The ultrasonic effect on the physicochemical and emulsifying properties of three animal proteins, bovine gelatin (BG), fish gelatin (FG) and egg white protein (EWP), and three vegetable proteins, pea protein isolate (PPI), soy protein isolate (SPI) and rice protein isolate (RPI), was investigated. Protein solutions (0.1–10 wt.%) were sonicated at an acoustic intensity of ∼34 W cm−2 for 2 min. The structural and physical properties of the proteins were probed in terms of changes in size, hydrodynamic volume and molecular structure using DLS and SLS, intrinsic viscosity and SDS-PAGE, respectively. The emulsifying performance of ultrasound treated animal and vegetable proteins were compared to their untreated counterparts and Brij 97. Ultrasound treatment reduced the size of all proteins, with the exception of RPI, and no reduction in the primary structure molecular weight profile of proteins was observed in all cases. Emulsions prepared with all untreated proteins yielded submicron droplets at concentrations ≤1 wt.%, whilst at concentrations >5 wt.% emulsions prepared with EWP, SPI and RPI yielded micron sized droplets (>10 μm) due to pressure denaturation of protein from homogenisation. Emulsions produced with sonicated FG, SPI and RPI had the similar droplet sizes as untreated proteins at the same concentrations, whilst sonicated BG, EWP and PPI emulsions at concentrations ≤1 wt.% had a smaller droplet size compared to emulsions prepared with their untreated counterparts. This effect was consistent with the observed reduction in the interfacial tension between these untreated and ultrasound treated proteins.
|Early online date||13 Feb 2015|
|Publication status||Published - Feb 2016|
- Egg white protein
- Pea protein isolate
- Soy protein isolate
- Rice protein isolate