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

Abstract

The influence of heating (100 °C; 0-15 min) on the relative molecular mass, protein unfolding and secondary structure of quinoa globulins was studied at pH 6.5 (low solubility), 8.5 and 10.5 (high solubility). The patterns of denaturation and aggregation varied with pH. Heating triggered the disruption of the disulfide bonds connecting the acidic and basic… (More)
DOI: 10.1016/j.foodchem.2015.08.069

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