Bile acid-binding capacity of peptide extracts obtained from chicken blood hydrolysates using HPLC

Bile acids are involved in the modulation of various metabolic processes facilitating the biliary excretion of endogenous and exogenous cholesterol. The objective of this study was to determine the glycocholic acid binding capacity (BC) of chicken blood hydrolysates using an optimized RP-HPLC method...

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Detalles Bibliográficos
Autores: Carrera-Alvarado, Gisela, Toldrá Vilardell, Fidel, Mora, Leticia
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2022
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/287081
Acceso en línea:http://hdl.handle.net/10261/287081
https://api.elsevier.com/content/abstract/scopus_id/85145257821
Access Level:acceso abierto
Palabra clave:Anticholesterolemic activity
Bile acid binding capacity
Chicken blood hydrolysates
Hypocholesterolemic peptides
Descripción
Sumario:Bile acids are involved in the modulation of various metabolic processes facilitating the biliary excretion of endogenous and exogenous cholesterol. The objective of this study was to determine the glycocholic acid binding capacity (BC) of chicken blood hydrolysates using an optimized RP-HPLC methodology. Samples were hydrolysed using a combination of five different enzymes. Alcalase and Protamex hydrolysates presented the highest BC, with mean values of 20.09% and 20.61%, respectively. Subsequently, both hydrolysates were ultrafiltered to obtain fractions >10 kDa, between 10 and 3 kDa, and <3 kDa, and the highest BC values were obtained for peptide fractions >10 kDa. Finally, the protein fragments (MW > 10 kDa) potentially responsible for BC were identified by LC-MS/MS. The results confirmed the relation of BC with the molecular weight of the peptides generated, suggesting that certain protein fragments generated from chicken blood could contribute to a positive impact on health by interfering with cholesterol metabolism.