Current knowledge on the interfacial behaviour limits our understanding of plant protein functionality in emulsions

Drusch, Stephan; Klost, Martina; Kieserling, Helena

doi:10.1016/j.cocis.2021.101503

Cited by 51 publications

(13 citation statements)

References 67 publications

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“…Thus, the presence of FA fraction largely determined the foaming potential of FPI, which was undoubtedly inferior to that of individual FA (−23.9%, p < 0.05). The flexible spatial conformation, superior solubility, and lower molecular weights could enhance the migration efficiency of FA at the air-water interface, leading to the preferable foaming ability [43]. In comparison, the poor foaming activity of FG might be explained by the slow interface migration from the bulk aqueous phase into air/water interface due to the higher hydrophobic amino acids and molecular weights, respectively.…”

Section: The Foaming Properties Of Flaxseed Protein Fractionsmentioning

confidence: 99%

“…Instead, effective conformation adaptability and strong intermolecular crosslinks might inevitably occur for FG, leading to the formation of densely packed viscoelastic films. The higher initial value of interfacial pressure and slight reduction over time for FPI suggested that the low amounts of FA and noncovalent interactions with FG sufficiently resulted in low interfacial diffusion, adsorption, and conformation reorganization [43]. The abilities of flaxseed protein fractions to be absorbed at the air/water in were further evaluated through time-dependent alteration of surface tension (π) v As presented in Figure 2f, the initial π value of FPI (1.0%, w/v) was 41.60 mN .…”

Section: The Foaming Properties Of Flaxseed Protein Fractionsmentioning

confidence: 99%

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Comparative Composition Structure and Selected Techno-Functional Elucidation of Flaxseed Protein Fractions

Qin

et al. 2022

Foods

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This study aimed to comparatively elucidate the composition structure and techno-functionality of flaxseed protein isolate (FPI), globulin (FG), and albumin (FA) fractions. The results showed that FA possessed smaller particle dimensions and superior protein solubility compared to that of FG (p < 0.05) due to the lower molecular weight and hydrophobicity. FA and FG manifested lamellar structure and nearly spherical morphology, respectively, whereas FPI exhibited small lamellar strip structure packed by the blurring spheres. The Far-UV CD, FTIR spectrum, and intrinsic fluorescence confirmed more flexible conformation of FA than that of FG, followed by FPI. The preferential retention of free phenolic acids was observed for FA, leading to excellent antioxidant activities compared with that of FG in FPI (p < 0.05). FA contributed to the foaming properties of FPI, relying on the earlier interfacial adsorption and higher viscoelastic properties. FA displayed favorable emulsifying capacity but inferior stability due to the limited interfacial adsorption and deformation, as well as loose/porous interface. By comparison, an interlayer anchoring but no direct interface coating was observed for lipid droplets constructed by FG, thereby leading to preferable emulsion stability. However, FPI produced lipid droplets with dense interface owing to the effective migration of FA and FG from bulk phase, concomitant with the easy flocculation and coalescence. Thus, the techno-functionality of flaxseed protein could be tailed by modulating the retention of albumin fraction and specific phenolic acids.

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Section: The Foaming Properties Of Flaxseed Protein Fractionsmentioning

confidence: 99%

Section: The Foaming Properties Of Flaxseed Protein Fractionsmentioning

confidence: 99%

Comparative Composition Structure and Selected Techno-Functional Elucidation of Flaxseed Protein Fractions

Qin

et al. 2022

Foods

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“…At the A-W interface, without the oil solvent to interact with the hydrophobic residues of proteins, the structure rearrangement and special orientations are limited to a certain extent . The statement is also supported with the findings that β-lactoglobulin loses more tertiary and secondary structure at the O-W interface than at the A-W interface (Drusch, et al, 2021;Meinders & De Jongh, 2002;Zhai, et al, 2010). Consequently, when casein monomer and whey proteins co-adsorb at the A-W interface, the displacement of casein monomers by whey protein will be limited.…”

Section: Casein and Whey Protein Mixturessupporting

confidence: 60%

Interfacial properties of dairy ingredients: role of various protein fractions and emulsifier crystals

Zhou¹

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“…However, in this study, larger droplet sizes ( Figure 3 A) were observed at pH 7 and 9 with or without ionic salts. These results indicate that there would be other factors, i.e., nature of the protein, viscosity of aqueous phase and interfacial protein composition, which would also control the flow behavior of emulsion [ 30 ].…”

Section: Resultsmentioning

confidence: 99%

Effects of pH and Ionic Salts on the Emulsifying and Rheological Properties of Acorn Protein Isolate

et al. 2022

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This study was designed to evaluate the emulsifying and rheological properties of acorn protein isolate (API) in different pH mediums (pH 3, 7 and 9) and in the presence of ionic salts (1 M NaCl and 1 M CaCl2). API shows higher solubility in distilled water at pH 7, while at the same pH, a decrease in solubility was observed for API in the presence of CaCl2 (61.30%). A lower emulsifying activity index (EAI), lower stability index (ESI), larger droplet sizes and slight flocculation were observed for API in the presence of salts at different pHs. Importantly, CaCl2 treated samples showed relevantly higher EAI (252.67 m2/g) and ESI (152.67 min) values at all pH as compared to NaCl (221.76 m2/g), (111.82 min), respectively. A significant increase in interfacial protein concentration (4.61 mg/m2) was observed for emulsion at pH 9 with CaCl2, while the major fractions of API were observed in an interfacial layer after SDS-PAGE analysis. All of the emulsion shows shear thinning behavior (τc > 0 and n < 1), while the highest viscosity was observed for emulsion prepared with CaCl2 at pH 3 (11.03 ± 1.62). In conclusion, API, in the presence of ionic salts at acidic, neutral and basic pH, can produce natural emulsions, which could be substitutes for synthetic surfactants for such formulations.

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Current knowledge on the interfacial behaviour limits our understanding of plant protein functionality in emulsions

Cited by 51 publications

References 67 publications

Comparative Composition Structure and Selected Techno-Functional Elucidation of Flaxseed Protein Fractions

Comparative Composition Structure and Selected Techno-Functional Elucidation of Flaxseed Protein Fractions

Interfacial properties of dairy ingredients: role of various protein fractions and emulsifier crystals

Effects of pH and Ionic Salts on the Emulsifying and Rheological Properties of Acorn Protein Isolate

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