Heat-induced aggregation and gelation of egg white protein

On heating, egg white proteins unfold, aggregate through intermolecular interactions of non-covalent and covalent bonds, and form networks to gel. Since the physical properties of egg white gel have a great influence on the texture of foods that use egg white, the control techniques and mechanisms have been extensively studied. In addition to conventionally known hydrophobic interactions and disulfide bonds, lanthionine and lysinoalanine bonds are deeply involved in the heat gelation of egg white. Recently, it was revealed that the covalent bonds are also involved in the formation of soluble aggregates on dry heat treatment of dried egg white. Controlling the formation of soluble egg white protein aggregates is considered a key factor in controlling the heat-induced gelation of egg whites. The aggregation and gelation properties have been studied using various methods, such as the Maillard reaction and electrochemical reaction.