Ligand and flavor binding functional properties of β-lactoglobulin in the molten globule state induced by high pressure

Abstract

β-lactoglobulin (β-LG) in the molten globule state induced by high hydrostatic pressure (HHP) at 500 MPa and 50°C for 32 min exhibited a significant decrease in affinity for retinol and a significant increase in affinity for cis-parinaric acid (CPA) and 1-anilino-naphthalene-8-sulfonate (ANS) compared to native β-LG. The number of β-LG binding sites for retinol and CPA significantly decreased after HHP treatment. The HHP-induced molten globule state of β-LG exhibited less affinity for palmitic acid, capsaicin, or carvacrol ligands than native β-LG, and no detectable specific binding for α-ionone, β-ionone, cinnamaldehyde or vanillin flavors. HHP treatment resulted in changes in the hydrophobic calyx and surface hydrophobic sites of β-LG.