Ligand and Flavor Binding Functional Properties of β‐Lactoglobulin in the Molten Globule State Induced by High Pressure
Jian Yang, Joseph R. Powers, Stephanie Clark, A. Keith Dunker, Barry G. Swanson
Journal of Food Science
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.
Extracted Claims
6 claims extracted from this paper into the knowledge graph
β‐lactoglobulin (β‐LG) in the molten globule state less affinity palmitic acid, capsaicin, or carvacrol ligands
“The HHP‐induced molten globule state of β‐LG exhibited less affinity for palmitic acid, capsaicin, or carvacrol ligands than native β‐LG”
β‐lactoglobulin (β‐LG) in the molten globule state no detectable specific binding α‐ionone, β‐ionone, cinnamaldehyde or vanillin flavors
“and no detectable specific binding for α‐ionone, β‐ionone, cinnamaldehyde or vanillin flavors.”
high hydrostatic pressure (HHP) treatment resulted in changes hydrophobic calyx and surface hydrophobic sites of β‐LG
“HHP treatment resulted in changes in the hydrophobic calyx and surface hydrophobic sites of β‐LG.”