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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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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
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 ›
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