ArticleMolecules (Basel, Switzerland)2018
Characterizing the Structural and Functional Properties of Soybean Protein Extracted from Full-Fat Soybean Flakes after Low-Temperature Dry Extrusion.
Article in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 32 citations in OpenAlex.
- Beyond Mixed Utilization: Fractionation, Functional Divergence, and Precision Applications of Soybean 7S and 11S Globulins.Comprehensive reviews in food science and food safety · 2026Review
- Rapid Protein Extraction from Canola Meal Pre-Treated with Enzymatic Reactive Extrusion.Foods (Basel, Switzerland) · 2026Article
- Engineering Processes for Plant-Based Meat Analogs: Current Status and Future Outlook.Comprehensive reviews in food science and food safety · 2025Review
- The Potential of Fermentation-Based Processing on Protein Modification: A Review.Foods (Basel, Switzerland) · 2025Review
- Study on peanut protein oxidation and metabolomics/proteomics analysis of peanut response under hypoxic/re-aeration storage.Food chemistry: X · 2024Article
- Impacts of the Dynamic High-Pressure Pre-Treatment and Post-Treatment of Whey Protein Aggregates on Their Physicochemical Properties and Emulsifying Activities.Foods (Basel, Switzerland) · 2022Article
- Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies.Foods (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
The soy protein isolates (SPI) extracted from different extruded full-fat soybean flakes (FFSF), and their conformational and functional properties were characterized. Overall, the free thiol (SH) content of SPI increased when the extrusion temperature was below 80 °C and decreased at higher temperatures. Soy glycinin (11S) showed higher stability than β-conglycinin (7S) during extrusion. Results also indicated that the increase in some hydrophobic groups was due to the movement of hydrophobic groups from the interior to the surface of the SPI molecules at extrusion temperatures from 60 to 80 °C. However, the aggregation of SPI molecules occurred at extrusion temperatures of 90 and 100 °C, with decreasing levels of hydrophobic groups. The extrusion temperature negatively affected the emulsifying activity index (EAI); on the other side, it positively affected the emulsifying stability index (ESI), compared to unextruded SPI.
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Registered trials
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