Characterization of Sodium Mobility and Binding by 23Na NMR Spectroscopy in a Model Lipoproteic Emulsion Gel for Sodium Reduction

Kyle S. Okada, Youngsoo Lee

Research output: Contribution to journalArticle


The effects of formulation and processing parameters on sodium availability in a model lipid/protein-based emulsion gel were studied for purposes of sodium reduction. Heat-set model gels were prepared with varying levels of protein, lipid, and NaCl contents and high pressure homogenization treatments. Single quantum and double quantum-filtered 23Na NMR spectroscopy experiments were used to characterize sodium mobility, structural order around “bound” (restricted mobility) sodium, and sodium binding, which have been correlated to saltiness perception in food systems previously. Total sodium mobility was lower in gels with higher protein or fat content, and was not affected by changes in homogenization pressure. The gels with increased protein, fat, or homogenization pressure had increased structure surrounding “bound” sodium and more relative “bound” sodium due to increased interfacial protein interactions. The data obtained in this study provide information on factors affecting sodium availability, which can be applied towards sodium reduction in lipid/protein-based foods.

Original languageEnglish (US)
Pages (from-to)1563-1568
Number of pages6
JournalJournal of food science
Issue number7
StatePublished - Jul 2017


  • Na NMR spectroscopy
  • lipoproteic gels
  • sodium mobility
  • sodium reduction

ASJC Scopus subject areas

  • Food Science

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