The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Effect of ultrasound treatments on functional properties and structure of millet protein concentrate
Open accessAbstract
In this study, the effect of high power ultrasound (US) probe in varying intensities and times (18.4, 29.58, and 73.95 W/cm2 for 5, 12.5 and 20 min respectively) on functional properties of millet protein concentrate (MPC) was investigated, and also the structural properties of best modified treatment were evaluated by FTIR, DSC, Zeta potential and SDS-PAGE techniques. The results showed the solubility in all US treated MPC was significantly (p < .05) higher than those of the native MPC. Foaming capacity of native MPC (271.03 ± 4.51 ml) was reduced after US treatments at low intensities (82.37 ± 5.51 ml), but increased upon US treatments at high intensities (749.7 ± 2 ml). In addition, EAI and ES increased after US treatments. One of the best US treatments that can improve the functional properties of MPC was 73.95 W/cm2 for 12.5 min that resulted in reduction of molecular weight and increase nearly 36% in the negative surface charge that was confirmed by SDS-page and Zeta potential results, respectively.
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Cites
Infrared spectroscopy of proteins
Barth, A. (2007) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2007.06.004 · Cited by 5,129 · cited 1×
“These increase in wave number according to the fact that frequency of stretching vibration reduced because of hydrogen bond formation [41].”
BackgroundFTIR reveals structural differences between native β‐sheet proteins and amyloid fibrils
Zandomeneghi, G., Krebs, M. R. H., McCammon, M. G., & Fändrich, M. (2004) · Protein Science · doi:10.1110/ps.041024904 · Cited by 725
Nakai, S. (1983) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf00118a001 · Cited by 421
Cited by
Rahman, M. M., & Lamsal, B. P. (2021) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12709 · Cited by 438
Ultrasound driven conformational and physicochemical changes of soy protein hydrolysates
Tian, R., Feng, J., Huang, G., Tian, B., Zhang, Y., Jiang, L., & Sui, X. (2020) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2020.105202 · Cited by 263
Figueroa-González, J. J., Lobato-Calleros, C., Vernon-Carter, E. J., Aguirre-Mandujano, E., Alvarez-Ramirez, J., & Martínez-Velasco, A. (2022) · LWT · doi:10.1016/j.lwt.2021.112561 · Cited by 144
Rashwan, A. K., Osman, A. I., Abdelshafy, A. M., Mo, J., & Chen, W. (2025) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2023.2279696 · Cited by 144
Thermosonication-induced structural changes and solution properties of mung bean protein
Zhong, Z., & Xiong, Y. L. (2020) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2019.104908 · Cited by 142
Metadata
- Authors
- Nazari, B., Mohammadifar, M. A., Shojaee-Aliabadi, S., Feizollahi, E., & Mirmoghtadaie, L.
- Venue
- Ultrasonics Sonochemistry
- Publisher
- Elsevier BV
- Published
- 2018-03
- Volume
- 41
- Pages
- 382-388
- ISSN
- 1350-4177 (ISSN-L)
- OpenAlex
- W2762658802
- Cited by
- 352
- References
- 3
- FWCI
- 12.03
- Type
- journal article
- Language
- en
- Open access
- green
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