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New insights into the cholesterol esterase- and lipase-inhibiting potential of bioactive peptides from camel whey hydrolysates: Identification, characterization, and molecular interaction.
Baba, Waqas N; Mudgil, Priti; Baby, Bincy; Vijayan, Ranjit; Gan, Chee-Yuen; Maqsood, Sajid.
Afiliación
  • Baba WN; Department of Food Nutrition and Health, College of Food and Agriculture, United Arab Emirates University, 15551 Al Ain, United Arab Emirates.
  • Mudgil P; Department of Food Nutrition and Health, College of Food and Agriculture, United Arab Emirates University, 15551 Al Ain, United Arab Emirates.
  • Baby B; Department of Biology, College of Science, United Arab Emirates University, 15551 Al Ain, United Arab Emirates.
  • Vijayan R; Department of Biology, College of Science, United Arab Emirates University, 15551 Al Ain, United Arab Emirates.
  • Gan CY; Analytical Biochemistry Research Centre (ABrC), Universiti Sains Malaysia, 11800 USM, Penang, Malaysia.
  • Maqsood S; Department of Food Nutrition and Health, College of Food and Agriculture, United Arab Emirates University, 15551 Al Ain, United Arab Emirates. Electronic address: sajid.m@uaeu.ac.ae.
J Dairy Sci ; 104(7): 7393-7405, 2021 Jul.
Article en En | MEDLINE | ID: mdl-33934858
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.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Camelus / Esterol Esterasa Tipo de estudio: Diagnostic_studies Límite: Animals Idioma: En Revista: J Dairy Sci Año: 2021 Tipo del documento: Article País de afiliación: Emiratos Árabes Unidos

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Camelus / Esterol Esterasa Tipo de estudio: Diagnostic_studies Límite: Animals Idioma: En Revista: J Dairy Sci Año: 2021 Tipo del documento: Article País de afiliación: Emiratos Árabes Unidos