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 similar to 370 to similar 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.
Keywords:
High-intensity ultrasound / Egg white proteins / Particle properties / Functionality / Susceptibility to hydrolysis / Structure characterization
Source:
Food and Bioprocess Technology, 2017, 10, 7, 1224-1239
Publisher:
Springer, New York
Funding / projects:
Ministry of Education, Science and Technological Development of the Republic of Serbia [E!6750]
TY - JOUR
AU - Stefanović, Andrea B.
AU - Jovanović, Jelena R.
AU - Dojcinović, Marina B.
AU - Lević, Steva
AU - Nedović, Viktor
AU - Bugarski, Branko
AU - Knežević-Jugović, Zorica
PY - 2017
UR - http://aspace.agrif.bg.ac.rs/handle/123456789/4342
AB - 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 similar to 370 to similar 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.
PB - Springer, New York
T2 - Food and Bioprocess Technology
T1 - Effect of the Controlled High-Intensity Ultrasound on Improving Functionality and Structural Changes of Egg White Proteins
EP - 1239
IS - 7
SP - 1224
VL - 10
DO - 10.1007/s11947-017-1884-5
ER -
@article{
author = "Stefanović, Andrea B. and Jovanović, Jelena R. and Dojcinović, Marina B. and Lević, Steva and Nedović, Viktor and Bugarski, Branko and Knežević-Jugović, Zorica",
year = "2017",
abstract = "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 similar to 370 to similar 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.",
publisher = "Springer, New York",
journal = "Food and Bioprocess Technology",
title = "Effect of the Controlled High-Intensity Ultrasound on Improving Functionality and Structural Changes of Egg White Proteins",
pages = "1239-1224",
number = "7",
volume = "10",
doi = "10.1007/s11947-017-1884-5"
}
Stefanović, A. B., Jovanović, J. R., Dojcinović, M. B., Lević, S., Nedović, V., Bugarski, B.,& Knežević-Jugović, Z.. (2017). Effect of the Controlled High-Intensity Ultrasound on Improving Functionality and Structural Changes of Egg White Proteins. in Food and Bioprocess Technology
Springer, New York., 10(7), 1224-1239.
https://doi.org/10.1007/s11947-017-1884-5
Stefanović AB, Jovanović JR, Dojcinović MB, Lević S, Nedović V, Bugarski B, Knežević-Jugović Z. Effect of the Controlled High-Intensity Ultrasound on Improving Functionality and Structural Changes of Egg White Proteins. in Food and Bioprocess Technology. 2017;10(7):1224-1239.
doi:10.1007/s11947-017-1884-5 .
Stefanović, Andrea B., Jovanović, Jelena R., Dojcinović, Marina B., Lević, Steva, Nedović, Viktor, Bugarski, Branko, Knežević-Jugović, Zorica, "Effect of the Controlled High-Intensity Ultrasound on Improving Functionality and Structural Changes of Egg White Proteins" in Food and Bioprocess Technology, 10, no. 7 (2017):1224-1239,
https://doi.org/10.1007/s11947-017-1884-5 . .
