TY - JOUR
T1 - New insights into the cholesterol esterase- and lipase-inhibiting potential of bioactive peptides from camel whey hydrolysates
T2 - Identification, characterization, and molecular interaction
AU - Baba, Waqas N.
AU - Mudgil, Priti
AU - Baby, Bincy
AU - Vijayan, Ranjit
AU - Gan, Chee Yuen
AU - Maqsood, Sajid
N1 - Funding Information:
The authors are grateful to United Arab Emirates University for funding this research through a research grants (UPAR-31F094) awarded to PI, Sajid Maqsood. The University Sains Malaysia RUI grant (1001/CABR/8011045) to Chee-Yuen Gan is also acknowledged. Hassan M. Hassan (Department of Food Nutrition and Health, UAE University) is acknowledged for RP-UPLC analysis. The authors declare that they have no conflict of interest.
Publisher Copyright:
© 2021 American Dairy Science Association
PY - 2021/7
Y1 - 2021/7
N2 - 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.
AB - 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.
KW - bioactive peptide
KW - camel milk
KW - cholesterol esterase
KW - pancreatic lipase
KW - whey protein
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U2 - 10.3168/jds.2020-19868
DO - 10.3168/jds.2020-19868
M3 - Article
C2 - 33934858
AN - SCOPUS:85104957903
SN - 0022-0302
VL - 104
SP - 7393
EP - 7405
JO - Journal of Dairy Science
JF - Journal of Dairy Science
IS - 7
ER -