PÉPTIDOS GENERADOS EN JAMÓN CURADO COMO MARCADORES DE CALIDAD
[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...
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| Tipo de recurso: | tesis doctoral |
| Fecha de publicación: | 2015 |
| País: | España |
| Institución: | Universitat Politècnica de València (UPV) |
| Repositorio: | RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia |
| Idioma: | español |
| OAI Identifier: | oai:riunet.upv.es:10251/55506 |
| Acceso en línea: | https://riunet.upv.es/handle/10251/55506 |
| Access Level: | acceso abierto |
| Palabra clave: | Péptidos Jamón curado Biomarcadores Proteolisis Oxidación Proteómica Espectrometría de masas Cuantificación Intensidad de pico Proteínas Péptidos inhibidores de ECA Células Caco-2 TECNOLOGIA DE ALIMENTOS |
| Sumario: | [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. |
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