4.3 Article

Denaturation and in Vitro Gastric Digestion of Heat-Treated Quinoa Protein Isolates Obtained at Various Extraction pH

Journal

FOOD BIOPHYSICS
Volume 11, Issue 2, Pages 184-197

Publisher

SPRINGER
DOI: 10.1007/s11483-016-9429-4

Keywords

Quinoa; Protein; Heat processing; Denaturation; Digestibility; Extraction pH

Funding

  1. CONICYT (Formation of Advanced Human Capital Program), Chile
  2. IPOP Customized Nutrition program of Wageningen University and Research Centre

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The aim of this study was to determine the influence of heat processing on denaturation and digestibility properties of protein isolates obtained from sweet quinoa (Chenopodium quinoa Willd) at various extraction pH values (8, 9, 10 and 11). Pretreatment of suspensions of protein isolates at 60, 90 and 120 A degrees C for 30 min led to protein denaturation and aggregation, which was enhanced at higher treatment temperatures. The in vitro gastric digestibility measured during 6 h was lower for protein extracts pre-treated at 90 and 120 A degrees C compared to 60 A degrees C. The digestibility decreased with increasing extraction pH, which could be ascribed to protein aggregation. Protein digestibility of the quinoa protein isolates was higher compared to wholemeal quinoa flour. We conclude that an interactive effect of processing temperature and extraction pH on in vitro gastric digestibility of quinoa protein isolates obtained at various extraction pH is observed. This gives a first indication of how the nutritional value of quinoa protein could be influenced by heat processing, protein extraction conditions and other grain components.

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