Chemical and physical lipophilization of proteins

With a view to enhance the amphipathic nature of food proteins, chemical and physical modification were carried out. Soy glycinin and α S1 ‐casein were lipophilized by chemically attaching naturally occurring fatty acids to them. The covalent attachment of fatty acyl residues to these proteins caused an increase in their emulsification activity. Soy proteins and the maize protein, zein, were associated with soy lecithin and phosphatidate, respectively, by sonication. The emulsification activity of phospholipid‐protein complexes was greatly increased after they were treated with 50% ethanol or enzyme digestion.