Unraveling the Role of Flavor Structure and Physicochemical Properties in the Binding Phenomenon with Commercial Food Protein Isolates
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.
| Main Authors: | , , , , |
|---|---|
| Format: | Article/Letter to editor biblioteca |
| Language: | English |
| Subjects: | commercial food protein isolates, flavor structure, molecular interactions, plant-based proteins, protein-flavor binding, |
| Online Access: | https://research.wur.nl/en/publications/unraveling-the-role-of-flavor-structure-and-physicochemical-prope |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| Summary: | 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. |
|---|