Characterization of Sodium Mobility and Binding by (23) Na NMR Spectroscopy in a Model Lipoproteic Emulsion Gel for Sodium Reduction.
Related Articles Characterization of Sodium Mobility and Binding by (23) Na NMR Spectroscopy in a Model Lipoproteic Emulsion Gel for Sodium Reduction.
J Food Sci. 2017 May 27;:
Authors: Okada KS, Lee Y
Abstract
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 (23) Na 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.
PMID: 28556249 [PubMed - as supplied by publisher]
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