Quinoa protein: Composition, structure and functional properties

Dakhili, Samira; Abdolalizadeh, Leyla; Hosseini, Seyede Marzieh; Shojaee-Aliabadi, Saeedeh; Mirmoghtadaie, Leila

doi:10.1016/j.foodchem.2019.125161

Cited by 364Seed and Plant BiochemistryProteins in Food SystemsFood and Agricultural Sciences

Quinoa protein: Composition, structure and functional properties

Dakhili, Samira, Abdolalizadeh, Leyla, Hosseini, Seyede Marzieh, Shojaee-Aliabadi, Saeedeh, Mirmoghtadaie, Leila·2019·Food Chemistry

DOI 10.1016/j.foodchem.2019.125161

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Abstract

Quinoa (Chenopodium quinoa willd.) is an annual herbaceous flowering plant showing appropriate nutritional and functional properties due to its high quality protein with a wide amino acid spectrum, particularly rich in lysine. The mature quinoa seed predominantly consists of 11S-type globulin called chenopodin, comprising about 37% of the total protein, and also 2S albumin accounting for 35% of the seed protein both stabilized through disulfide bridges. Moreover, quinoa seed contains low concentration of prolamins (0.5-7% of total protein) making it suitable for patients with celiac disease. Different enzymatic, chemical and physical modification methods also can influence the structural and finally nutritional and functional properties of protein isolate. Consequently, considering appropriate nutritional and functional properties of quinoa protein, it can be considered as a good candidate to supply human food products.

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The effects of co-components depend on chemical identity, extraction retention, pH, ionic strength, oxidation state, and formulation.
“Their effects depend on chemical identity, extraction retention, pH, ionic strength, oxidation state, and formulation”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Dakhili et al., 2019
Saponins may be beneficial at low levels by assisting interfacial tension reduction, but detrimental at higher levels if they displace proteins from the interface or destabilize protein-dominated films.
“This distinction is important because saponins may be beneficial at low levels by assisting interfacial tension reduction, but detrimental at higher levels if they displace proteins from the interface or destabilize protein-dominated films”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Dakhili et al., 2019
Co-components in amaranth, buckwheat, and quinoa protein ingredients should be considered as active structural modifiers rather than passive impurities.
“Co-components in amaranth, buckwheat, and quinoa protein in gredients should be considered as active structural modifiers rather than passive impurities.”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Dakhili et al., 2019
Quinoa contains a lot of protein, a balanced range of amino acids, high lysine (5.1-6.4%) and methionine (0.4-1.0%), vitamins (A, C, and E), and many minerals.
“It contains a lot of protein, a balanced range of amino acids, and a lot of lysine (5.1–6.4%), and methionine (0.4–1.0%) contains vitamins (A, C, and E) and many types of minerals [89,113].”
From Nutritional and Functional New Perspectives and Potential Health Benefits of Quinoa and Chia Seeds (2023) · cites this paper as [113]

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Quinoa protein
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Authors: Dakhili, S., Abdolalizadeh, L., Hosseini, S. M., Shojaee-Aliabadi, S., & Mirmoghtadaie, L.
Affiliations: National Nutrition and Food Technology Research Institute (IR)
Corresponding author: Mirmoghtadaie, Leila
ORCID: Abdolalizadeh, Leyla
Hosseini, Seyede Marzieh
Mirmoghtadaie, Leila
Venue: Food Chemistry
Publisher: Elsevier BV
Published: 2019-11
Volume: 299
Pages: 125161
ISSN: 0308-8146 (ISSN-L)
DOI: 10.1016/j.foodchem.2019.125161
OpenAlex: W2957711347
Cited by: 363
References: 102
Citations by year: 2026: 40 · 2025: 64 · 2024: 69 · 2023: 63 · 2022: 56 · 2021: 46 · 2020: 23 · 2019: 2
FWCI: 2.87
Type: journal article
Language: en
Update notices: erratum (2020-04-25)
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Food Chemistry (publishedVersion)
PubMed (publishedVersion)
Funders: Shahid Beheshti University of Medical Sciences
Student Research Committee, Tabriz University of Medical Sciences
Topics: Life Sciences › Agricultural and Biological Sciences › Food Science › Seed and Plant Biochemistry
Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
Life Sciences › Agricultural and Biological Sciences › Food Science › Food and Agricultural Sciences
Keywords: quinoa protein, quinoa, 11S globulin, 2S albumin, prolamin, celiac disease, protein structure, amino acid composition, lysine, protein functional properties, protein extraction, disulfide bonds, protein modification
MeSH terms: Amino Acids, Celiac Disease, Disulfides, Humans, Plant Proteins, Seeds, Plant Proteins, Dietary, Chenopodium quinoa, Prolamins

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Quinoa protein: Composition, structure and functional properties

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