Heat-denaturation and aggregation of quinoa (Chenopodium quinoa) globulins as affected by the pH value

•Disulfide bonds were disrupted by heating quinoa globulins at alkaline pH but not at neutrality.•The oligomeric proteins dissociated rapidly at highly alkaline pH.•Extensive disulfide-driven aggregation did not occur was not observed at highly alkaline pH.•Heat-treatments in this study did not alte...

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Veröffentlicht in:	Food chemistry 2016-04, Vol.196, p.17-24
Hauptverfasser:	Mäkinen, Outi E., Zannini, Emanuele, Koehler, Peter, Arendt, Elke K.
Format:	Artikel
Sprache:	eng
Schlagworte:	Alkali treatment Chenopodin Chenopodium quinoa - chemistry Circular Dichroism Globulins - chemistry Hot Temperature Hydrogen-Ion Concentration Molten globule Protein Denaturation Protein Structure, Secondary
Online-Zugang:	Volltext
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