The effects of in vitro gastrointestinal (GI) digestion on the antioxidative activity of hydrolysates prepared from chicken blood plasma and red blood cell (RBC) by pepsin and thermolysin were investigated. The pepsin-hydrolyzed plasma (PHP) showed the highest scavenging activity of ABTS radicals (P < 0.05). RBC and plasma hydrolysates prepared by pepsin were hydrolyzed by GI proteases to a greater extent than hydrolysates prepared by thermolysin as evidenced by MALDI-TOF mass spectra. The antioxidative activity of all digesta increased compared to their respective parent hydrolysates, and PHP digesta showed the highest activity (P < 0.05). The digesta of PHP and thermolysin-hydrolyzed plasma showed cytoprotective properties in a dose-dependent manner, and 100 μg/mL of PHP digesta exhibited the highest protection of HepG2 cells against tert-butyl hydroperoxide (P < 0.05). Based on dichloro-dihydro-fluorescein diacetate assay, PHP digesta exhibited the greatest intracellular reactive oxygen species scavenging activity of approximately 71% at 100 μg/mL (P < 0.05). The peptide sequencing of PHP digesta revealed that they contained less than 10 amino acid residues, with an average hydrophobicity of 18.6. Chicken blood plasma is a better protein source for protein hydrolysates, and their digesta showed higher antioxidant activity compared to RBCs.
Keywords: GI digestion; cellular antioxidant; chicken blood; hydrolysate; plasma.
© 2019 Poultry Science Association Inc.