Interaction between Fish Skin Gelatin and Pea Protein at Air-Water Interface after Ultrasound Treatment
Journal article, 2022
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.
Fish skin gelatin
Interfacial properties
Turbiscan Tower
Foaming properties
Pea protein
CLSM
Author
Davide Odelli
Federal University of Viçosa
Technical University of Denmark (DTU)
Università Cattolica del Sacro Cuore
Krystalia Sarigiannidou
Technical University of Denmark (DTU)
Alberto Soliani
Technical University of Denmark (DTU)
Rodolphe Marie
Technical University of Denmark (DTU)
Mohammad Amin Mohammadifar
Technical University of Denmark (DTU)
Flemming Jessen
Technical University of Denmark (DTU)
Giorgia Spigno
Università Cattolica del Sacro Cuore
Mar Vall-Llosera Juanola
Chalmers, Biology and Biological Engineering, Food and Nutrition Science
Antonio Fernandes de Carvalho
Federal University of Viçosa
Michela Verni
University of Bari Aldo Moro
Federico Casanova
Technical University of Denmark (DTU)
Foods
23048158 (eISSN)
Vol. 11 5 659Subject Categories
Physical Chemistry
Food Engineering
Biophysics
DOI
10.3390/foods11050659
PubMed
35267292