β-Lactoglobulin (β-LG) is a globular whey protein with distinct physicochemical properties: a hydrophobic β-barrel, amphiphilic character, and sensitivity to pH, ionic strength, and heat. These properties enable ligand binding, conformational rearrangement, and self-assembly into nanostructures, making it a promising food-grade nanocarrier for bioactive compounds due to its biocompatibility, biodegradability, and structural versatility. This review critically addresses the gap between laboratory potential and industrial translation through three interconnected pillars: (1) chemical mechanisms of β-LG nanocarrier formation (self-assembly, cross-linking); (2) stimuli-responsive engineering, distinguishing native pH/enzyme sensitivity from engineered release behavior; (3) scalable manufacturing (e.g., microfluidics). Key limitations (instability, allergenicity, high purification cost, poor hydrophilic compound loading) and future directions (protein engineering, recombinant production, computational design, active targeting) are also discussed to facilitate translation to practical applications.
