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Functional aspects of blood plasma proteins 4. Elucidation of the mechanism of gelation of plasma and egg albumen proteins

1985; Wiley; Volume: 20; Issue: 4 Linguagem: Inglês

10.1111/j.1365-2621.1985.tb01959.x

1365-2621

Nazlin K. Howell, R.A. Lawrie,

Protein Interaction Studies and Fluorescence Analysis

Summary. The mechanism of gelation of plasma and egg albumen proteins in a cake‐type model system was elucidated by chemical modification, polyacrylamide gel electrophoresis and electron microscopy. It was demonstrated by chemical modification that gelation via disulphide bonds was predominant in all the plasma and egg albumen proteins. Hydrophobic and hydrogen bonds also prevailed in the plasma protein gels. In contrast the breakdown of hydrophobic and hydrogen bonds increased the strength of egg albumen gels. Electrophoretic characterization confirmed that most of the component proteins of plasma and egg albumen were modified chemically. Electron micrographs of the gels of plasma, egg albumen and a mixture of these proteins revealed a generally similar type of network structure, and indicated the compatibility of these proteins. The plasma gels had a more dense network, however, than the egg albumen gels and this was reflected in their correspondingly greater gel strength.