9 results on '"Flahaut, Christophe"'
Search Results
2. A multi-centre peptidomics investigation of food digesta: current state of the art in mass spectrometry analysis and data visualisation
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Portmann, Reto, Jiménez-Barrios , Pablo, Jardin, Julien, Abbühl, Lychou, Barile, Daniela, Danielsen, Marianne, Huang, Yu-Ping, Dalsgaard, Trine Kastrup, Miralles, Beatriz, Briard-Bion , Valérie, Cattaneo, Stefano, Chambon, Christophe, Cudennec, Benoit, De Noni, Ivano, Deracinois , Barbara, Dupont, Didier, Duval, Angéline, Flahaut, Christophe, López-Nicolás, Rubén, Nehir El, Sedef, Pica, Valentina, Santé-Lhoutellier, Véronique, Stuknytė, Milda, Laetitia , Laetitia, Sayd, Thierry, Recio, Isidra, Egger, Lotti, Agroscope, Schwarzenburgstr, 161, 3003 Bern, Switzerlan, Instituto de Investigaci ́on en Ciencias de la Alimentaci ́on (CIAL, CSIC-UAM), Madrid, Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut Agro Rennes Angers, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Department of Food Science and Technology, University of California, Davis, One Shields Avenue, Davis, CA 95616, Department of Food Science, Aarhus University, Centre for Innovative Food Research (CiFood), Agro Food Park 48, 8200 Aarhus, University of Milan, Department of Food, Environmental and Nutritional Sciences, via G. Celoria 2, 20133 Milan, Qualité des Produits Animaux (QuaPA), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Transfrontalière BioEcoAgro - UMR 1158 (BioEcoAgro), Université d'Artois (UA)-Université de Liège-Université de Picardie Jules Verne (UPJV)-Université du Littoral Côte d'Opale (ULCO)-Université de Lille-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-JUNIA (JUNIA), Université catholique de Lille (UCL)-Université catholique de Lille (UCL), Department of Food Science and Human Nutrition, Universidad de Murcia, Campus de Espinardo, 30100 Murcia, and Department of Food Engineering, Faculty of Engineering, Ege University, 35100 Izmir
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Visualisation ,Mass spectrometry ,Bioinformatics ,Protein digestion ,In vitro digestion ,Peptidomics ,[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition ,Food Science - Abstract
International audience; Mass spectrometry has become the technique of choice for the assessment of a high variety of molecules in complex food matrices. It is best suited for monitoring the evolution of digestive processes in vivo and in vitro. However, considering the variety of equipment available in different laboratories and the diversity of sample preparation methods, instrumental settings for data acquisition, statistical evaluations, and interpretations of results, it is difficult to predict a priori the ideal parameters for optimal results. The present work addressed this uncertainty by executing an inter-laboratory study with samples collected during in vitro digestion and presenting an overview of the state-of-the-art mass spectrometry applications and analytical capabilities available for studying food digestion. Three representative high-protein foodsskim milk powder (SMP), cooked chicken breast and tofuwere digested according to the static INFOGEST protocol with sample collection at five different time points during gastric and intestinal digestion. Ten laboratories analysed all digesta with their in-house equipment and applying theirconventional workflow. The compiled results demonstrate in general, that soy proteins had a slower gastric digestion and the presence of longer peptide sequences in the intestinal phase compared to SMP or chicken proteins, suggesting a higher resistance to the digestion of soy proteins. Differences in results among the various laboratories were attributed more to the peptide selection criteria than to the individual analytical platforms. Overall, the combination of mass spectrometry techniques with suitable methodological and statistical approaches is adequate for contributing to the characterisation of the recently defined digestome.
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- 2023
3. Impact of Bioinformatics Search Parameters for Peptides' Identification and Their Post-Translational Modifications: A Case Study of Proteolysed Gelatines from Beef, Pork, and Fish.
