, basic research is still needed in order to explain the importance of factors such as the charge and the hydrophobicity of proteins in determining their partitioning.
Therefore the objectives of this study are:
- To compare different established methods for measuring the hydrophobicity of proteins.
- To study the effect of the hydrophobicity of proteins on their partitioning in different aqueous two‑phase system.
- To research a predictive correlation for increasing partitioning of proteins in aqueous two‑phase systems based on their hydrophobicity.
In the first chapter, hydrophobicity is defined in relation to the protein structure. In the second, methods for measuring hydrophobicity are reviewed. In the third, chromatography is used for measuring the hydrophobicity of five model proteins. In the fourth, hydrophobicity of proteins is determined by precipitation caused by the addition of salt, and in the fifth, the hydrophobicity values derived from the previous techniques are related to the partitioning of proteins in aqueous two‑phase systems.
