Abstract: In this paper, the effect of heat treatment on the denaturation of α-lactalbumin (α-La) and its interaction with other milk protein components as well as the influencing factors are reviewed. The thermal stability of α-La can be affected by Ca2+ binding. It cannot self-aggregate after denaturation, but can form aggregates with β-lactoglobulin (β-Lg) and serum albumin (SA). Aggregates of α-La/β-Lg produced by high temperature short time (HTST) treatment can be used to produce protein drinks with low viscosity, low turbidity and high solubility. Aggregates of α-La/SA have a good gel structure. α-La/β-Lg aggregates can also combine with κ-casein on the surface of casein micelles, forming polymers that are beneficial to shorten the fermentation process and improve the gel structure of yogurt. The combination of α-La with immunoglobulin G allows reduced allergenicity of milk with HTST, ultra-pasteurization and ultra-high temperature treatments. A suitable heat treatment should be selected in practice to improve the production efficiency.

Key words: α-lactalbumin, heat treatment, thermal denaturation, interaction, application