Digested total protein and protein fractions from chia seed (Salvia hispanica L.) had high scavenging capacity and inhibited 5-LOX, COX-1-2, and iNOS enzymes.

The objective was to identify and characterize peptides from digested total protein (DTP) and isolated protein fractions (DPF), and their potential antioxidant, anti-inflammatory and anti-atherosclerotic effects, from chia seed (Salvia hispanica L.). Total protein and protein fractions from chia seed underwent simulated gastrointestinal digestion. The sequence, physicochemical properties, and biological potential of peptides were determined using chemical, in silico, and biochemical assays. Peptides from DTP (n = 9) and DPF albumin (n = 12), globulin (n = 11), prolamin (n = 5) and glutelin (n = 17) had interaction with cyclooxygenase-2 (COX-2), p65- nuclear factor kappa B, lipoxygenase-1 (LOX-1) and toll-like receptor 4 (p < 0.05). DTP, and digested albumin, globulin, and glutelin showed scavenging capacity for superoxide, hydrogen peroxide, nitric oxide and DPPH (1,1-diphenyl-2-picrylhydrazyl), and inhibition of 5-LOX, COX-1-2, and inducible nitric oxide synthase (iNOS) enzymes (p < 0.05). Chia seed proteins has peptides with potential beneficial health effects highlighting the importance of chia consumption.