TY - JOUR
T1 - Effect of functional groups in strawberry flavoring on pea protein-flavor interactions
T2 - Potential applicable in flavor formulation for plant-based protein aqueous foods
AU - Wongprasert, Thanakorn
AU - Mathatheeranan, Pakavit
AU - Siripitakpong, Panatthida
AU - Vilaivan, Tirayut
AU - Suriya, Utid
AU - Rungrotmongkol, Thanyada
AU - Cadwallader, Keith
AU - Suppavorasatit, Inthawoot
N1 - Publisher Copyright:
© 2024
PY - 2024/10/30
Y1 - 2024/10/30
N2 - This research aimed to explore binding interactions between pea protein isolate (PPI) and selected strawberry flavorings including vanillin, γ-decalactone, furaneol, and (Z)-3-hexen-1-ol within an aqueous system. The results showed that binding affinities of PPI with all various functional group of flavor compounds decreased as temperature increased from 5 °C to 25 °C. Notably, at 25 °C, γ-decalactone displayed the highest binding affinity, followed by vanillin, (Z)-3-hexen-1-ol, and furaneol. Lowest binding was observed for furaneol, explained by its greater lipophilicity (lower partition coefficient values or LogP value) and molecular structure in each functional group in the flavor compounds. Thermodynamically, the interaction between PPI and each selected flavor compound was spontaneous, with evidence suggesting primary forces being hydrophobic interactions or hydrogen bonding/van der Waals forces. Computational molecular docking further confirmed these interaction types. This research provides insights into the interactions between PPI and strawberry flavorings, aiding in the selection of optimal flavor compound proportion for protein-rich products.
AB - This research aimed to explore binding interactions between pea protein isolate (PPI) and selected strawberry flavorings including vanillin, γ-decalactone, furaneol, and (Z)-3-hexen-1-ol within an aqueous system. The results showed that binding affinities of PPI with all various functional group of flavor compounds decreased as temperature increased from 5 °C to 25 °C. Notably, at 25 °C, γ-decalactone displayed the highest binding affinity, followed by vanillin, (Z)-3-hexen-1-ol, and furaneol. Lowest binding was observed for furaneol, explained by its greater lipophilicity (lower partition coefficient values or LogP value) and molecular structure in each functional group in the flavor compounds. Thermodynamically, the interaction between PPI and each selected flavor compound was spontaneous, with evidence suggesting primary forces being hydrophobic interactions or hydrogen bonding/van der Waals forces. Computational molecular docking further confirmed these interaction types. This research provides insights into the interactions between PPI and strawberry flavorings, aiding in the selection of optimal flavor compound proportion for protein-rich products.
KW - Binding thermodynamics
KW - Flavor binding
KW - Molecular docking
KW - Pea protein
KW - Strawberry flavor
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UR - http://www.scopus.com/inward/citedby.url?scp=85200129100&partnerID=8YFLogxK
U2 - 10.1016/j.fochx.2024.101702
DO - 10.1016/j.fochx.2024.101702
M3 - Article
C2 - 39184319
AN - SCOPUS:85200129100
SN - 2590-1575
VL - 23
JO - Food Chemistry: X
JF - Food Chemistry: X
M1 - 101702
ER -