Recovery and characterisation of quinoa protein via neutral to alkaline extraction: Protein profiles and heat-induced aggregation behaviour
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Higher extraction pH and harsher treatments increase void-volume aggregates, which is consistent with irreversible association and altered solubility and interfacial behavior.
“Higher extraction pH and harsher treatments increase void-volume aggregates, which is consistent with irreversible association and altered solubility and interfacial behavior”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Cui et al., 2025
The Results sections on solubility and heat-induced aggregation (page unavailable) link extreme alkaline extraction and heating to aggregation and reduced solubility; the interfacial-properties section reports differences between extraction pHs. But the paper does not identify the aggregates as void-volume aggregates or establish irreversible association. It also reports less additional heat-induced aggregation for protein extracted at pH 11 than at pH 9, so higher extraction pH does not uniformly increase aggregation under harsher treatment. (LLM, conf=0.86)
Experimental — accuracy not yet measuredThese treatments also increase ζ-potential magnitude and hydrophobic exposure while maintaining recognizable globulin structures.
“These treatments also increase ζ -potential magnitude and hydrophobic exposure while maintaining recognizable globulin struc tures”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Cui et al., 2025
The Results and discussion sections on solubility and heat-induced aggregation report hydrophobic-group exposure under extreme alkaline conditions and greater retention of globular structures at mild alkaline pH. But the solubility section reports a decrease, not an increase, in surface charge from pH 9 to pH 11. The paper therefore does not support all three changes occurring together; page numbers were not available in our copy. (LLM, conf=0.85)
Experimental — accuracy not yet measuredReported protein contents, Osborne-type fractions, SDS-PAGE profiles, SEC/HPSEC distributions, DLS particle size, ζ-potential, FTIR/CD spectra, and fluorescence responses are all sensitive to extraction pH, solvent system, ionic strength, defatting, dilution, filtration, drying, and residual co-components.
“Reported protein contents, Osborne-type fractions, SDS-PAGE profiles, SEC/H PSEC distributions, DLS particle size, ζ -potential, FTIR/CD spectra, and fluorescence responses are all sensitive to extraction pH, solvent system, ionic strength, defatting, dilution, filtration, drying, and residual co-components”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Cui et al., 2025
The Results and discussion section reports that extraction pH changed protein yield, purity, and co-extracted carbohydrate content; the Conclusions also report effects on protein profiles and heat-induced aggregation. The paper does not establish that all the listed measurements are sensitive to every listed preparation factor. Defatting and freeze-drying appear as fixed preparation steps, not variables tested for their effects; the cited passages do not address Osborne fractions, SEC/HPSEC, ζ-potential, FTIR/CD, or fluorescence. Page numbers were not available in our copy. (LLM, conf=0.89)
Experimental — accuracy not yet measuredThermal and alkaline treatments tend to increase β-sheets, β-turns and decrease α-helix, consistent with enhanced β-aggregation and cross-linking.
“Thermal and alkaline treatments tend to increase β -sheets, β -turns and decrease α -helix, consistent with enhanced β -aggregation and cross-linking”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Cui et al., 2025
The Results and discussion section (“Impact of extraction pH on the heat-induced aggregation of QPI”; page unavailable) reports heat-induced aggregation and suggests covalent interactions contribute to insoluble aggregates. It does not report increases in β-sheets or β-turns, a decrease in α-helix, or a link between those specific structural changes and aggregation; searches for those secondary-structure terms found no supporting passage. (LLM, conf=0.86)
Experimental — accuracy not yet measuredHigher extraction pH, from 9 to 11, and thermal treatments tend to increase void-volume aggregates and β-associated aggregation.
“Higher extraction pH, from 9 to 11, and thermal treatments tend to increase void-volume aggregates and β -associated aggregation.”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Cui et al., 2025
Extreme alkaline extraction, such as pH 11, can accelerate formation of high-MW aggregates; these aggregates reduce solubility and slow interfacial rearrangement, often weakening emulsification despite more unfolding.
“However, extreme alkaline extraction, such as pH 11, can accelerate formation of high-MW aggregates. These aggregates reduce solubility and slow interfacial rearrangement, which often weaken emulsification despite more unfolding (Cui et al., 2025; Liu et al., 2023; Wang et al., 2025a).”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Cui et al., 2025
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Cites
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Current insights into protein solubility: A review of its importance for alternative proteins
Grossmann, L., & McClements, D. J. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.108416 · Cited by 367 · see citing works
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Cited by
Sorted by citations
Yan, X., & Zhu, F. (2027) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113137
- Authors
- Cui, H., Roy, D., Li, S., Loo, T. S., Guo, Q., & Ye, A.
- Venue
- Current Research in Food Science
- Publisher
- Elsevier BV
- Published
- 2025
- Volume
- 11
- Pages
- 101214
- ISSN
- 2665-9271
- PMC
- PMC12529351
- Cited by
- 9
- References
- 3
- Language
- en
- Licence
- Funders
- Ministry for Business Innovation and Employment (MAUX 2013)
- Ministry of Business, Innovation and Employment
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