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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
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
Ultrasound-induced structural modification and thermal properties of oat protein
Li, R., & Xiong, Y. L. (2021) · LWT · doi:10.1016/j.lwt.2021.111861 · Cited by 112
Mozafarpour, R., Koocheki, A., Sani, M. A., McClements, D. J., & Mehr, H. M. (2022) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2022.102768 · Cited by 91
Gulzar, S., Martín-Belloso, O., & Soliva-Fortuny, R. (2024) · Foods · doi:10.3390/foods13030376 · Cited by 60
Karabulut, G., Feng, H., & Yemiş, O. (2022) · Plant Foods for Human Nutrition · doi:10.1007/s11130-022-01017-7 · Cited by 60
Ultrasound-induced changes in the structure and functionality of starch and protein
Zhu, M., Xiong, W., Devkota, L., & Dhital, S. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.112111 · Cited by 40
Adal, E. (2024) · Journal of Food Measurement and Characterization · doi:10.1007/s11694-024-02379-z · Cited by 35
Sidiq, M., Muzzaffar, S., Masoodi, F. A., & Irfan, S. (2024) · Measurement: Food · doi:10.1016/j.meafoo.2024.100205 · Cited by 6
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.