Interaction between Fish Skin Gelatin and Pea Protein at Air-Water Interface after Ultrasound Treatment
Artikel i vetenskaplig tidskrift, 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
Författare
Davide Odelli
Universidade Federal de Vicosa
Danmarks Tekniske Universitet (DTU)
Università Cattolica del Sacro Cuore
Krystalia Sarigiannidou
Danmarks Tekniske Universitet (DTU)
Alberto Soliani
Danmarks Tekniske Universitet (DTU)
Rodolphe Marie
Danmarks Tekniske Universitet (DTU)
Mohammad Amin Mohammadifar
Danmarks Tekniske Universitet (DTU)
Flemming Jessen
Danmarks Tekniske Universitet (DTU)
Giorgia Spigno
Università Cattolica del Sacro Cuore
Mar Vall-Llosera Juanola
Chalmers, Biologi och bioteknik, Livsmedelsvetenskap
Antonio Fernandes de Carvalho
Universidade Federal de Vicosa
Michela Verni
Universita degli Studi di Bari Aldo Moro
Federico Casanova
Danmarks Tekniske Universitet (DTU)
Foods
23048158 (eISSN)
Vol. 11 5 659Ämneskategorier
Fysikalisk kemi
Livsmedelsteknik
Biofysik
DOI
10.3390/foods11050659
PubMed
35267292