Salt Fractionation Essay

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Discussion: The proteins solubility can be determine based on the salt concentration in the solution in a way that when the concentration is low, various charged groups on a protein molecule will be stabilized by the presence of salt. This actually attracts the protein into the solution and the solubility of protein is enhanced which is generally known as salting-in process. On the other hand, as the concentration of the salt increases, the point of maximum solubility of the protein is reached and cause the increase in salt concentration which suggest that there was less water available to solubilise the protein. As the water interaction become less marked, the protein-protein interactions became more important causing the protein to aggregate and come out of solution. This protein precipitation in the presence of excess salt is also known as salting-out process. In this experiment, ammonium sulphate was used for the salt fractionation process. Ammonium sulphate was used especially for salt fractionation due to its high solubility and it is relatively inexpensive. Enzyme purification can also be carried out by following the same set of methodology as those for protein since enzyme is protein. However, some attention such as permanent loss of activity must be put into consideration due to denaturation under unfavourable conditions. In the first procedure, saturated salt solution was added slowly to the protein mixture to bring up the concentration of the salt of the mixture. The precipitated protein was collected and categorized based on the concentration of the salt solution at which it is formed in which it is called as fractionation. As a result, the protein fractions that were collected at the earlier stages of addition of the salt are less soluble in the salt solution than the fractions that were collected later after that (Spadaro, 2003). This can be seen from

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