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Modulation of soy protein isolate gel properties by a novel “two-step” gelation process: Effects of pre-aggregation with different divalent sulfates
Abstract
A novel pre-aggregation process prior to gelation was applied to modulate the aggregation and gelation pathway of soy protein isolate (SPI). SPI dispersions were pre-aggregated with CaSO 4 , MgSO 4 or ZnSO 4 at 0-15 mM and then gelled by adding CaSO 4 up to a final salt concentration of 35 mM. Compared with the sample without pre-aggregation, the storage modulus of SPI gels pre-aggregated with 10 mM CaSO 4 , 10 mM MgSO 4 , and 2.5 mM ZnSO 4 were increased by 50.5%, 35.7%, and 63.6%, respectively. The fracture stress, texture profile analysis parameters, and water holding capacity were markedly improved by an appropriate level of pre-aggregation. To a certain extent, pre-aggregation could promote the formation of uniform structure with thicker strands, whereas over-aggregation resulted in a coarser network, which was correlated with the volume-mean diameter (D 4,3 ) of pre-aggregated SPI particles. The results are of great value for further understanding of gelation mechanism of proteins.
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“Salt ions facilitate protein gelation by decreasing electrostatic repulsion between protein molecules and forming salt bridges (Lu et al. 2010;Wang et al. 2022).”
From A Review of Gelation of Plant Proteins and Their Influencing Factors (2025) · cites this paper as Wang et al. 2022
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The development history and recent updates on soy protein-based meat alternatives
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Effects of succinylation on the structure and thermal aggregation of soy protein isolate
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Guo, R., Liu, L., Huang, Y., Lv, M., Zhu, Y., Wang, Z., Zhu, X., & Sun, B. (2023) · Food Research International · doi:10.1016/j.foodres.2023.113124 · Cited by 96
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Ye, X., Wei, L., Sun, L., Xu, Q., Cao, J., Li, H., Pang, Z., & Liu, X. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.135397 · Cited by 60
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Metadata
- Authors
- Wang, X., Yu, M., Wang, Z., Luo, K., Adhikari, B., Miao, S., & Liu, S.
- Affiliations
- Fuzhou University (CN)
- China Rural Technology Development Center (CN)
- Hunan Agricultural University (CN)
- RMIT University (AU)
- Teagasc - The Irish Agriculture and Food Development Authority (IE)
- Corresponding author
- Miao, Song
- Liu, Shutao
- Venue
- Food Chemistry
- Publisher
- Elsevier BV
- Published
- 2022-11
- Volume
- 394
- Pages
- 133515
- ISSN
- 0308-8146 (ISSN-L)
- OpenAlex
- W4282960932
- Cited by
- 38
- References
- 39
- Citations by year
- 2026: 11 · 2025: 12 · 2024: 8 · 2023: 7
- FWCI
- 3.42
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Food Chemistry (publishedVersion)
- PubMed (publishedVersion)
- RMIT Research Repository (RMIT University Library) (submittedVersion)
- Figshare (submittedVersion)
- Funders
- National Natural Science Foundation of China (32101986)
- Natural Science Foundation of Fujian Province (2020J05128)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
- Health Sciences › Nursing › Nutrition and Dietetics › Food composition and properties
- Keywords
- soy protein isolate, protein gelation, pre-aggregation, calcium sulfate, magnesium sulfate, zinc sulfate, gel mechanical properties, storage modulus, fracture stress, texture profile analysis, water holding capacity, protein aggregation, gel network structure
- MeSH terms
- Gels, Rheology, Sulfates, Water, Soybean Proteins
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