Plant-based proteins: Advanced extraction technologies, interactions, physicochemical and functional properties, food and related applications, and health benefits
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Their shared globulin/albumin basis provides a common starting point, but extraction pH, fraction recovery, co-component retention, and post-extraction processing shift them into different structural states, including soluble albumin-rich fractions, globulin-dominant oligomers, loose flocs, submicron particles, microgels, and fibrillar or β-sheet aggregates.
“Their shared globulin/albumin basis provides a common starting point, but extraction pH, fraction recovery, co-component retention, and post-extraction processing shift them into different structural states, including soluble albumin-rich fractions, globulindominant oligomers, loose flocs, submicron particles, microgels, and fibrillar or β -sheet aggregates”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Rashwan et al., 2025
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Experimental — accuracy not yet measuredPseudocereal proteins can shift between soluble globulin-like assemblies, dissociated subunits, colloidal particles, and heat- or pH-induced aggregates, leading to similar trade-offs among solubility, molecular emulsification, particle-assisted stabilization, and gelation.
“Like legume proteins, pseudocereal proteins can shift between soluble globulin-like assemblies, dissociated subunits, colloidal particles, and heat- or pH-induced aggregates, leading to similar trade-offs among solubility, molecular emulsification, particle-assisted stabilization, and gelation (Rashwan et al., 2025; Xu et al., 2023).”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Rashwan et al., 2025
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Experimental — accuracy not yet measuredLegumes and some oat protein systems provide a more relevant comparison for pseudocereal protein structure-function because they also contain substantial 7S/11S globulins and albumins.
“from a structure-function perspective, legumes and some oat protein systems provide a more relevant comparison because they also contain substantial 7S/11S globulins and albumins (Rashwan et al., 2025; Zhang et al., 2024a).”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Rashwan et al., 2025
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Cited by
Sorted by citations
Patil, N. D., Kumar, A., Bains, A., Fareed, M., Dhull, S. B., Nagraik, R., & Chawla, P. (2025) · Food Chemistry: X · doi:10.1016/j.fochx.2025.102608 · Cited by 15 · see citing works
RetractedYan, X., & Zhu, F. (2027) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113137
- Authors
- Rashwan, A. K., Osman, A. I., Abdelshafy, A. M., Mo, J., & Chen, W.
- Affiliations
- Department of Traditional Chinese Medicine, School of Medicine, Sir Run Run Shaw Hospital, Zhejiang University, Hangzhou, China
- School of Chemistry and Chemical Engineering, Queen’s University Belfast, Belfast, Northern Ireland, UK
- Department of Food Science and Technology, Faculty of Agriculture, Al-Azhar University-Assiut Branch, Assiut, Egypt
- Venue
- Critical Reviews in Food Science and Nutrition
- Publisher
- Informa UK Limited
- Published
- 2023-11-15
- Volume
- 65
- Issue
- 4
- Pages
- 667-694
- ISSN
- 1040-8398
- 1549-7852
- Cited by
- 122
- References
- 3
- Language
- en
- Funders
- National Key Research and Development Program of China (202)
- Zhejiang Provincial Key R&D Program of China (8)
- Open Project of Wencheng Joint Research Center of Big Health Industry of Zhejiang University
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