Influence of ultrasound probe treatment time and protease type on functional and physicochemical characteristics of egg white protein hydrolysates
2018
Аутори
Stefanović, AndreaJovanović, Jelena
Balanč, Bojana
Šekuljica, Nataša
Jakovetić Tanasković, Sonja
Dojčinović, Marina
Knežević-Jugović, Zorica
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
The objective of this study was to discover the relationship between the ultrasound probe treatment (UPT) on egg white proteins (EWPs) before EWPs hydrolysis by different proteases, and the functional properties of the obtained hydrolysates. To fulfill this goal, the protein solubility, foaming, and emulsifying properties were studied as a function of the UPT time and then related to the surface characteristics and structural properties. The changes in the hydrolysates microstructures and macromolecular conformation, induced by the UPT, were followed using scanning electron microscope analyzis (SEM) and Fourier transforms infrared spectroscopy (FTIR). The results showed that UPT influenced (P lt 0.05) the proteolysis of egg white proteins for all examined treatment times. Alcalase hydrolysates (AHs) and papain hydrolysates (PHs) were found to have a higher solubility, as a consequence of their relatively higher foaming, and emulsifying properties compared to the untreated hydrolysate...s. The changes in surface hydrophobicity, sulfhydryl content and surface charge of AHs and PHs indicated unfolding of EWPs affected by ultrasound. SEM analyzis showed that UPT destroyed the microstructures of AHs and PHs, while FTIR spectra indicated remarkable changes in the macromolecular conformation of AHs and PHs after UPT. This study revealed that by combining ultrasound pre-hydrolysis treatment under controlled conditions with thoughtful proteases selection, hydrolysates with improved functional properties could be produced, enhancing utilization of EWPs in food products.
Кључне речи:
functionality of egg white / hydrolysates / ultrasound probe treatment / structural characterization / surface characteristicsИзвор:
Poultry Science, 2018, 97, 6, 2218-2229Издавач:
- Oxford Univ Press, Oxford
Финансирање / пројекти:
- E!6750
- Развој нових инкапсулационих и ензимских технологија за производњу биокатализатора и биолошки активних компонената хране у циљу повећања њене конкурентности, квалитета и безбедности (RS-MESTD-Integrated and Interdisciplinary Research (IIR or III)-46010)
DOI: 10.3382/ps/pey055
ISSN: 0032-5791
PubMed: 29514309
WoS: 000434235700043
Scopus: 2-s2.0-85048045212
Колекције
Институција/група
Tehnološko-metalurški fakultetTY - JOUR AU - Stefanović, Andrea AU - Jovanović, Jelena AU - Balanč, Bojana AU - Šekuljica, Nataša AU - Jakovetić Tanasković, Sonja AU - Dojčinović, Marina AU - Knežević-Jugović, Zorica PY - 2018 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3997 AB - The objective of this study was to discover the relationship between the ultrasound probe treatment (UPT) on egg white proteins (EWPs) before EWPs hydrolysis by different proteases, and the functional properties of the obtained hydrolysates. To fulfill this goal, the protein solubility, foaming, and emulsifying properties were studied as a function of the UPT time and then related to the surface characteristics and structural properties. The changes in the hydrolysates microstructures and macromolecular conformation, induced by the UPT, were followed using scanning electron microscope analyzis (SEM) and Fourier transforms infrared spectroscopy (FTIR). The results showed that UPT influenced (P lt 0.05) the proteolysis of egg white proteins for all examined treatment times. Alcalase hydrolysates (AHs) and papain hydrolysates (PHs) were found to have a higher solubility, as a consequence of their relatively higher foaming, and emulsifying properties compared to the untreated hydrolysates. The changes in surface hydrophobicity, sulfhydryl content and surface charge of AHs and PHs indicated unfolding of EWPs affected by ultrasound. SEM analyzis showed that UPT destroyed the microstructures of AHs and PHs, while FTIR spectra indicated remarkable changes in the macromolecular conformation of AHs and PHs after UPT. This study revealed that by combining ultrasound pre-hydrolysis treatment under controlled conditions with thoughtful proteases selection, hydrolysates with improved functional properties could be produced, enhancing utilization of EWPs in food products. PB - Oxford Univ Press, Oxford T2 - Poultry Science T1 - Influence of ultrasound probe treatment time and protease type on functional and physicochemical characteristics of egg white protein hydrolysates EP - 2229 IS - 6 SP - 2218 VL - 97 DO - 10.3382/ps/pey055 ER -
@article{ author = "Stefanović, Andrea and Jovanović, Jelena and Balanč, Bojana and Šekuljica, Nataša and Jakovetić Tanasković, Sonja and Dojčinović, Marina and Knežević-Jugović, Zorica", year = "2018", abstract = "The objective of this study was to discover the relationship between the ultrasound probe treatment (UPT) on egg white proteins (EWPs) before EWPs hydrolysis by different proteases, and the functional properties of the obtained hydrolysates. To fulfill this goal, the protein solubility, foaming, and emulsifying properties were studied as a function of the UPT time and then related to the surface characteristics and structural properties. The changes in the hydrolysates microstructures and macromolecular conformation, induced by the UPT, were followed using scanning electron microscope analyzis (SEM) and Fourier transforms infrared spectroscopy (FTIR). The results showed that UPT influenced (P lt 0.05) the proteolysis of egg white proteins for all examined treatment times. Alcalase hydrolysates (AHs) and papain hydrolysates (PHs) were found to have a higher solubility, as a consequence of their relatively higher foaming, and emulsifying properties compared to the untreated hydrolysates. The changes in surface hydrophobicity, sulfhydryl content and surface charge of AHs and PHs indicated unfolding of EWPs affected by ultrasound. SEM analyzis showed that UPT destroyed the microstructures of AHs and PHs, while FTIR spectra indicated remarkable changes in the macromolecular conformation of AHs and PHs after UPT. This study revealed that by combining ultrasound pre-hydrolysis treatment under controlled conditions with thoughtful proteases selection, hydrolysates with improved functional properties could be produced, enhancing utilization of EWPs in food products.", publisher = "Oxford Univ Press, Oxford", journal = "Poultry Science", title = "Influence of ultrasound probe treatment time and protease type on functional and physicochemical characteristics of egg white protein hydrolysates", pages = "2229-2218", number = "6", volume = "97", doi = "10.3382/ps/pey055" }
Stefanović, A., Jovanović, J., Balanč, B., Šekuljica, N., Jakovetić Tanasković, S., Dojčinović, M.,& Knežević-Jugović, Z.. (2018). Influence of ultrasound probe treatment time and protease type on functional and physicochemical characteristics of egg white protein hydrolysates. in Poultry Science Oxford Univ Press, Oxford., 97(6), 2218-2229. https://doi.org/10.3382/ps/pey055
Stefanović A, Jovanović J, Balanč B, Šekuljica N, Jakovetić Tanasković S, Dojčinović M, Knežević-Jugović Z. Influence of ultrasound probe treatment time and protease type on functional and physicochemical characteristics of egg white protein hydrolysates. in Poultry Science. 2018;97(6):2218-2229. doi:10.3382/ps/pey055 .
Stefanović, Andrea, Jovanović, Jelena, Balanč, Bojana, Šekuljica, Nataša, Jakovetić Tanasković, Sonja, Dojčinović, Marina, Knežević-Jugović, Zorica, "Influence of ultrasound probe treatment time and protease type on functional and physicochemical characteristics of egg white protein hydrolysates" in Poultry Science, 97, no. 6 (2018):2218-2229, https://doi.org/10.3382/ps/pey055 . .