38 research outputs found

    Impact of tannin supplementation on proteolysis during post-ruminal digestion in wethers using a dynamic in vitro system: a plant (Medicago sativa) digestomic approach

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    The aim of this study was to characterize the effects of tannins on plant protein during sheep digestion, using a digestomic approach combining in vivo (rumen) conditions and an in vitro digestive system (abomasum and small intestine). Ruminal fluid from wethers infused with a tannin solution or water (control) was introduced into the digester, and protein degradation was followed by LC-MS/MS. Tannin infusion in the rumen led to a clear decrease in protein degradation-related fermentation end-products, whereas RuBisCo protein was more abundant than in control wethers. In the simulated abomasum, peptidomic analysis showed more degradation products of RuBisCo in the presence of tannins. The effect of RuBisCo protection by tannins continued to impact Rubisco digestion into early-stage intestinal digestion, but was no longer detectable in late-stage intestinal digestion. The peptidomics approach proved a potent tool for identifying and quantifying the type of protein hydrolyzed throughout the gastrointestinal tract

    Empreinte peptidique de la fraction prot Ă©ique soluble du jambon de Bayonne

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    Development of a MALDI imaging mass spectrometry (IMS) approach to bacterial proteomics: first application to Listeria monocytogenes biofilms exposed to a desiccation

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    Development of a MALDI imaging mass spectrometry (IMS) approach to bacterial proteomics: first application to Listeria monocytogenes biofilms exposed to a desiccation. 7. Congress of European Microbiologists FEMS 201

    The chemical reactivity of proteins during in vitro dynamic meat digestion

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    International audienceMeat processing can affect the chemical reactivity of proteins; for instance, it is well known that meat cooking leads to protein oxidation. The proteins modifications can also develop during digestion because of the physicochemical conditions of the stomach, i.e. oxygen pressure, low pH, and reducing conditions. This issue is of great importance to better assess the nutritional quality of meat, assessed by its amino acids composition and their digestibility properties. These qualities, as well as the organoleptic aspect, make meat an indispensable food, especially for specific population such as elderly. In this context, this study aimed at characterizing the chemical reactivity during meat during digestion, and its modulation by aging digestive physiology. For this, a dynamic in vitro artificial digestive computer-controlled system (DIDGI®) was used to reflect human gastro-intestinal conditions for adult and elderly physiologies. Peptides and proteins from stomach, duodenum and ileum were analysed by high-resolution LC-MS/MS mass spectrometry to identify protein digestion targets and their susceptibility to chemical conditions. The label-free protein quantification was performed using peptide relative intensity summation. The chemical reactivity was assessed by protein oxidation, evaluated by measuring carbonyls formation, and by antioxidant activity, measured using ORAC test. Kinetics of protein hydrolysis and protein oxidation during gastro-intestinal digestion were analyzed using ANOVA (Statistica software). The first results showed an increase in protein oxidation, all along the in vitro meat digestion. Moreover, the chemical reactivity of meat digestion was not modified by the aging, despite the difference in pH decrease between both digestive physiologies. This preliminary results will be completed in regard with the proteins hydrolysis kinetics, studied using the workflow presented in a poster by Sayd et al

    MALDI imaging and profiling mass spectrometry approach for the analysis of Listeria monocytogenes biofilms exposed to a desiccation

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    MALDI imaging and profiling mass spectrometry approach for the analysis of Listeria monocytogenes biofilms exposed to a desiccation. SMMAP 2017, Spectrométrie de Masse, Métabolomique et Analyse Protéomiqu
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