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

Waqas N. Baba, Priti Mudgil, Bincy Baby, Ranjit Vijayan, Chee Yuen Gan, Sajid Maqsood

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

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 (IC50 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.

Original languageEnglish
Pages (from-to)7393-7405
Number of pages13
JournalJournal of Dairy Science
Volume104
Issue number7
DOIs
Publication statusPublished - Jul 2021

Keywords

  • bioactive peptide
  • camel milk
  • cholesterol esterase
  • pancreatic lipase
  • whey protein

ASJC Scopus subject areas

  • Food Science
  • Animal Science and Zoology
  • Genetics

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