Food and Bioprocess Technology

, Volume 10, Issue 7, pp 1224–1239 | Cite as

Effect of the Controlled High-Intensity Ultrasound on Improving Functionality and Structural Changes of Egg White Proteins

  • Andrea B. Stefanović
  • Jelena R. Jovanović
  • Marina B. Dojčinović
  • Steva M. Lević
  • Viktor A. Nedović
  • Branko M. Bugarski
  • Zorica D. Knežević-Jugović
Original Paper


The objective of this research was to investigate the impact of high-intensity ultrasound (HIU) generated by a probe-type sonicator (frequency 20 ± 0.2 kHz and an amplitude of 40%) for 2–20 min on the selected functional and structural properties of egg white proteins (EWPs) and their susceptibility to hydrolysis by alcalase. The protein solubility, foaming, and emulsifying properties were studied as a function of ultrasonication time and related to protein particle and structural properties. The length of ultrasonication exhibited important effect on EWP particle size, uniformity, and charge, affecting also the protein conformation and susceptibility to alcalase hydrolysis and determining functional properties. There was a linear correlation between the particle size decrease and the solubility while a two-step linear correlation between the foam capacity (FC)/foam stability (FS) and particle size was apparent. Specifically, FC and FS sharply increased with decreasing particle size for range from ∼370 to ∼260 nm, and below this range from 260.6 to 68.4 nm, the changes were not that substantial. Besides, the solubility, FC, and FS were directly and linearly related with the absolute value of the particle zeta potential. The overall emulsifying properties were also improved with an increase of sonication time, through both the decrease of the mean particle diameter and the increase of zeta potential, but there was no direct correlation between the emulsion activity/stability index and protein particle size and/or charge. Analysis of EWP structure by Raman spectroscopy revealed that the HIU leads to changes in the secondary structure, while heat and ultrasound generated by the ultrasound bath were not sufficient to exhibit this effect.

Graphical abstract


High-intensity ultrasound Egg white proteins Particle properties Functionality Susceptibility to hydrolysis Structure characterization 



The authors wish to extend their appreciation to the Ministry of Education, Science and Technological Development of the Republic of Serbia for their financial support within the EUREKA Project E!6750 and Project III-46010.

Supplementary material

11947_2017_1884_Fig10_ESM.gif (222 kb)
Online Resource 1

The emulsion activity/stability index of 2 wt. % ovalbumin treated with high-intensity ultrasound probe for various times (2, 5, 10, 15 and 20 min) at 20±0.2 kHz (GIF 222 kb)

11947_2017_1884_MOESM1_ESM.tif (2.8 mb)
High resolution image (TIFF 2882 kb)
11947_2017_1884_Fig11_ESM.gif (30 kb)
Online Resource 2

Correlations between EAI and ESI and particle size (a) and zeta potential (b) of UPT ovalbumin solution (GIF 29 kb)

11947_2017_1884_Fig12_ESM.gif (28 kb)
Online Resource 2

Correlations between EAI and ESI and particle size (a) and zeta potential (b) of UPT ovalbumin solution (GIF 29 kb)

11947_2017_1884_MOESM2_ESM.tif (1.1 mb)
High resolution image (TIFF 1093 kb)
11947_2017_1884_MOESM3_ESM.tif (1 mb)
High resolution image (TIFF 1043 kb)


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Copyright information

© Springer Science+Business Media New York 2017

Authors and Affiliations

  • Andrea B. Stefanović
    • 1
  • Jelena R. Jovanović
    • 1
  • Marina B. Dojčinović
    • 2
  • Steva M. Lević
    • 3
  • Viktor A. Nedović
    • 3
  • Branko M. Bugarski
    • 4
  • Zorica D. Knežević-Jugović
    • 1
  1. 1.Department of Biochemical Engineering and Biotechnology, Faculty of Technology and MetallurgyUniversity of BelgradeBelgradeRepublic of Serbia
  2. 2.Department of General Technical Sciences, Faculty of Technology and MetallurgyUniversity of BelgradeBelgradeRepublic of Serbia
  3. 3.Department for Food Technology and Biochemistry, Faculty of AgricultureUniversity of BelgradeBelgradeRepublic of Serbia
  4. 4.Department of Chemical Engineering, Faculty of Technology and MetallurgyUniversity of BelgradeBelgradeRepublic of Serbia

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