Food Chemistry
The aggregation of denatured protein molecules into an insoluble network, following denaturation and driven by newly exposed hydrophobic groups.
Why beating and heating egg whites turns a runny liquid into a firm meringue or omelette.
Loss of a protein's secondary, tertiary and quaternary structure without breaking peptide bonds, caused by heat, pH change, salts, solvents or shear.
The pH at which a protein carries no net electrical charge, so electrostatic repulsion between molecules is minimal.
The main phosphoprotein of milk, about 80% of milk protein, existing as micelles stabilised by κ-casein. Precipitates at pH 4.6 or on rennet action.
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