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

Davide Odelli, Krystalia Sarigiannidou, Alberto Soliani, Rodolphe Marie, Mohammad Amin Mohammadifar, Flemming Jessen, Giorgia Spigno, Mar Vall-llosera, Antonio Fernandes de Carvalho, Michela Verni, Federico Casanova*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

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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.
Original languageEnglish
Article number659
JournalFoods
Volume11
Issue number5
Number of pages15
ISSN2304-8158
DOIs
Publication statusPublished - 2022

Keywords

  • Foaming properties
  • Fish skin gelatin
  • Pea protein
  • Interfacial properties
  • Turbiscan Tower
  • CLSM

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