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

被引：110

作者：

Escudero, Elizabeth ^{[1
]}

Mora, Leticia ^{[1
]}

Toldra, Fidel ^{[1
]}

机构：

[1] CSIC, Inst Agroquim & Tecnol Alimentos, Valencia 46980, Spain

来源：

FOOD CHEMISTRY | 2014年 / 161卷

关键词：

Dry-cured ham; ACE inhibitory peptides; Processing; Gastrointestinal digestion; Mass spectrometry; FOOD-DERIVED PEPTIDES; CONVERTING-ENZYME; BIOACTIVE PEPTIDES; ANTIHYPERTENSIVE PEPTIDES; PURIFICATION; PROTEINS; IDENTIFICATION; FERMENTATION; IMPACT; PH;

D O I：

10.1016/j.foodchem.2014.03.117

中图分类号：

O69 [应用化学];

学科分类号：

070301 [无机化学];

摘要：

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 degrees 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 mu M. Peptides IAGRP and PTPVP have also been identified in the processed sample (6 min at 117 degrees 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. (C) 2014 Elsevier Ltd. All rights reserved.

引用

页码：305 / 311

页数：7

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