Title: Purification of Egg white protein

Name: Michael Johnson
Partner: David Logad & Nandita
Date: 2nd – 9th September 2004
Group: Thursday 11:30am - 3:30pm

Introduction
Salting Out
In 1888 Hofmeister that it can be possible to dehydrate a protein by adding salt to the solution, salting out. When a protein in a aqueous solution it is surrounded by water, in fact there can be up to 0.35g of water tightly bound to 1g of protein (Simpson 2004).
Also the effectiveness of the salting out can be affected by the type of salt used. This is because of the charge the salt can bring on the protein making it either likely or less likely interacted with water.
"The protein structure can also have an affect with it hydophobicity with hydrophobic patches on it (caused by the side chains Phe, Tyr, Leu, Ile, Met & Val). So the optimum salt is one that will cause hydration of the polar regions and dehydration of the hydrophobic regions of the protein. With which the salt does not......

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Title: Purification Of Egg White Protein
Approximate Word Count: 4310
Approximate Pages: 18 (250 words per double-spaced page)

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