Journal
JOURNAL OF FUNCTIONAL FOODS
Volume 1, Issue 2, Pages 199-207Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jff.2009.01.009
Keywords
Flaxseed; Protein hydrolysates; Bioactive peptides; Angiotensin converting enzyme; Renin; IC50; Enzyme inhibition kinetics
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Funding
- Advanced Foods and Materials Network of Centre of Excellence (AFMnet)
- Natural Sciences and Engineering Research Council of Canada (NSERC)
- Manitoba Health Research Council
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Enzymatic hydrolysates from flaxseed protein were investigated for in vitro inhibition of angiotensin I-converting enzyme (ACE) and renin activities. Pepsin, ficin, trypsin, papain, thermolysin, pancreatin and Alcalase were used to hydrolyze flaxseed proteins followed by fractionation using ultrafiltration to isolate low-molecular-weight peptides, and separation of the Alcalase hydrolysate into cationic peptide fractions. Using N-(3-[2-furyl]acryloyl)-phenylalanylglycylglycine as substrate, the protein hydrolysates showed a concentration-dependent ACE inhibition (IC50, 0.0275-0.151 mg/ml) with thermolysin hydrolysate and Alcalase cationic peptide fraction I (FI) showing the most potent activity. Flaxseed peptide fractions also showed no or moderate inhibitory activities against human recombinant renin (IC50, 1.22-2.81 mg/ml). Kinetics studies showed that the thermolysin hydrolysate and FI exhibited mixed-type pattern of ACE inhibition whereas cationic peptide fraction II inhibited renin in uncompetitive fashion. These results show that the protein components of flaxseed meal possess peptide amino acid sequences that can be exploited as potential food sources of anti-hypertensive agents. (C) 2009 Elsevier Ltd. All rights reserved.
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