New insights into the cholesterol esterase- and lipase-inhibiting potential of bioactive peptides from camel whey hydrolysates: Identification, characterization, and molecular interaction

Novel antihypercholesterolemic bioactive peptides (BAP) from peptic camel whey protein hydrolysates (CWPH) were generated at different time, temperature, and enzyme concentration (%). Hydrolysates showed higher pancreatic lipase- (PL; except 3 CWPH) cholesterol esterase (CE)-inhibiting potential, as depicted by lower half-maximal inhibitory values (IC50 values) compared with nonhydrolyzed proteins (CWP). Peptide sequencing in silico data that most BAP CWPH could bind active site of PL, whereas only the CE. Based on number reactive residues greater substrate binding sites, FCCLGPVPP was identified a potential CE-inhibitory peptide, PAGNFLPPVAAAPVM, MLPLMLPFTMGY, LRFPL PL inhibitors. Molecular docking selected hydrophilic hydrophobic interactions between target enzymes. Thus, derived warrant further investigation candidates for adjunct therapy hypercholesterolemia.