| Literature DB >> 26434317 |
Chibuike C Udenigwe1, Abayomi P Adebiyi1, Alain Doyen2, Huan Li1, Laurent Bazinet2, Rotimi E Aluko3.
Abstract
Flaxseed protein isolate (FPI) contains high amount of arginine, which plays important physiological roles especially as nitric oxide precursor in the vascular endothelium. Arginine-rich peptides can be generated from FPI and used as a source of nitric oxide, which can produce in vivo vasodilatory effects during hypertension. Enzymatic hydrolysis of FPI with trypsin and pronase resulted in a hydrolysate that was fractionated using electrodialysis-ultrafiltration (EDUF). EDUF experiment resulted in migration of peptides to the anionic and cationic recovery compartments. Compared to FPI with 11% arginine, about one-third of the cationic fraction was composed of arginine. Thirteen potential peptide sequences were identified to be present in the cationic compartment of which 12 contained at least one arginine residue. None of the peptides identified from the anionic compartment contained arginine. Oral administration of the cationic peptides (200mg/kgbodywt.) to spontaneously hypertensive rats resulted in a more rapid decrease in systolic blood pressure when compared to similar amounts of FPI or the amino acid form of arginine. It was concluded that the rapid effect of the arginine-rich peptide product suggests faster rate of peptide absorption than amino acids and this may be exploited to provide fast relief from hypertension.Entities:
Keywords: Angiotensin converting enzyme; Arginine; Bioactive peptides; Electrodialysis; Flaxseed protein; Renin; Ultrafiltration
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Year: 2011 PMID: 26434317 DOI: 10.1016/j.foodchem.2011.11.024
Source DB: PubMed Journal: Food Chem ISSN: 0308-8146 Impact factor: 7.514