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Enhancing quinoa (Chenopodium quinoa Willd) protein extraction: Alkaline solubilization coupled to isoelectric precipitation effects on structure, digestibility and antinutrients

Manzanilla-Valdez, Maria Lilibeth, Boesch, Christine, Martinez-Villaluenga, Cristina, Montaño, Sarita, Hernández-Álvarez, Alan Javier·2024·Food Hydrocolloids for Health
DOI 10.1016/j.fhfh.2024.100191
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  • Saponins are most relevant in quinoa protein ingredients because their retention depends strongly on washing, soaking, alkaline extraction, and isoelectric precipitation conditions.

    “Saponins are most relevant in quinoa protein ingredients because their retention depends strongly on washing, soaking, alkaline extrac­ tion, and isoelectric precipitation conditions”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Manzanilla-Valdez et al., 2024

    Section 4.10.6 (page unavailable) reports saponin levels in quinoa protein ingredients and suggests that water-soluble saponins may become concentrated during protein extraction. It does not establish that retention depends strongly on washing, soaking, alkaline extraction, or isoelectric precipitation conditions individually, or that saponins are the most relevant compounds in these ingredients. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

  • In quinoa protein ingredients, alkaline solubilization followed by isoelectric precipitation can alter antinutritional factors, including phytic acid and saponins, while also changing secondary structure and in vitro protein digestibility.

    “In quinoa protein ingredients, alkaline solubilization followed by isoelectric precipitation can alter antinutritional factors, including phytic acid and saponins, while also changing secondary structure and in vitro protein digestibility”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Manzanilla-Valdez et al., 2024

  • These extraction-dependent changes suggest that phytate and minerals should be considered when interpreting digestibility, gelation, and aggregation behavior, especially in systems where calcium, magnesium, or other ions participate in network formation.

    “These extraction-dependent changes suggest that phytate and minerals should be considered when interpreting digestibility, gelation, and aggregation behavior, especially in systems where calcium, magnesium, or other ions participate in network formation”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Manzanilla-Valdez et al., 2024

  • As a polyanionic antinutrient, phytate can bind minerals and may influence protein aggregation, mineral availability, and enzyme accessibility through charge screening, ion-mediated association, or mineral chelation.

    “As a polyanionic antinutrient, phytate can bind minerals and may influence protein aggregation, mineral availability, and enzyme accessibility through charge screening, ionmediated association, or mineral chelation”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Manzanilla-Valdez et al., 2024

  • Alkaline solubilization coupled with isoelectric precipitation modified quinoa protein secondary structure and improved in vitro digestibility, while also changing antinutritional components such as phytic acid, saponins, oxalates, and phenolics.

    “alkaline solubilization coupled with isoelectric precipitation modified quinoa protein secondary structure and improved in vitro digestibility, while also changing antinutritional components such as phytic acid, saponins, oxalates, and phenolics (Manzanilla-Valdez et al., 2024).”

    From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Manzanilla-Valdez et al., 2024

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Cited by

Sorted by citations

Authors
Manzanilla-Valdez, M. L., Boesch, C., Martinez-Villaluenga, C., Montaño, S., & Hernández-Álvarez, A. J.
ORCID
Hernández-Álvarez, Alan Javier
Venue
Food Hydrocolloids for Health
Publisher
Elsevier BV
Published
2024-12
Volume
6
Pages
100191
ISSN
2667-0259
DOI
10.1016/j.fhfh.2024.100191
Cited by
9
References
4
Language
en
Licence
Funders
Consejo Nacional de Humanidades, Ciencias y Tecnologías

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