Abstract
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.
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