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Ambli, Mouna, Deracinois, Barbara, Jenequin, Anne-Sophie, Ravallec, Rozenn, Cudennec, Benoit, and Flahaut, Christophe
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POST-translational modification ,PEPTIDES ,BIOINFORMATICS software ,AMINO acid sequence ,PROTEOMICS ,FISH locomotion ,GELATIN - Abstract
Bioinformatics software, allowing the identification of peptides by the comparison of peptide fragmentation spectra obtained by mass spectrometry versus targeted databases or directly by de novo sequencing, is now mandatory in peptidomics/proteomics approaches. Programming the identification software requires specifying, among other things, the mass measurement accuracy of the instrument and the digestion enzyme used with the number of missed cleavages allowed. Moreover, these software algorithms are able to identify a large number of post-translational modifications (PTMs). However, peptide and PTM identifications are challenging in the agrofood field due to non-specific cleavage sites of physiological- or food-grade enzymes and the number and location of PTMs. In this study, we show the importance of customized software programming to obtain a better peptide and PTM identification rate in the agrofood field. A gelatine product and one industrial gelatine hydrolysate from three different sources (beef, pork, and fish), each digested by simulated gastrointestinal digestion, MS-grade trypsin, or both, were used to perform the comparisons. Two main points are illustrated: (i) the impact of the set-up of specific enzyme versus no specific enzyme use and (ii) the impact of a maximum of six PTMs allowed per peptide versus the standard of three. Prior knowledge of the composition of the raw proteins is an important asset for better identification of peptide sequences. [ABSTRACT FROM AUTHOR]
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- 2023
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4. New Bioactive Peptides Identified from a Tilapia Byproduct Hydrolysate Exerting Effects on DPP-IV Activity and Intestinal Hormones Regulation After Canine Gastrointestinal Simulated Digestion
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Theysgeur, Sandy, Cudennec, Benoit, Deracinois, Barbara, Perrin, Claire, Guiller, Isabelle, Lepoudère, Anne, Flahaut, Christophe, and Ravallec, Rozenn
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in vitro gastrointestinal digestion ,Protein Hydrolysates ,Swine ,Dipeptidyl Peptidase 4 ,In Vitro Techniques ,Cat Diseases ,Article ,Mass Spectrometry ,Gastrointestinal Hormones ,lcsh:QD241-441 ,Dogs ,lcsh:Organic chemistry ,Fish Products ,Animals ,Humans ,Dog Diseases ,Hydrolysis ,digestive, oral, and skin physiology ,DPP-IV inhibitory peptides ,Biological Transport ,Overweight ,Animal Feed ,glucagon-like peptide 1 ,cholecystokinin ,Gastrointestinal Tract ,Glucose ,Cats ,Caco-2 Cells ,Peptides ,bioactive peptides ,fish byproduct hydrolysate ,Tilapia - Abstract
Like their owners, dogs and cats are more and more affected by overweight and obesity-related problems and interest in functional pet foods is growing sharply. Through numerous studies, fish protein hydrolysates have proved their worth to prevent and manage obesity-related comorbidities like diabetes. In this work, a human in vitro static simulated gastrointestinal digestion model was adapted to the dog which allowed us to demonstrate the promising effects of a tilapia byproduct hydrolysate on the regulation of food intake and glucose metabolism. Promising effects on intestinal hormones secretion and dipeptidyl peptidase IV (DPP-IV) inhibitory activity were evidenced. We identify new bioactive peptides able to stimulate cholecystokinin (CCK) and glucagon-like peptide 1 (GLP-1) secretions, and to inhibit the DPP-IV activity after a transport study through a Caco-2 cell monolayer.
