In vitro gastrointestinal digestion and transepithelial transport of bioactive peptide lunasin: study of released and bioavailable peptides
| Autor: | Fernández-Tomé, Samuel, Cruz-Huerta, Elvia, Amigo, Lourdes, Recio, Isidra, Hernández-Ledesma, Blanca |
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| Přispěvatelé: | Ministerio de Economía y Competitividad (España) |
| Rok vydání: | 2016 |
| Předmět: | |
| Zdroj: | Digital.CSIC. Repositorio Institucional del CSIC instname |
| Popis: | Póster presentado al VI Congreso Internacional de Ciencia y Tecnología de los Alimentos, celebrado en Córdoba (Argentina) del 2 al 5 de noviembre de 2016. Gastrointestinal digestion of dietary functional compounds is one of the primary aspects to be evaluated before their potential application into nutraceuticals or functional foods. Bioactive foodderived peptides might be highly modified during its transit through the gastrointestinal tract giving rise to the release of new active fragments or, on the contrary, to fragments with less or null activity compared with their precursors. Therefore, the proteolytic attack of pepsin, pancreatic and epithelial brush-border enzymes is known to play a key role on their physiological relevance. Moreover, these peptides can be absorbed and reach the target tissues acting at systemic level or exert effects locally in contact with the broad panel of digestive cells and receptors. Lunasin is a 43-amino acid peptide present in soybean with a variety of proven chemopreventive properties. Preliminary studies had suggested that protease inhibitors such as Bowman-Birk inhibitor and Kunitz-trypsin inhibitor were responsible for the partial resistance of lunasin, when present in soybean protein or food, to the digestive process. The aim of this study was to evaluate the in vitro behavior of synthetic lunasin under conditions simulating gastrointestinal digestion in the absence or presence of the major Bowman-Birk family isoinhibitor (IBB1), and to assess the bioavailability of peptide lunasin and selected lunasin-derived fragment arising from its digestion in Caco-2 cell monolayers. By liquid chromatography coupled with tandem mass spectrometry, it was confirmed the protective role of IBB1 on lunasin digestion, being this effect dependent of the amount of IBB1 present at the intestinal phase. Peptide profiles of gastric and gastrointestinal digests were characterized and it was shown that the regions 1SKWQHQQDSC10, 11RKQLQGVN18, 19LTPCEKHIME28 and 29KIQGRGDDDDDDDDD43 from lunasin were particularly resistant to the action of pepsin, trypsin and chymotrypsin enzymes. Among these lunasin-derived fragments, peptides 1SKWQHQQDSC10 and 29KIQGRGDDDDDDDDD43 demonstrated a notable resistance against the epithelial brushborder peptidases. In addition, lunasin peptide and fragment 11RKQLQGVN18 were found to cross intact through Caco-2 monolayer with apparent permeability values (apical-to-basolateral) of 3.32 × 10-7 and 2.50 × 10-7 cm/s, respectively. The transepithelial absorption of these peptides was not modified by the transcytosis inhibitor wortmannin, but it was enhanced by the tight junction disruptor cytochalasin D, suggesting that the paracellular pathway was the main mechanism involved in their transport. This work has received financial support from projects AGL2011-24643 and AGL2015-66886-R from Spanish Ministry of Economy and Competitiveness (MINECO). S. F. –T. and B. H. –L. acknowledge MINECO for their FPI and “Ramón y Cajal” post-doctoral contract, respectively. |
| Databáze: | OpenAIRE |
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