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Characterization of Sodium Mobility and Binding by 23 Na NMR Spectroscopy in a Model Lipoproteic Emulsion Gel for Sodium Reduction
Author(s) -
Okada Kyle S.,
Lee Youngsoo
Publication year - 2017
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/1750-3841.13750
Subject(s) - sodium , homogenization (climate) , chemistry , emulsion , analytical chemistry (journal) , chromatography , biochemistry , organic chemistry , biodiversity , ecology , biology
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.