Power Ultrasound Assisted Design of Egg Albumin Nanoparticles

Abstract

The objective of this work was to develop egg white (EW) nanoparticles by application of high intensity ultrasound (HIUS) at different solution pHs and treatment temperatures. At pH 7 HIUS without heating decreased the particle size. In contrast, the use of thermosonication (TS) increased the particle size. At pH 3, the application of both HIUS and TS induced a significant reduction of particle size. at pH 7 zeta potential did not vary significantly when native solutions were sonicated without heating; however a great decrease was observed when TS or heating were applied. At pH 3, sonication decreased the zeta potential of particles but TS or heating increased the charge. By applying TS (85°C, 20 min and pH 3) a bimodal distribution was obtained, including particles of 295 and 70 nm of diameter. At the same pH, without heating, a monomodal population of 220 nm of diameter was obtained.

Egg albumin–folic acid nanocomplexes: Performance as a functional ingredient and biological activity

“…EW nanoparticles were designed according to a previous work (Arzeni et al, 2015). Briefly, EW solutions (5% (w/w), pH 3 and 7) were sonicated for 5, 10, 15 and 20 min using an ultrasonic processor Vibra Cell Sonics, model VCX 750 (Newtown, CT, USA) with a maximum net power output of 750 W at a frequency of 20 kHz and an amplitude of 20% (maximum amplitude 40%, 228 µm).…”

“…High intensity ultrasound (HIUS) technology has been effective in controlling particle size of different biopolymers. In a previous research, EW nanoparticles have been developed by application of HIUS or thermosonication (Arzeni, Pérez, & Pilosof, 2015). By applying HIUS without heating for 20 min to an EW solution at pH 3, a monomodal population of 220 nm of diameter was obtained as evaluated by dynamic light scattering.…”

Effect of processing technologies on the digestibility of egg proteins

“…The increase in the SH groups was also accompanied with the decrease of both particle size and particle size distribution (Jovanović et al., 2016) and was attributed to ultrasound‐assisted disruption of protein interactions responsible for the formation of protein aggregates. Ultrasound processing has been reported to break the protein aggregates into smaller particles (Jambrak et al., 2014) and to significantly decrease the particle size of native egg white proteins (Arzeni et al., 2015). A significant increase ( p < .05) was also recorded in the ζ potential of the ultrasound processed egg white proteins and was attributed to the structural rearrangement of the proteins caused by ultrasonic cavitation (Jovanović et al., 2016).…”

Determining Sonication Effect on E. coli in Liquid Egg, Egg Yolk and Albumen and Inspecting Structural Property Changes by Near-Infrared Spectra

“…It contains about 40 different proteins, such as ovalbumin, lysozyme, ovomucoid, ovotransferrin. Ovalbumin, which constitutes about 54% of the total egg white protein, is mainly responsible for gelation [ 4 , 5 , 6 , 7 ].…”