Abstract

During the dry-curing of ham takes place a series of biochemical reactions among which proteolysis of muscle proteins is one of the most important. The result of this proteolysis is an accumulation of amino acids and oligopeptides which directly or indirectly contribute to the aroma, flavor and final quality of the ham. Although there is evidence of the presence of oligopeptides at the end of dry-curing, little is known about their amino acid sequences and the effect of these peptides on human health. In this sense, it is known that peptides can regulate different processes in the body exerting a positive impact on some functions of the body that may have an important influence on health. In the last decade, biologically active peptides have been isolated from different types of food. These peptides have been attributed bioactive properties such as antihypertensive, antioxidant or antimicrobial activity, among others. Given the evidence of the presence of peptides in dry-cured ham, the present Thesis investigated the presence of angiotensin I-converting enzyme (ACE) inhibitory activity and antioxidant activity in peptide fractions obtained from dry-cured ham. Moreover, the effect produced in systolic blood pressure of spontaneously hypertensive rats after the administration of peptide fractions possessing ACE-inhibitory activity was verified in vivo. The peptides responsible for the detected antihypertensive and antioxidant activities, were isolated and sequenced by liquid chromatography coupled to mass spectrometry. Thus, several peptides with in vitro ACE-inhibitory and antioxidant activity were identified as well as a peptide with an important in vivo antihypertensive activity.