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The quality of thermally induced aggregates of the globular proteins conalbumin, serum albumin, p-lactoglobulin and lysozyme has been examined at various salt concentrations and pH values. The properties of the aggregates were characterized by their dry matter content. The results are given as simple phase diagrams. The following areas of dry matter content were found: solubility; transparent and opaque gels (dry matter content of S-9%); precipitates (dry matter content above 9). Gels were formed only close to conditions of solubility. Only serum albumin was found to be a protein with good gelling properties. A small gelling area was registered for plactoglobulin, while no gelling was observed for conalbumin or lysozyme under the conditions examined. No common simple physical characteristic of the proteins used could be correlated to good gelling behavior.

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