Effect of Protein-Lipid-Salt Interactions on Sodium Availability in the Mouth and Consequent Perception of Saltiness: In Solutions

Date

2015-09-02

Author

Yücel, Umut
Peterson, Devin G.

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The influence of protein sodium interactions on the availability of sodium in the aqueous phase of liquid samples and consequently on the perception of saltiness was investigated. The aqueous effluents of casein and casein emulsion salt solutions were monitored for sodium availability from a tongue column system. In the aqueous protein salt solutions, increasing the protein/salt ratio from 1:1 to 5:1 or 10:1 significantly decreased the initial salt concentration in the effluent and resulted in a higher salt concentration in the effluent over time. Sensory analysis was in agreement. Samples with increased protein were rated as having significantly lower initial saltiness and a higher salty aftertaste. However, when casein was formulated as an emulsion, the initial release of sodium in the effluent was enhanced (compared to nonemulsified protein). Increasing the emulsion interfacial area (more hydrophilic segments of the protein were structured into the aqueous phase) resulted in a higher salt concentration in the aqueous phase and greater perceived saltiness intensity. In summary, protein interactions, specifically ionic, were reported as food interactions that influence salt perception and provide a basis to develop higher flavor quality low-sodium food products.

Subject Keywords

Salt reduction, Protein-salt ionic interactions, Emulsions, Aftertaste, Sensory

URI

https://hdl.handle.net/11511/57732

Journal

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY

DOI

https://doi.org/10.1021/acs.jafc.5b02311

Collections

Department of Food Engineering, Article

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Citation Formats

U. Yücel and D. G. Peterson, “Effect of Protein-Lipid-Salt Interactions on Sodium Availability in the Mouth and Consequent Perception of Saltiness: In Solutions,” JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, pp. 7487–7493, 2015, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/57732.