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Beta-lactoglobulin (BLG) is the primary whey protein found in the milk of cows and other ruminants, though it is notably absent from human breast milk [1]. It belongs to the lipocalin family of proteins, which are characterized by a conserved eight-stranded beta-barrel structure that forms a central hydrophobic pocket, or calyx, designed to bind and transport small lipophilic molecules such as retinol, fatty acids, and vitamin D [3]. While its exact physiological function in the neonate is not fully elucidated, it is believed to assist in the digestion of milk lipids and the transfer of passive immunity [1]. Clinically, bovine beta-lactoglobulin is significant as a major food allergen, designated as Bos d 5, and is a frequent cause of IgE-mediated cow's milk allergy in pediatric populations [2]. Due to its robust stability against acid denaturation and proteolysis, as well as its ability to bind various ligands, BLG is also utilized in pharmaceutical research as a versatile carrier for the oral delivery of hydrophobic drugs and bioactive compounds [3]. (Sources: [1] UniProt P02754; [2] Hochwallner et al., Methods 2014; [3] Kontopidis et al., J Dairy Sci 2004).
Acts as a carrier protein for small hydrophobic molecules by sequestering them within its central beta-barrel calyx; functions as a major allergen by inducing IgE-mediated hypersensitivity and mast cell degranulation.
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