Beta-lactoglobulin is a typical member of the lipocalin family.

The overall shape of beta-lactoglobulin is characteristic of the lipocalin family.

Beta-lactoglobulin was found to have a role in the transport of hydrophobic ligands such as retinol or fatty acids.

In addition to the immune response to beta-lactoglobulin and casein, the fate of an unrelated dietary antigen, gliadin, was studied.

HB plots of the open and closed forms of beta-lactoglobulin are very similar, all unique motifs can be recognized in both forms.

One of the main structural differences with beta-lactoglobulin is that it does not have any free thiol group that can serve as the starting-point for a covalent aggregation reaction.

Fukushima Y, Kawata Y, Onda T, Kitagawa M. Long-term consumption of whey hydrolysate formula by lactating women reduces the transfer of beta-lactoglobulin into human milk.

Using RNA interference scientists have produced a cow whose milk contains increased amounts of casein, a protein used to make cheese and other foods, and almost no beta-lactoglobulin, a component in milk whey protein that causes allergies.

The structure of beta-lactoglobulin reveals that the barrel-form structure with the central cavity of the protein has an "entrance" surrounded by five beta-loops with centers around 26, 35, 63, 87, and 111, which undergo a conformational change during the ligand binding and close the cavity.