Dataset Information

Interaction between Fish Skin Gelatin and Pea Protein at Air-Water Interface after Ultrasound Treatment.

ABSTRACT: The interaction between fish skin gelatin (FG) and pea protein isolate (PPI) was investigated at the air-water interface (A-W) before and after a high intensity (275 W, 5 min) ultrasound treatment (US). We analyzed the properties of the single protein suspensions as well as an equal ratio of FG:PPI (MIX), in terms of ζ-potential, particle size, molecular weight, bulk viscosity and interfacial tension. The foaming properties were then evaluated by visual analysis and by Turbiscan Tower. Confocal laser scanning microscopy (CLSM) was employed to explore the role of the proteins on the microstructure of foams. The results showed that the ultrasound treatment slightly influenced physicochemical properties of the proteins, while in general, did not significantly affect their behavior both in bulk and at the air-water interface. In particular, PPI aggregate size was reduced (-48 nm) while their negative charges were increased (-1 mV) after the treatment. However, when the proteins were combined, higher molecular weight of aggregates, higher foam stability values (+14%) and lower interfacial tension (IFT) values (47.2 ± 0.2 mN/m) were obtained, leading us to assume that a weak interaction was developed between them.

SUBMITTER: Odelli D

PROVIDER: S-EPMC8909765 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature

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Interaction between Fish Skin Gelatin and Pea Protein at Air-Water Interface after Ultrasound Treatment.

Odelli Davide D Sarigiannidou Krystalia K Soliani Alberto A Marie Rodolphe R Mohammadifar Mohammad Amin MA Jessen Flemming F Spigno Giorgia G Vall-Llosera Mar M de Carvalho Antonio Fernandes AF Verni Michela M Casanova Federico F

Foods (Basel, Switzerland) 20220223 5

The interaction between fish skin gelatin (FG) and pea protein isolate (PPI) was investigated at the air-water interface (A-W) before and after a high intensity (275 W, 5 min) ultrasound treatment (US). We analyzed the properties of the single protein suspensions as well as an equal ratio of FG:PPI (MIX), in terms of ζ-potential, particle size, molecular weight, bulk viscosity and interfacial tension. The foaming properties were then evaluated by visual analysis and by Turbiscan Tower. Confocal ...[more]

PMID: 35267292

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Project description:Soft anions exhibit surface activity at the air/water interface that can be probed using surface-sensitive vibrational spectroscopy, but the structural implications of this surface activity remain a matter of debate. Here, we examine the nature of anion-water interactions at the air/water interface using a combination of molecular dynamics simulations and quantum-mechanical energy decomposition analysis based on symmetry-adapted perturbation theory. Results are presented for a set of monovalent anions, including Cl-, Br-, I-, CN-, OCN-, SCN-, NO2-, NO3-, and ClOn- (n=1,2,3,4), several of which are archetypal examples of surface-active species. In all cases, we find that average anion-water interaction energies are systematically larger in bulk water although the difference (with respect to the same quantity computed in the interfacial environment) is well within the magnitude of the instantaneous fluctuations. Specifically for the surface-active species Br-(aq), I-(aq), ClO4-(aq), and SCN-(aq), and also for ClO-(aq), the charge-transfer (CT) energy is found to be larger at the interface than it is in bulk water, by an amount that is greater than the standard deviation of the fluctuations. The Cl-(aq) ion has a slightly larger CT energy at the interface, but NO3-(aq) does not; these two species are borderline cases where consensus is lacking regarding their surface activity. However, CT stabilization amounts to <20% of the total induction energy for each of the ions considered here, and CT-free polarization energies are systematically larger in bulk water in all cases. As such, the role of these effects in the surface activity of soft anions remains unclear. This analysis complements our recent work suggesting that the short-range solvation structure around these ions is scarcely different at the air/water interface from what it is in bulk water. Together, these observations suggest that changes in first-shell hydration structure around soft anions cannot explain observed surface activities.

Dataset Information

Interaction between Fish Skin Gelatin and Pea Protein at Air-Water Interface after Ultrasound Treatment.

Publications

Interaction between Fish Skin Gelatin and Pea Protein at Air-Water Interface after Ultrasound Treatment.

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