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- 2021
5. Partial-, Double-Enzymatic Dephosphorylation and EndoGluC Hydrolysis as an Original Approach to Enhancing Identification of Casein Phosphopeptides (CPPs) by Mass Spectrometry
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Deracinois, Barbara, Matéos, Aurélie, Romelard, Audrey, Boulier, Audrey, Auger, Julie, Baniel, Alain, Ravallec, Rozenn, Flahaut, Christophe, Transfrontalière BioEcoAgro - UMR 1158 (BioEcoAgro), Université d'Artois (UA)-Université de Liège-Université de Picardie Jules Verne (UPJV)-Université du Littoral Côte d'Opale (ULCO)-Université de Lille-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-JUNIA (JUNIA), and Université catholique de Lille (UCL)-Université catholique de Lille (UCL)
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endoGluC hydrolysis ,[SDV]Life Sciences [q-bio] ,casein phosphopeptides ,enzymatic dephosphorylation ,Chemical technology ,[SDE]Environmental Sciences ,TP1-1185 ,casein phosphopeptides, endoGluC hydrolysis, enzymatic dephosphorylation, mass spectrometry ,Article ,mass spectrometry - Abstract
International audience; The identification of phosphopeptides is currently a challenge when they are part of a complex matrix of peptides, such as a milk protein enzymatic hydrolysate. This challenge increases with both the number of phosphorylation sites on the phosphopeptides and their amino acid length. Here, this paper reports a four-phase strategy from an enzymatic casein hydrolysate before a mass spectrometry analysis in order to enhance the identification of phosphopeptides and phosphosites: (i) the control protein hydrolysate, (ii) a two-step enzymatic dephosphorylation of the latter, allowing for the almost total dephosphorylation of peptides, (iii) a one-step enzymatic dephosphorylation, allowing for the partial dephosphorylation of the peptides and (iv) an additional endoGluC enzymatic hydrolysis, allowing for the cleavage of long-size peptides into shorter ones. The reverse-phase high-pressure liquid chromatography–tandem mass spectrometry (RP-HPLC-MS/MS) analyses of hydrolysates that underwent this four-phase strategy allowed for the identification of 28 phosphorylation sites (90%) out of the 31 referenced in UniprotKB/Swiss-Prot (1 June 2021), compared to 17 sites (54%) without the latter. The alpha-S2 casein phosphosites, referenced by their similarity in the UniProt database, were experimentally identified, whereas pSer148, pThr166 and pSer187 from a multiphosphorylated long-size kappa-casein were not. Data are available via ProteomeXchange with identifier PXD027132.
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- 2021
6. Rapid Identification of Vibrio Species of the Harveyi Clade Using MALDI-TOF MS Profiling With Main Spectral Profile Database Implemented With an In-House Database: Luvibase.
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Mougin, Julia, Flahaut, Christophe, Roquigny, Roxane, Bonnin-Jusserand, Maryse, Grard, Thierry, and Le Bris, Cédric
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VIBRIO harveyi ,MASS spectrometry ,BACTERIAL diversity ,DATABASES ,VIBRIO ,MOLECULAR phylogeny ,GENE expression profiling - Abstract
Vibrio bacteria, and particularly members of the Harveyi clade, are the causative agents of vibriosis. This disease is responsible for mass mortality events and important economic losses on aquaculture farms. Improvements in surveillance and diagnosis are needed to successfully manage vibriosis outbreaks. 16S rRNA gene sequencing is generally considered to be the gold standard for bacterial identification but the cost and long processing time make it difficult to apply for routine identification. In contrast, MALDI-TOF MS offers rapid diagnosis and is commonly used in veterinary laboratories today. The major limiting factor for using this technique is the low environmental bacterial diversity in the commonly available databases. Here, we demonstrate that the sole use of the commercially available Bruker BioTyper database is not fully adequate for identifying Vibrio bacteria isolated from aquaculture farms. We therefore developed a new in-house database named Luvibase, composed of 23 reference MALDI-TOF mass spectra profiles obtained from Vibrio collection strains, mostly belonging to the Harveyi clade. The comparison of the accuracy of MALDI-TOF MS profiling and 16S rRNA gene sequencing revealed a lack of resolution for 16S rRNA gene sequencing. In contrast, MALDI-TOF MS profiling proved to be a more reliable tool for resolving species-level variations within the Harveyi clade. Finally, combining the Luvibase with the Bruker ver.9.0.0.0 database, led to successful identification of 47 Vibrio isolates obtained from moribund abalone, seabass and oysters. Thus, the use of Luvibase allow for increased confidence in identifying Vibrio species belonging to the Harveyi clade. [ABSTRACT FROM AUTHOR]
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- 2020
