Milk β-lactoglobulin, the major protein in whey protein, possesses a unique molecular structure that provides binding sites for many ligands, endowing it with versatile functional properties including gelation, emulsification, and foaming. Hence, it has a broad application prospect. This paper first introduces the molecular structure, ligand binding sites, gelation, emulsification, and foaming properties of β-lactoglobulin. Then, it discusses the effect of several main processing methods including heat treatment, high-pressure processing, pulsed electric field treatment, and ultraviolet radiation induction on the properties of β-lactoglobulin. Finally, it elucidates the application of β-lactoglobulin in food processing, nanomaterials and basic research, aiming to provide a theoretical and scientific reference for promoting the industrial application of β-lactoglobulin in the food industry and other related industries.

Cow’s milk is rich in protein, fat, and other high-quality nutrients, which is an important nutritional source for infants. On the other hand, milk protein is the main factor inducing food allergy in infants and young children. In this study, five kinds of commercially available infant milk powder were selected for static digestion in vitro. The digestive stability of proteins in the five kinds of milk powder was analyzed by electrophoresis and degree of hydrolysis measurement. An enzyme-linked immunosorbent assay (ELISA) was used to evaluate the antigenicity of whey protein in milk powder. The results showed that α-lactalbumin and β-lactoglobulin showed good digestive stability in samples 1, 2, and 4. After gastrointestinal digestion, the antigenicity of α-lactalbumin and β-lactoglobulin decreased in sample 1 but increased in sample 2. The antigenicity of α-lactalbumin increased, while that of β-lactoglobulin decreased in sample 4. Both allergens had lower digestion stability in sample 3 and 5. The antigenicity of α-lactalbumin and β-lactoglobulin increased in sample 5. The antigenicity of α-lactalbumin increased while that of β-lactoglobulin decreased in sample 3.