Abstract

[EN] A series of biochemical reactions responsible for aroma, color, texture and flavour of the final product occur during the dry-cured ham processing. Among these reactions, proteolysis of muscle proteins is one of the most important, resulting in the generation of a large amount of peptides which could be used as quality markers of dry-cured ham. In this sense, proteomic techniques based on mass spectrometry have become a fundamental tool for the identification of peptides naturally generated throughout the dry-cured ham processing. So, the present Thesis has been focused on the study of the intense degradation of three proteins present in dry-cured ham: LIM domain-binding protein 3, ubiquitin-60S ribosomal protein and titin protein, identifying the peptide sequences generated at different times along the process and evaluating their potential as markers of dry-cured ham processing time. Moreover, peptide oxidation that occurs during dry-curing process has been studied due to its importance on final quality of dry-cured ham as well as its influence on the nutrititional and sensory characteristics, showing oxidation of methionine residues in numerous peptides generated from the degradation of the major myofibrillar proteins. Besides the identification of peptidic sequences, recent advances in mass spectrometry techniques have allowed the precise quantitation of proteins in complex mixtures. So, a label-free methodology has been optimized for the relative quantitation of major sarcoplasmic proteins from the quantitation of the generated peptides and the study of the proteolytic degradation along the dry-cured ham processing. This methodology represents an advance regarding quantitative methods used to date as it allows a simple, accurate and reliable evaluation of changes in the abundance of proteins throughout the dry-cured ham processing. Several recent studies have been focused on the study of the potential of dry-cured ham as a source of bioactive peptides, mainly those showing angiotensin I-converting enzyme (ACE) inhibitory activity. However, it is not clear whether these peptides are able to cross the intestinal barrier and reach the blood stream in an active form. Thus, in the present Thesis the transepithelial transport of dry-cured ham peptides having ACE inhibitory activity has been simulated through a Caco-2 cell monolayer, showing the absorption of intact peptides or fragments generated by the action of intestinal peptidases, which could exert an in vivo antihypertensive effect.; [ES] Durante el proceso de elaboracion del jamon curado tienen lugar una serie de reacciones bioquimicas responsables del aroma, color, textura y sabor del producto final. Entre estas reacciones destaca la intensa proteolisis de las proteinas musculares, cuyo resultado es la generacion de una gran cantidad de peptidos algunos de los cuales podrian ser utilizados como marcadores de calidad del jamon. En este sentido, las tecnicas proteomicas basadas en espectrometria de masas son una herramienta fundamental para la…

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