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7. Understanding the blood–brain barrier using gene and protein expression profiling technologies
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Pottiez, Gwënaël, Flahaut, Christophe, Cecchelli, Roméo, and Karamanos, Yannis
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BLOOD-brain barrier , *GENE expression , *PROTEINS , *HOMEOSTASIS , *GENOMICS , *LIQUID chromatography , *GEL electrophoresis , *MASS spectrometry - Abstract
Abstract: The blood–brain barrier (BBB) contributes to the brain homeostasis by regulating the passage of endogenous and exogenous compounds. This function is in part due to well-known proteins such as tight junction proteins, plasma membrane transporters and metabolic barrier proteins. Over the last decade, genomics and proteomics have emerged as supplementary tools for BBB research. The development of genomic and proteomic technologies has provided several means to extend the BBB knowledge and to investigate additional routes for the bypass of this barrier. These profiling technologies have been used on BBB models to decipher the physiological characteristics and, under stress conditions, to understand the molecular mechanisms of brain diseases. In this review, we will report and discuss the genomic and proteomic studies recently carried out to enhance the understanding of BBB features. [Copyright &y& Elsevier]
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- 2009
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8. Aqueous hydroformylation reaction mediated by randomly methylated β-cyclodextrin: How substitution degree influences catalytic activity and selectivity
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Legrand, François-Xavier, Sauthier, Mathieu, Flahaut, Christophe, Hachani, Johan, Elfakir, Claire, Fourmentin, Sophie, Tilloy, Sébastien, and Monflier, Eric
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HYDROFORMYLATION , *CHEMICAL reactions , *CYCLODEXTRINS , *TIME-of-flight mass spectrometry , *ELECTROSPRAY ionization mass spectrometry , *CATALYSIS , *CHROMATOGRAPHIC analysis - Abstract
Abstract: A crude mixture of randomly methylated β-cyclodextrin (RAME-β-CD) has been fractionated by chromatographic column to evaluate the influence of the methylation degree on activity and selectivity of a rhodium/tris(m-sulfonatophenyl)phosphane trisodium salt (TPPTS) catalytic system in hydroformylation of 1-decene. Each sample of methylated β-cyclodextrin (β-CD) was carefully analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) and electrospray ionization mass spectrometry (ESI-MS). The catalytic activity was found to gradually increase with the number of methyl groups on the methylated β-CD whereas the chemoselectivity and regioselectivity remained unchanged. [Copyright &y& Elsevier]
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- 2009
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9. MALDI-TOF mass spectrometry for the identification of lactic acid bacteria isolated from a French cheese: The Maroilles.
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Nacef, Menouar, Chevalier, Mickaël, Chollet, Sylvie, Drider, Djamel, and Flahaut, Christophe
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LACTIC acid bacteria , *MATRIX-assisted laser desorption-ionization , *TIME-of-flight mass spectrometry , *COMPOSITION of cheese , *PASTEURIZATION of milk , *APPROPRIATE technology for the food industry - Abstract
In this study we identified the culturable population of mesophilic lactic acid bacteria (LAB) from a French cheese Maroilles made either with raw or pasteurized milk using MALDI-TOF mass spectrometry (MS). Samples from rind and heart of Maroilles cheese were used, the LAB were selected on MRS agar at 30 °C and 197 Gram-positive and catalase-negative strains were subjected to identification by MALDI-TOF MS profiling. All strains were unambiguously identified: 105 strains from Maroilles made with raw milk (38 on the rind and 67 in the heart) and 92 strains from Maroilles made with pasteurized milk (39 on the rind and 53 in the heart). MALDI-TOF MS identification allowed identification of three genera belonging to LAB including Lactobacillus , Enterococcus and Leuconostoc . Lactobacillus was the most represented genus with seven species: Lactobacillus plantarum ( L. plantarum ), L. paracasei , L. curvatus , L. rhamnosus , L. fructivorans , L. parabuchneri , L. brevis found in Maroilles made with both kind of milk. The correlation between the 16S rDNA-based identification performed on selected strains and those obtained by MALDI-TOF-MS demonstrates that this fast, economically affordable, robust and reliable method for bacteria characterisation stands as an attractive alternative to the commonly-used methods and its application in food industry is discussed. [ABSTRACT FROM AUTHOR]
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- 2017
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