Release of Angiotensin I-Converting Enzyme Inhibitory Peptides from Flaxseed (Linum usitatissimum L.) Protein under Simulated Gastrointestinal Digestion

Abstract

The scope of this study was to determine the ability of flaxseed (Linum usitatissimum L.) proteins to release angiotensin I-converting enzyme inhibitory (ACEI) peptides during simulated gastrointestinal (GI) digestion using a static (SM; no absorption in the intestinal phase) and a dynamic model (DM; simultaneous absorption of digested products in the intestinal phase via passive diffusion). Gastric and gastric + small intestinal digests of flaxseed proteins of both models possessed ACEI activity. The ACEI activity of the gastric + small intestinal digest in the DM (IC(50) unabsorbed, 0.05 mg N/mL; IC(50) absorbed, 0.04 mg N/mL) was significantly higher (p < 0.05) than that of the SM (IC(50), 0.39 mg N/mL). Two peptides, a pentapeptide (Trp-Asn-Ile/Leu-Asn-Ala) and a hexapeptide (Asn-Ile/Leu-Asp-Thr-Asp-Ile/Leu), were identified in the most active ACEI fraction (0.5-1 kDa) of the absorbable flaxseed protein digest by de novo sequencing.