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

Abstract

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) and cholesterol esterase (CE)-inhibiting potential, as depicted by lower half-maximal inhibitory concentration values (IC 50 values) compared with nonhydrolyzed camel whey proteins (CWP). Peptide sequencing and in silico data depicted that most BAP from CWPH could bind active site of PL, whereas as only 3 peptides could bind the active site of CE. Based on higher number of reactive residues in the BAP and greater number of substrate binding sites, FCCLGPVPP was identified as a potential CE-inhibitory peptide, and PAGNFLPPVAAAPVM, MLPLMLPFTMGY, and LRFPL were identified as PL inhibitors. Molecular docking of selected peptides showed hydrophilic and hydrophobic interactions between peptides and target enzymes. Thus, peptides derived from CWPH warrant further investigation as potential candidates for adjunct therapy for hypercholesterolemia.

Identification and characterization of cholesterol esterase and lipase inhibitory peptides from amaranth protein hydrolysates

“…For example, FGAPR, FPFVPAPT, and FPFPPTLGY could bind up to 13, 12, and 11 bound residues on the active sites of PL (i. e. Phe78, Phe216, His152, Ser153, and His264), respectively. Similar binding hot spots for lipase inhibiting peptides from camel whey protein hydrolysates have been reported by Baba et al (2021) . From the APHs (AB-4), peptide MPFLPR, FPFVGP, FPFPPTLGY, FGAPR and FPFVPAPT were predicted to bind to the highest number of hotspots on the active site of PL.…”

“…From this study, peptides that showed the ability to bind to important amino acids of lipase were of hydrophobic amino acid supremacy i.e. leucine and proline Ngoh et al, 2017 , Baba et al, 2021 observed similar results in pinto beans and camel whey protein hydrolysates, respectively. They reported that in most of the lipase inhibiting peptides, proline and leucine are identified as the interacting residues.…”

“…These outcomes are similar to those reported by ( Nagaoka et al, 2001 ) who had previously reported the number of residues in hypocholesterolemic peptides ranges from 5 to 20. ( Baba et al, 2021 ) and ( Mudgil et al, 2019a ) have also recently reported a similar number of amino acid in the identified peptides which were predicted to possess CEase and PL inhibitory properties. Moreover, peptides (GGV, IVG, and VGVL) from the Amaranth protein reported by Soares et al (2015) demonstrated inhibition of HMG-CoA reductase enzyme, which implies a promising hypocholesterolemic effect.…”

“…Amongst the identified bioactive peptides from APHs, peptide FPFVPAPT could establish a bond with two amino acid residues present in the catalytic triad (Ser 194 and His435), and Ala108, and Phe324 which are part of an active site residue of CEase suggesting the strong inhibitory potential of this peptide against CEase. The peptides that could bind the residues of Phe324 and His435 are particularly gaining attention as CEase inhibitors, as previously reported in bioactive peptides derived from camel milk protein hydrolysates ( Mudgil et al, 2019a ) and camel whey protein hydrolysates ( Baba et al, 2021 ).

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Conjoint application of ultrasonication and redox pair mediated free radical method enhances the functional and bioactive properties of camel whey-quercetin conjugates

“…Recently, production of modified whey-polyphenol conjugates with enhanced techno-functional as well as bioactive properties is generating high research interest and has been identified as the hotspot in the field of food science [13] . Moreover, recent research on whey proteins from camel milk is gaining considerable importance in today’s world due to its therapeutic properties [3] , [6] , [7] . Camel whey has been reported for their high techno-functional potential that warrants its use in food industry [32] , [33] , [68] .…”