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

J. Yang, J. R. Powers, S. Clark, A. Dunker, B. G. Swanson

Research output: Contribution to journalArticle

25 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)444-452
Number of pages9
JournalJournal of Food Science
Volume68
Issue number2
StatePublished - Mar 2003
Externally publishedYes

Fingerprint

lactoglobulins
norisoprenoids
Lactoglobulins
Hydrostatic Pressure
high pressure treatment
functional properties
vitamin A
flavor
Norisoprenoids
Ligands
Pressure
capsaicin
naphthalene
carvacrol
sulfonates
vanillin
acids
calyx
Vitamin A
palmitic acid

Keywords

  • β-lactoglobulin
  • Flavor
  • High pressure
  • Hydrophobic probes
  • Molten globule

ASJC Scopus subject areas

  • Food Science

Cite this

Ligand and flavor binding functional properties of β-lactoglobulin in the molten globule state induced by high pressure. / Yang, J.; Powers, J. R.; Clark, S.; Dunker, A.; Swanson, B. G.

In: Journal of Food Science, Vol. 68, No. 2, 03.2003, p. 444-452.

Research output: Contribution to journalArticle

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