Flaxseed protein hydrolysate has been fractionated by electrodialysis with two ultrafiltration membranes (20 and 50 kDa) stacked in the system for the recovery of two specific cationic peptide fractions (KCl-F1 and KCl-F2). After 360 min of treatment, peptide migration increased as a function of time in KCl compartments. Moreover, the use of two different ultrafiltration membrane allowed concentration of the 300-400 and 400-500 Da molecular weight range peptides in the KCl-F1 and KCl-F2 fractions, respectively, compared to the initial hydrolysate. After mass spectrometry analysis, higher amounts of low molecular weight peptides were recovered in the KCl-F2 compartment while relatively higher molecular weight peptides were more detected in the KCl-F1 compartment. Amino acid analysis showed that His, Lys and Arg were especially concentrated in the KCl compartments. Finally, glucose-transport assay demonstrated that the KCl-F2 fraction increased glucose uptake while oral administration of KCl-F1 and final FPH decreased systolic blood pressure.
Keywords: ACE; AEM; Amino acids analysis; Antihypertensive activity; BSA; CEM; DSA; EDUF; Electrodialysis with ultrafiltration membrane; FPH; Flaxseed protein hydrolysate; Glucose uptake; HMWP; IEM; LMWP; MW; MWCO; SBP; SHR; UFM; angiotensin converting enzyme; anion-exchange membrane; bovine serum albumin; cation-exchange membrane; dimensionally-stable anode; electrodialysis with ultrafiltration membranes; flaxseed protein hydrolysate; high molecular weight peptide; ion-exchange membrane; low molecular weight peptide; molecular weight; molecular weight cut-off; spontaneously hypertensive rats; systolic blood pressure; ultrafiltration membrane.
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