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

• Autores: Anaya Gonzáles, Roberta Brita, Mamani Aycachi, Raúl Antonio, Miranda Tomasevich, Tomás Yuret, Cóndor Alarcón, Reynán, Cundia Alarcón, Orlando Edwin, Borda Lizarbe, Marco Antonio
• Formato: artículo
• Fecha de Publicación: 2025
• Institución: Sociedad Química del Perú
• Repositorio: Revista de la Sociedad Química del Perú
• Lenguaje: español
• OAI Identifier: oai:rsqp.revistas.sqperu.org.pe:article/520
• Enlace del recurso: https://revistas.sqperu.org.pe/index.php/revistasqperu/article/view/520
• Nivel de acceso: acceso abierto
• Materia: Chenopodium quinoa; cultivars; fractionation; electrophoresis; reserve proteins; cultivares; fraccionamiento; electroforesis; proteínas de reserva

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.