The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Functional and Structural Properties of 2S Soy Protein in Relation to Other Molecular Protein Fractions
Open accessAbstract
The purpose of this investigation is to develop a better understanding of the structure-function relationship of the 2S fraction of soy protein that has not been considered in earnest by the research community. Defatted soy flour was used to extract the three major fractions of the protein (2S, 7S, and 11S). It was found that 2S exhibits better foaming and emulsification properties than the other two molecular fractions. Work was extended to structural properties, which were monitored using spectrophotometry, atomic force microscopy, scanning electron microscopy, small-deformation dynamic oscillation on shear, and large-deformation compression testing. An experimental protocol utilizing glucono-delta-lactone (GDL), GDL with N-ethylmaleimide, or GDL with urea was capable of identifying the nature of molecular interactions responsible for gelation. Surprisingly, it was found that in the initial stages of structure formation, 2S fared better than 7S, with 11S exhibiting the highest rates of aggregation. Given time, however, 7S produced a firmer network with a better water-holding capacity than that of 2S. Non-covalent interactions, as opposed to disulfide bridging, were found to be largely responsible for the changing functionality of the molecular fractions throughout the experimentation from the formation of a vestigial structure to that of a mature gel.
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“Therefore, proteins rich in 11S and 7S globulins exhibit stronger gelation capacities (Tay et al. 2006), such as soy protein, pea protein, chickpea protein, kidney bean protein, and panda bean protein (Mundi and Aluko 2012;Pang et al. 2021;Zhu et al. 2022;Ge et al. 2022).”
From A Review of Gelation of Plant Proteins and Their Influencing Factors (2025) · cites this paper as Tay et al. 2006
Citations
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Cited by
Soy protein isolates: A review of their composition, aggregation, and gelation.
Zheng, L., Regenstein, J. M., Zhou, L., & Wang, Z. (2022) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12925 · Cited by 266
Physicochemical and Functional Properties of 2S, 7S, and 11S Enriched Hemp Seed Protein Fractions
Ajibola, C. F., & Aluko, R. E. (2022) · Molecules · doi:10.3390/molecules27031059 · Cited by 46
A Review of Gelation of Plant Proteins and Their Influencing Factors
Hui, D., Liang, W., Wang, R., Feng, X., & Tang, X. (2025) · Sustainable Food Proteins · doi:10.1002/sfp2.70037 · Cited by 12
Metadata
- Authors
- Tay, S. L., Kasapis, S., Perera, C. O., & Barlow, P. J.
- Affiliations
- National University of Singapore (SG)
- Venue
- Journal of Agricultural and Food Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2006-07-08
- Volume
- 54
- Issue
- 16
- Pages
- 6046-6053
- ISSN
- 0021-8561 (ISSN-L)
- 1520-5118
- OpenAlex
- W1964889438
- Cited by
- 28
- References
- 24
- Citations by year
- 2026: 2 · 2025: 2 · 2023: 3 · 2022: 4 · 2021: 1 · 2020: 2 · 2019: 1 · 2018: 1 · 2015: 1
- FWCI
- 3.66
- Type
- journal article
- Language
- en
- Open access
- green
- figshare.com
- Licence
- cc-by
- Locations
- Journal of Agricultural and Food Chemistry (publishedVersion)
- PubMed (publishedVersion)
- RMIT Research Repository (RMIT University Library) (submittedVersion)
- National University of Singapore (submittedVersion)
- Figshare (submittedVersion, cc-by)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Health Sciences › Nursing › Nutrition and Dietetics › Food composition and properties
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- structure-function relationship, foaming properties, emulsifying properties, protein gelation, protein aggregation, water holding capacity, non-covalent interactions, disulfide bonds, defatted soy flour, glucono-δ-lactone
- MeSH terms
- Chemistry, Physical, Gels, Hydrogen-Ion Concentration, Microscopy, Electron, Scanning, Structure-Activity Relationship, Time Factors, Soybean Proteins, Emulsifying Agents, Chemical Phenomena
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- CoChat. (2026). Citation check: Functional and Structural Properties of 2S Soy Protein in Relation to Other Molecular Protein Fractions. https://app.cochat.ai/papers/10.1021/jf060387a
- The paper
- Tay, S. L., Kasapis, S., Perera, C. O., & Barlow, P. J. (2006). Functional and Structural Properties of 2S Soy Protein in Relation to Other Molecular Protein Fractions. Journal of Agricultural and Food Chemistry. https://doi.org/10.1021/jf060387a
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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).
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