Publication: Obtención de péptidos alimentarios mediante hidrólisis enzimática con efectos sobre la salud intestinal
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2016-08-10
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Universidad Complutense de Madrid
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Abstract
En la presente Tesis Doctoral, se estudió la obtención e identificación de péptidos alimentarios mediante el uso de hidrólisis enzimática y sus efectos sobre la salud gastrointestinal. La secuenciación y cuantificación de los péptidos se realizó mediante cromatografía de líquidos de alta eficacia en fase inversa acoplada a espectrometría de masas en tándem (RP-HPLC-MS/MS). Se analizaron distintos hidrolizados y digeridos gastrointestinales de caseínas, proteínas de suero de leche y lunasina. Inicialmente, se propone la producción de caseinofosfopéptidos (CPPs) mediante la hidrólisis con tripsina de un subproducto de caseína generado durante la fabricación de un ingrediente funcional con actividad antihipertensiva. La identificación y la semi-cuantificación de CPPs revelaron algunos cambios cualitativos y cuantitativos en los CPPs generados en los hidrolizados con distintas condiciones de tiempo de hidrólisis y precipitación selectiva. Una vez realizada la identificación de CPPs en los hidrolizados trípticos, el subproducto también se sometió a un proceso de digestión gastrointestinal simulando las condiciones fisiológicas. La comparación de los péptidos resultantes mostró gran homología en las secuencias de CPPs formados por la hidrólisis con tripsina y la digestión gastrointestinal simulada. Se observó que algunas regiones de αS1-caseína, concretamente las comprendidas entre los residuos (43-59) y (60-74), de la αs1-caseína y los residuos (1-25) y (30-50) de β-caseína, fueron capaces de resistir tanto a la hidrólisis con tripsina como a la digestión gastrointestinal. Por lo tanto, se demuestra que el subproducto industrial puede ser empleado como fuente de CPPs para favorecer la absorción de minerales a nivel intestinal...
In this Thesis, the production and identification of food peptides by using enzymatic hydrolysis and several effects on the gastrointestinal health have been studied. Peptide identification and quantification was performed by reversed phase-high-performance liquid chromatography coupled to tandem mass spectrometry (RP-HPLC-MS/MS). Different hydrolysates and simulated gastrointestinal digests from casein, whey proteins and lunasin were analyzed. Initially, it was proposed the production of caseinphosphopeptides (CPPs) by tryptic hydrolysis of a casein-derived by-product generated during the manufacture of a functional ingredient with antihypertensive activity. Identification and semi-quantification of peptides revealed some qualitative and quantitative changes in the CPPs generated under different hydrolysis conditions and selective precipitation. The by-product was also subjected to gastrointestinal digestion simulating physiological conditions. Comparison of the resulting peptides obtained by these two hydrolysis processes showed an important sequence homology in the fraction of CPPs. Some regions, specifically αS1-casein (43-59), (60-74), β-casein (1-25) and (30-50), were able to resist both tryptic hydrolysis and simulated digestion. Therefore, it is proved that the casein-derived by-product can be used as a source of CPPs to enhance the absorption of minerals at intestinal level...
In this Thesis, the production and identification of food peptides by using enzymatic hydrolysis and several effects on the gastrointestinal health have been studied. Peptide identification and quantification was performed by reversed phase-high-performance liquid chromatography coupled to tandem mass spectrometry (RP-HPLC-MS/MS). Different hydrolysates and simulated gastrointestinal digests from casein, whey proteins and lunasin were analyzed. Initially, it was proposed the production of caseinphosphopeptides (CPPs) by tryptic hydrolysis of a casein-derived by-product generated during the manufacture of a functional ingredient with antihypertensive activity. Identification and semi-quantification of peptides revealed some qualitative and quantitative changes in the CPPs generated under different hydrolysis conditions and selective precipitation. The by-product was also subjected to gastrointestinal digestion simulating physiological conditions. Comparison of the resulting peptides obtained by these two hydrolysis processes showed an important sequence homology in the fraction of CPPs. Some regions, specifically αS1-casein (43-59), (60-74), β-casein (1-25) and (30-50), were able to resist both tryptic hydrolysis and simulated digestion. Therefore, it is proved that the casein-derived by-product can be used as a source of CPPs to enhance the absorption of minerals at intestinal level...
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Tesis inédita de la Universidad Complutense de Madrid, Facultad de Farmacia, Departamento de Bioquímica y Biología Molecular II, leída el 18/01/2016