ArticleJournal of agricultural and food chemistry2023
Unraveling the Role of Flavor Structure and Physicochemical Properties in the Binding Phenomenon with Commercial Food Protein Isolates.
Article in Journal of agricultural and food chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 22 citations in OpenAlex.
- Drying-Induced Structural and Oxidative Transformations in Sustainable Proteins: Impact on Physicochemical Properties and Flavor-Binding Functionality.Foods (Basel, Switzerland) · 2026Review
- Sensory Properties and Aroma Compound Profiles of Pea Protein Isolates in Relation to High Hydrostatic Pressure and High-Pressure Homogenization Treatments.Food science & nutrition · 2026Article
- An in vitro study exploring the role of mucin in the protein-flavor binding mechanism.NPJ science of food · 2025Article
- Salivary emulsification shapes flavor release and perception in sturgeon caviar during oral processing.Food chemistry: X · 2025Article
- Effects of Roasting Level and Milk Addition onJournal of agricultural and food chemistry · 2025Article
- 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 · 2024Article
- Plant-based seafood alternatives: Current insights on the nutrition, protein-flavour interactions, and the processing of these foods.Current research in food science · 2024Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Food protein-flavor binding influences flavor release and perception. The complexity of the binding phenomenon lies in the flavor and protein properties. Thus, molecular interactions between commercial whey- or plant-based protein isolates (PI) such as pea, soy, and lupin, with carbonyl and alcohol flavor compounds were assessed by static headspace (HS) GC-MS. HS results showed that not only the displacement of the carbonyl group from the inner part of the flavor structure toward the edge promoted binding up to 52.76% ± 4.65 but also the flavor's degree of unsaturation. Similarly, thermal treatment led to a slight increase in hexanal-protein binding because of possible protein conformational changes. Protein's residual fat (<1%) seemed insufficient to promote significant flavor binding to PI. Despite the complexity of commercial food protein isolates, the results displayed that binding is predominantly influenced by the flavor structure and physicochemical properties, with the protein source and residual fat playing a secondary role.
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