Production of antihypertensive and antidiabetic peptide fractions from quinoa (Chenopodium quinoa Willd.) by electrodialysis with ultrafiltration membranes

A Quinoa Protein Hydrolysate Fractionated by Electrodialysis with Ultrafiltration Membranes Improves Maternal and Fetal Outcomes in a Mouse Model of Gestational Diabetes Mellitus

“…Quinoa was recognized by the Food and Agricultural Organization as a key food for the eradication of hunger, malnutrition, and poverty due to its high nutritional benefits, market value, and high adaptability to various growing conditions in terms of salinity, rain, temperature, and pest infections. [59] In this work, we used a methodology involving a three-step method of ex- Considering that the FQH fraction was the one with the highest yield and based on previous data from our group showing that this fraction was bioactive in cells [44] we decided to use this fraction of the hydrolysate for the study in vivo. Our results showed that a mean intake of 4.5 mL of a solution of 25 mg 10 mL −1 (mean intake of 11.3 mg per mice per day) was effective at preventing metabolic derangements in pregnant mice with GDM, including glucose intolerance, fetal overweight, and hepatic TG accumulation and at stimulating molecular pathways downstream insulin signaling in the liver.…”

“…The protein extraction from quinoa followed the protocol recently described by González‐Muñoz et al. [ 44 ] Briefly, quinoa flour was dispersed in alkaline water (NaOH 40 mM, pH ≈12) in a ratio of 1:30 w/v for 4 h. The dispersion was then centrifuged (Hettich Universal, 320R, UK) at 4200 × g for 12 min at 8 °C, after which the soluble protein fraction in the supernatant was precipitated at pH 3.5 (isoelectric point) using HCl 2N and centrifuged at 4500 × g for 7 min at 8 °C. Finally, the pH of the protein concentrate was adjusted to pH 7.0 with NaOH and freeze‐dried (Labconco Freezone plus, Kansas, MO, USA) and stored hermetically at −40 °C until further use.…”

“…The electrodialysis arrangement was represented four compartments, two for the recuperation and concentration of peptides, one was located between the UFM1 and anionic EM and the other one ubicated between the UFM2 and the cationic EM as described by González‐Muñoz et al. [ 44 ] On other compartment was for the electrode rinsing solution, and the last one corresponded to the feed solution. Each electro‐separation (batch production) was carried out at a QH concentration of 2% w/v (protein base) during 6 h at room temperature (25–30 °C) and under a constant electric field of 20 V cm −1 .…”

“…The pH of the compartments was maintained constant at pH 7.0 using 1.0 M NaOH or HCl [ 45 ] as well as the conductivity (5.0–5.5 mS cm −1 ) by the incorporation of KCl for constant peptide migration. [ 46 ] As described in González‐Muñoz et al., [ 44 ] three different quinoa peptide fractions resulted from the EDUF fractionation: one anionic and one cationic fraction (both composed by peptides smaller than 20 kDa), and an neutral fraction of the quinoa hydrolysate (FQH) which did not migrate, and was probably composed by peptides with neutral charge, or charged peptides with a molecular weight higher than the UFM (20 kDa) or with not time to migrate to any compartment (anionic or cationic).…”

“…Electrodialysis with ultrafiltration membranes (EDUF) fractionation protocol was performed according to González-Muñoz et al [44] Briefly, an electrodialysis cell of 100 cm 2 of effective sur-face area was used and the difference of voltage between the anode and cathode was given by a power source of 0-100 V. The electrodialysis cell was composed of four membranes: one cationic exchange membrane (EM), one anionic exchange EM, and two polyether sulfone ultrafiltration membrane (UFM) with molecular weight cut-off of 20 kDa. The electrodialysis arrangement was represented four compartments, two for the recuperation and concentration of peptides, one was located between the UFM1 and anionic EM and the other one ubicated between the UFM2 and the cationic EM as described by González-Muñoz et al [44] On other compartment was for the electrode rinsing solution, and the last one corresponded to the feed solution. Each electroseparation (batch production) was carried out at a QH concentration of 2% w/v (protein base) during 6 h at room temperature (25-30 °C) and under a constant electric field of 20 V cm −1 .…”