The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.
The aggregation, structures and emulsifying properties of soybean protein isolate induced by ultrasound and acid
Abstract
The effects of ultrasound and acid on the aggregation, structures and emulsifying properties of soybean protein isolate (SPI) were investigated. Results of solubility showed that ultrasonic treatments at 0.001 M HCl increased the content of soluble SPI. The particle size of soluble aggregates subjected to ultrasonication and acid was initially decreased and then increased with increasing ultrasonic time. Secondary structure analysis, by circular dichroism, indicated lower a-helix and higher random coil amounts in SPI treated with short ultrasonic time, in contrast to the higher a-helix and lower random coil in SPI treated with longer time (more than 20 min). Emulsions prepared with SPI by 10 min of ultrasonication demonstrated significantly (P < 0.05) small droplet sizes and long term stability in comparison with their untreated counterparts. These results highlight that the emulsifying properties of SPI can be significantly improved by the synergistic effect of ultrasound and acid.
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“Huang et al. [35] observed the application of ultrasonic treatment for more than 10 min on soy protein isolate resulted in a significant increase in α-helix content, along with a noticeable decrease in the content of random coil structures.”
From A comprehensive review of ultrasonic assisted extraction (UAE) for bioactive components: Principles, advantages, equipment, and combined technologies (2023) · cites this paper as [35]
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ULTRASOUND: Its Chemical, Physical and Biological Effects
Suslick, K. S., & Nyborg, W. L. (1990) · The Journal of the Acoustical Society of America · doi:10.1121/1.398864 · Cited by 1,100
Effect of ultrasound on the technological properties and bioactivity of food: a review
Soria, A. C., & Villamiel, M. (2010) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2010.04.003 · Cited by 1,035
Ultrasound: Its Chemical, Physical, and Biological Effects
Ritenour, E. R. (1989) · Radiology · doi:10.1148/radiology.173.1.136 · Cited by 937
Food proteins: A review on their emulsifying properties using a structure–function approach
Lam, R. S. H., & Nickerson, M. T. (2013) · Food Chemistry · doi:10.1016/j.foodchem.2013.04.038 · Cited by 896
Chandrapala, J., Zisu, B., Palmer, M. V., Kentish, S. E., & Ashokkumar, M. (2011) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2010.12.016 · Cited by 611
Food protein functionality: A comprehensive approach
Foegeding, E. A., & Davis, J. P. (2011) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2011.05.008 · Cited by 486
Jiang, J., Xiong, Y. L., & Chen, J. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf101045b · Cited by 329
Enhancement of Food Processes by Ultrasound: A Review
Tao, Y., & Sun, D. (2013) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2012.667849 · Cited by 326
Schröder, A., Berton‐Carabin, C., Venema, P., & Cornacchia, L. (2017) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2017.06.001 · Cited by 308
Li, S., Yang, X., Zhang, Y., Ma, H., Liang, Q., Qu, W., He, R., Zhou, C., & Mahunu, G. K. (2015) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2015.11.019 · Cited by 222
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Shen, L., Pang, S., Zhong, M., Sun, Y., Qayum, A., Liu, Y., Rashid, A., Xu, B., Liang, Q., Ma, H., et al. (2023) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2023.106646 · Cited by 892
“However, Huang et al. [35] observed the application of ultrasonic treatment for more than 10 min on soy protein isolate resulted in a significant increase in α -helix content, along with a noticeable decrease in the content of random coil structures.”
BackgroundSelf-citationNasrabadi, M. N., Doost, A. S., & Mezzenga, R. (2021) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2021.106789 · Cited by 774
Yan, S., Xu, J., Zhang, S., & Li, Y. (2021) · LWT · doi:10.1016/j.lwt.2021.110881 · Cited by 461
Self-citationThe functional modification of legume proteins by ultrasonication: A review
Gharibzahedi, S. M. T., & Smith, B. M. (2020) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2020.02.002 · Cited by 325
Yu, J., Xiao, K., Xu, H., Li, Y., Xue, Q., Xue, W., Zhang, A., Wen, X., Xu, G., & Huang, X. (2023) · Water Research · doi:10.1016/j.watres.2023.119866 · Cited by 296
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Metadata
- Authors
- Huang, L., Ding, X., Li, Y., & Ma, H.
- Affiliations
- Jiangsu University (CN)
- Corresponding author
- Huang, Liurong
- Venue
- Food Chemistry
- Publisher
- Elsevier BV
- Published
- 2019-05
- Volume
- 279
- Pages
- 114-119
- ISSN
- 0308-8146 (ISSN-L)
- OpenAlex
- W2903645087
- Cited by
- 224
- References
- 37
- Citations by year
- 2026: 34 · 2025: 37 · 2024: 45 · 2023: 34 · 2022: 25 · 2021: 23 · 2020: 19 · 2019: 7
- FWCI
- 11.53
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Food Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (31701540)
- Natural Science Foundation of Jiangsu Province (31701538, BK20170539)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Agricultural and Biological Sciences › Food Science › Protein Hydrolysis and Bioactive Peptides
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- soy protein isolate, ultrasound treatment, acid treatment, protein aggregation, protein secondary structure, emulsifying properties, emulsion stability, droplet size, protein solubility, helix content
- MeSH terms
- Circular Dichroism, Emulsions, Hydrochloric Acid, Particle Size, Solubility, Sonication, Spectrophotometry, Soybean Proteins, Protein Aggregates
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