Corn distillers solubles as a novel bioresource of bioactive peptides with ACE and DPP IV inhibition activity: characterization, in silico evaluation, and molecular docking

This study aimed to investigate the biological potential of underutilized and low-value corn distillers solubles, containing a unique unexplored blend of heat-treated corn and yeast proteins, from the bioethanol industries, by bioinformatic and biochemical approaches. Protein hydrolysates were produced by applying four commercially accessible proteases, among which alcalase provided the best results in terms of yield, degree of hydrolysis, molecular weight, number of proteins, bioactive peptides, and deactivation against anti-angiotensin I-converting enzyme (ACE) and anti-dipeptidyl peptidase IV (DPP IV). The optimal conditions to produce anti-ACE and anti-DPP IV peptides were using alcalase for 10.82 h and an enzyme : substrate ratio of 7.90 (%w/w), with inhibition values for ACE and DPP IV of 98.76 ± 1.28% and 34.99 ± 1.44%, respectively. Corn (α-zein) and yeast (glyceraldehyde-3-phosphate dehydrogenase) proteins were mainly suitable, upon enzymolysis, for the release of bioactive peptides. The peptides DPANLPWG, FDFFDNIN, WNGPPGVF, and TPPFHLPPP inhibited ACE more effectively as verified with binding energies of -11.3, -11.6, -10.5, and -11.6 kcal mol-1, respectively, as compared to captopril (-6.38 kcal mol-1). Compared with the binding energy of sitagliptin (-8.6 kcal mol-1), WNGPPGVF (-9.6 kcal mol-1), WPLPPFG (-9.8 kcal mol-1), LPPYLPS (-9.7 kcal mol-1), TPPFHLPPP (-10.1 kcal mol-1), and DPANLPWG peptides (-10.1 kcal mol-1) had greater inhibition potential against DPP IV. The peptides impeded ACE and DPP IV majorly via hydrophobic and hydrogen linkage interactions. The key amino acids TYR523, GLU384, and HIS353 were bound to the catalytic sites of ACE and GLN553, GLU206, PHE364, VAL303, and THR304 were bound to the DPP IV enzyme. The PHs can be used as ingredients in the feed or food industries with possible health advantages.