Exploration of corn distillers solubles from selective milling technology as a novel source of plant-based ACE inhibitory protein hydrolysates.

Plant-based protein concentrate (PC) was extracted from under-utilized corn distillers solubles comprising a distinctive heat-treated blend of corn and yeast proteins. Enzymolysis of PC with alcalase generated protein hydrolysate (PH) containing angiotensin converting enzyme (ACE) inhibitory peptides. A novel kinetic model is developed to elucidate enzymolysis kinetics of PC. The PH of greatest DH (∼25%) revealed maximum ACE inhibition (%). Fractionated PH (<3 kDa) had non-toxic and non-allergenic unique peptides encrypted with anti-ACE fragments. Promising bioactive peptides (PeptideRanker > 0.85) docked with ACE had free energies between -8.40 and -10.60 kcal.mol-1 greater than captopril (-6.34 kcal.mol-1). The yeast-derived RLLPF peptide interacted with all active pockets of ACE (S1, S2, S') via hydrogen-, polar- and hydrophobic-bonds. Docking results suggested that ARG522, VAL518, TRP357, TYR523, GLU384, ALA356, ARG124, HIS387, HIS410, ASN66, and ALA354 of ACE aided in stabilizing complexes with peptides. Thus, PH could be used as antihypertensive ingredient for feed, food, or pharmaceutical industries.