Ligand and Flavor Binding Functional Properties of β-Lactoglobulin in the Molten Globule State Induced by High Pressure |
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| Authors: | J. Yang J.R. Powers S. Clark A.K. Dunker B.G. Swanson |
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| Affiliation: | Author Yang is with College of Agriculture and Life Science, Univ. of Guam, Mangilao, Guam.;Author Dunker is with Dept. of Biochemistry and Biophysics, Washington State Univ., Pullman, Washington.;Authors Powers, Clark, and Swanson are with Dept. of Food Science and Human Nutrition, Washington State Univ., Pullman, WA 99164-6376. |
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| 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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| Keywords: | β-lactoglobulin high pressure molten globule hydrophobic probes flavor |
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