4.7 Article

Antioxidant and Angiotensin Converting Enzyme-Inhibitory Properties of a Flaxseed Protein-Derived High Fischer Ratio Peptide Mixture

Journal

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 58, Issue 8, Pages 4762-4768

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/jf100149w

Keywords

Flaxseed protein; Fischer ratio; activated carbon; branched-chain amino acids; aromatic amino acids; antioxidant; angiotensin converting enzyme

Funding

  1. Manitoba Agriculture and Rural Development Initiative (ARDI)
  2. Natural Sciences and Engineering Research Council of Canada (NSERC)

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Hydrolysis of flaxseed proteins using thermolysin and pronase followed by mixing with activated carbon, centrifugation and filtration yielded a filtrate (peptide mixture) with a Fischer ratio (branched-chain amino acids/aromatic amino acids) of 23.65 and a phenylalanine + tyrosine content of 1.11%. Gel permeation chromatography showed that the flaxseed peptide sample contained mainly low molecular weight peptides (<4 kDa). The high Fischer ratio peptide sample exhibited antioxidant property by scavenging 2,2-diphenyl-1-picrylhydrazyl radical, superoxide radical, hydroxyl radical, and also by protecting linoleic acid from oxidation. In addition, the peptide mixture showed potential antihypertensive properties by inhibiting angiotensin I-converting enzyme in a mixed-type inhibition pattern. Protein hydrolysates with Fischer ratio higher than 20 and phenylalanine + tyrosine content lower than 2% have been used to treat patients with hepatic encephalopathy; thus, this multifunctional flaxseed peptide mixture could be used to formulate food products with multiple human health benefits during liver diseases, oxidative stress and hypertension.

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