SUMMARY— Egg white, near its normal concentration, was reacted at 25°C, pH 9.0, with levels of 3,3‐dimethylglutaric anhydride (DMGA) from 0 to 60 mol/mol egg white protein (EWP) (assuming egg white to have an average mol wt of 50,000). Analysis for amino acids and functional groups showed about 26% of the lysine residues reacted at 15 mol DMGA/mol EWP. Sulfhydryls are more resistant to reaction with 60% unreacted at 150 mol DMGA/mol EWP. Electrophoresis indicates significant changes in net charges on the protein, particularly on lysozyme which migrates anodically in six separate bands at higher DMGA levels. Ultracentrifugation sedimentation data suggest no hydrolysis or aggregation changes. Foam formation is not seriously altered, but the heat coagulation properties, as evidenced by angel cake failures, are changed. As measured by viscosity, light transmission and aerating ability, DMGA exerts a protective action against the effect of heat on these properties.

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SUMMARY– When egg yolk is dried and subsequently rehydrated, it loses its ability to form a stable foam. If sufficient carbohydrates are added to the egg yolk before dehydration, much of the foaming ability is retained by the rehydrated yolk. Evidence has been presented that, in plain‐dried yolk, the removal of water irreversibly changes the structure of the low‐density lipoproteins and that foam‐inhibiting free lipid is released from these lipoproteins. When yolk is co‐dried with added carbohydrates, the carbohydrates partially protect the lipoproteins from this irreversible structural change, probably by replacing the water of hydration at its binding sites during the drying process.