Heat-induced denaturation and aggregation of protein in quinoa (Chenopodium quinoa Willd.) seeds and whole meal

[Display omitted] •Physical barriers hinder extraction of 20–25% of protein from quinoa whole meal.•Maximally 37% of seed proteins form SS-linked covalent aggregates during boiling.•11S Globulin monomers which easily dissociate are most prone to aggregate.•Albumins do not aggregate but partially lea...

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Veröffentlicht in:	Food chemistry 2022-03, Vol.372, p.131330-131330, Article 131330
Hauptverfasser:	Van de Vondel, Julie, Lambrecht, Marlies A., Delcour, Jan A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Chenopodin Chenopodium quinoa Covalent aggregation Disulfide cross-links Globulins Hot Temperature Light microscopy Protein Aggregates Protein Denaturation Protein extractability Pseudocereal Seeds Size exclusion chromatography
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