Stability of ACE inhibitory ham peptides against heat treatment and in vitro digestion

Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from Spanish dry-cured ham have been examined for their stability during processing and after in vitro digestion. Results indicate that peptides preserved almost the same ACE inhibitory activity before and after applying diverse heati...

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Detalles Bibliográficos
Autores: Escudero, Elizabeth, Mora, Leticia, Toldrá Vilardell, Fidel
Tipo de recurso: artículo
Fecha de publicación:2014
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/114232
Acceso en línea:http://hdl.handle.net/10261/114232
Access Level:acceso abierto
Palabra clave:Dry-cured ham
Mass spectrometry
Processing
Gastrointestinal digestion
ACE inhibitory peptides
Descripción
Sumario:Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from Spanish dry-cured ham have been examined for their stability during processing and after in vitro digestion. Results indicate that peptides preserved almost the same ACE inhibitory activity before and after applying diverse heating (from 50 to 117 °C), times of processing (from 3 to 60 min) and simulated in vitro digestion with gastrointestinal proteases. Peptides KAAAAP, AAPLAP, KPVAAP, IAGRP, and KAAAATP were the most potent peptides with IC50 values ranging from 12.37 to 25.94 μM. Peptides IAGRP and PTPVP have also been identified in the processed sample (6 min at 117 °C), and in the in vitro digested sample. This study proves the high stability of ACE inhibitory peptides derived from Spanish dry-cured ham against temperature of processing and gastrointestinal digestion as well as the powerful ACE inhibitory activity of some of the peptides identified in Spanish dry-cured ham.