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

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.