Isolation and evaluation of quinoa (Chenopodium quinoa Willd.) protein fractions: A nutritional and bio-functional approach to the globulin fraction
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Quinoa proteins similarly show chenopodin (11S globulin) as oligomeric assemblies (300-380 kDa) with smaller dissociation products and low-MW albumins (<20 kDa), but the aggregate fraction is particularly sensitive to extraction pH and processing history.
“Quinoa proteins similarly show che nopedin (11S globulin) as oligomeric assemblies (300-380 kDa) with smaller dissociation products and low-MW albumins ( < 20 kDa), but the aggregate fraction is particularly sensitive to extraction pH and pro cessing history”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Tavano et al., 2022
Quinoa also contain 7S/13S proglobulin at 45-60 kDa and 2S albumins at 8-16 kDa, whose relative intensity varies with cultivar and extraction pH.
“They also contain 7S/13S proglobulin at 45-60 kDa and 2S albumins at 8-16 kDa, whose relative intensity varies with cultivar and extraction pH”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Tavano et al., 2022
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Quinoa protein: Composition, structure and functional properties
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Cited by
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Yan, X., & Zhu, F. (2027) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113137
- Authors
- Tavano, O. L., Amistá, M. J. D. M., Del Ciello, G., Rodrigues, M. C. M., Bono Nishida, A. M., Valadares, L. A., Siqueira, B. M., Gomes, R. A. D. S., Parolini, M. T., & Silva Junior, S. I. D.
- ORCID
- Tavano, Olga Luisa
- Venue
- Current Research in Food Science
- Publisher
- Elsevier BV
- Published
- 2022
- Volume
- 5
- Pages
- 1028-1037
- ISSN
- 2665-9271
- PMC
- PMC9234336
- Cited by
- 41
- References
- 1
- Language
- en
- Licence
- Funders
- Fundação de Ensino e Pesquisa de Uberaba (nº921/2009)
- Instituto de Tecnologia de Alimentos
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