TY - JOUR
T1 - Interaction between Fish Skin Gelatin and Pea Protein at Air-Water Interface after Ultrasound Treatment
AU - Odelli, Davide
AU - Sarigiannidou, Krystalia
AU - Soliani, Alberto
AU - Marie, Rodolphe
AU - Mohammadifar, Mohammad Amin
AU - Jessen, Flemming
AU - Spigno, Giorgia
AU - Vall-llosera, Mar
AU - Fernandes de Carvalho, Antonio
AU - Verni, Michela
AU - Casanova, Federico
PY - 2022
Y1 - 2022
N2 - 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.
AB - 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.
KW - Foaming properties
KW - Fish skin gelatin
KW - Pea protein
KW - Interfacial properties
KW - Turbiscan Tower
KW - CLSM
U2 - 10.3390/foods11050659
DO - 10.3390/foods11050659
M3 - Journal article
C2 - 35267292
SN - 2304-8158
VL - 11
JO - Foods
JF - Foods
IS - 5
M1 - 659
ER -