Protein-Flavor Interactions in Food Systems

The interplay between proteins and flavour compounds in food systems is central to sensory perception and product development. Proteins can bind, retain or release volatile molecules through a balance of hydrophobic, electrostatic and hydrogen-bonding interactions. These interactions influence the volatility, stability and perception of flavours in diverse matrices, from meat emulsions to plant-based beverages. Processing parameters—such as thermal treatment, enzymatic modification and physical methods like ultrasound—alter protein conformation and surface properties, modulating their binding capacity. This dynamic binding and release underlies flavour retention during processing, release during mastication, and the temporal profile of flavour perception. A detailed understanding of protein-flavour interactions supports the design of foods with tailored sensory attributes, reduced off-notes and enhanced consumer appeal, while also enabling clean-label strategies by optimising natural protein sources and processing technologies.

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Protein-Flavor Interactions in Food Systems publication trend

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Technical terms

Hydrophobic interaction: Non-covalent association between non-polar regions driven by water exclusion.

Partition coefficient: Ratio of concentrations of a compound in two immiscible phases, indicating its relative solubility in each.

Fluorescence quenching: Reduction of fluorescent emission upon binding or proximity of a quencher molecule, used to assess binding affinities.

Headspace analysis: Measurement of volatile compounds in the gas phase above a sample to evaluate aroma release.

Proteolysis: Enzymatic cleavage of peptide bonds, resulting in changes to protein structure and binding properties.

References

1. Structural changes induced by ultrasound improve the ability of the myofibrillar protein to bind flavor compounds from spices. Ultrasonics Sonochemistry (2023).
2. Flavor-protein interactions for four plant proteins with ketones and esters. Heliyon (2023).
3. Drivers of the In-Mouth Interaction between Lupin Protein Isolate and Selected Aroma Compounds: A Proton Transfer Reaction–Mass Spectrometry and Dynamic Time Intensity Analysis. Journal of Agricultural and Food Chemistry (2024).