MOLECULAR CHARACTERISATION OF PROTEINS FROM FOUR COMMERCIAL CULTIVARS OF Chenopodium quinoa Willd., Ayacucho

Abstract

The protein fractions from four commercial cultivars of Chenopodium quinoa, sourced from the districts of Acocro, Chiara, and Acos Vinchos, were characterized using SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) and quantified via the Bradford method. Electrophoretic profiles revealed 3–11 bands with molecular weights ranging from 5 to 123 kDa for albumins; 1–10 bands from 9 to 105 kDa for 7S globulins; 2–9 bands from 11 to 75 kDa for 11S globulins; 1–3 bands from 11 to 16 kDa for prolamins; and 1–7 bands from 13 to 61 kDa for glutelins. Protein quantification showed the highest concentration of 7S globulins at 25.15 mg/mL (in the Red from Acocro cultivar), while 11S globulins reached 19.46 mg/mL (in the Acos Vinchos Red cultivar). Albumins varied from 6.56 to 19.3 mg/mL (highest in the Black cultivar from Chiara), prolamins from 2.21 to 7.57 mg/mL, and glutelins from 7.86 to 16.5 mg/mL. Overall, these cultivars exhibited variability in molecular characteristics, with each displaying a distinct electrophoretic profile of protein bands.