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Interfacial behavior of lupin protein and its complexes with polysaccharides at different oil-water interfaces analyzed by general stress decomposition

Xingfa Ma, Mehdi Habibi, Leonard M.C. Sagis

2025Food Research International5 citationsDOIOpen Access PDF

Abstract

In this study, we studied the interfacial behavior of lupin proteins (LPI) and lupin protein-polysaccharide complexes (LPI-PS) (with sodium alginate, pectin, and κ-carrageenan), at different oil-water interfaces using interfacial dilatational rheology. Interfacial mechanical properties were investigated using large amplitude oscillatory dilatation (LAOD) and analyzed with the general stress decomposition (GSD) method. LPI and LPI-PS complexes adsorbed faster at apolar oil-water interfaces than at more polar oil-water interfaces. A significant change in the GSD parameters, E τ1L and E τ4 , was observed across different hydrophobic subphases (i.e., more polar oil, apolar oil, and air). At more polar oil-water interfaces, the E τ4 moduli were highly positive (1.6–5.2 mN/m), and E τ1L was very low (11.4–17.9 mN/m). At more apolar oil-water interfaces, the E τ4 moduli became slightly negative (between −2.7 and − 3.7 mN/m), and E τ1L was considerably increased (37.8–51.4 mN/m). At air-water interfaces, the E τ4 moduli were most negative (between −11.9 mN/m and − 13.1 mN/m), and E τ1L was highest (77.8–150.4 mN/m). These results suggested that the LPI-PS complexes may behave more similar to particles and form soft glass-like structures at polar oil-water interfaces, and more gel-like networks may form at apolar oil- and air-water interfaces. At the air-water interface such networks have previously been observed using atomic force microscopy. LPI showed a more substantial increase in E d ’ with reduced oil polarity than LPI-PS with lower structural flexibility. Emulsions prepared with more polar oils also showed worse emulsion flow stability than the others, due to the lower stiffness of their oil-water interfaces. • GSD parameters indicate different interfacial behavior with varying oil polarity. • More polar O/W interfaces were weaker and showed soft glass-like behavior. • Apolar O/W interfaces were stiffer and more gel-like (higher E τ1 and negative E τ4 ). • Complexes with low flexibility showed constant E d ’ with reduced oil polarity. • Emulsions prepared with apolar oils were more stable than those with polar oils.

Topics & Concepts

PolarChemistryEmulsionDecompositionAdsorptionChemical engineeringPolarity (international relations)PolysaccharideChemical polarityCrystallographyStress (linguistics)Elastic modulusHydrophobic effectChromatographyLayer (electronics)StereochemistryChemical physicsSodium CaseinateOrganic chemistryMolecular dynamicsOil dropletSodiumSurface tensionModuliBotanical Research and ChemistryProteins in Food SystemsPolysaccharides Composition and Applications
Interfacial behavior of lupin protein and its complexes with polysaccharides at different oil-water interfaces analyzed by general stress decomposition | Litcius