0000000000526107

AUTHOR

Jean-francois Ritt

showing 4 related works from this author

Oligopeptide assimilation and transport by Oenococcus oeni

2008

International audience; Aims: Oenococcus oeni is a slow-growing wine bacterium with a low growth yield. It thrives better on complex nitrogen sources than on free amino-acid medium. We aimed to characterize the oligopeptide use of this micro-organism. Methods and Results: Several peptides of two to eight amino-acid residues were able to provide essential amino acids. The disappearance of various peptides from extracellular medium was assessed with whole cells. Initial rates of utilization varied with the peptide, and free amino acids were released into the medium. Conclusions: Oenococcus oeni was able to transport the oligopeptides with two to five amino-acid residues tested and to hydrolys…

NitrogenWinePeptideApplied Microbiology and Biotechnology[ CHIM ] Chemical SciencesIndustrial Microbiology03 medical and health sciencesHydrolysis[CHIM]Chemical Sciences030304 developmental biologyOenococcus oeniWinechemistry.chemical_classificationBacteriological Techniques0303 health sciencesOligopeptidebiology030306 microbiologyBiological TransportGeneral MedicineMetabolismbiology.organism_classificationCulture MediaAmino acidBiochemistrychemistryAmino Acids EssentialOligopeptidesLeuconostocBacteriaBiotechnology
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Characterization of EprA, a major extracellular protein of Oenococcus oeni with protease activity

2008

International audience; Extracellular proteins from Oenococcus oeni. a wine-making bacterium, were isolated during growth on media differing by their nitrogen content. Analysis by two-dimensional electrophoresis revealed a low number of protein signals. Among the main spots, one signal corresponded to a single protein, which contained a lysine repeat domain characteristic of cell-wall hydrolases. We demonstrated that this major protein, named EprA, was able to hydrolyse several proteins. The heterologous production of this protein in Escherichia coli confirmed the protease activity of EprA. With a MW of 21.3 kDa and a pl of 5.3, EprA presents optimal activity at pH 7.0 and 45 degrees C. Thi…

ProteasesHydrolyzed proteinNitrogenmedicine.medical_treatmentWinemedicine.disease_causeMicrobiology[ CHIM ] Chemical SciencesMicrobiology03 medical and health sciencesBacterial Proteinsmedicine[CHIM]Chemical SciencesElectrophoresis Gel Two-DimensionalPolyacrylamide gel electrophoresisEscherichia coli030304 developmental biologyOenococcus oenichemistry.chemical_classification0303 health sciencesProteasebiology030306 microbiologyTemperatureGeneral MedicineHydrogen-Ion Concentrationbiology.organism_classificationCulture MediaMolecular WeightEnzymeBiochemistrychemistryFermentationFood MicrobiologyElectrophoresis Polyacrylamide GelOenococcusLeuconostocFood SciencePeptide Hydrolases
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Lateral reorganization of plasma membrane is involved in the yeast resistance to severe dehydration

2010

International audience; In this study, we investigated the kinetic and the magnitude of dehydrations on yeast plasma membrane (PM) modifications because this parameter is crucial to cell survival. Functional (permeability) and structural (morphology, ultrastructure, and distribution of the protein Sur7-GFP contained in sterol-rich membrane microdomains) PM modifications were investigated by confocal and electron microscopy after progressive (non-lethal) and rapid (lethal) hyperosmotic perturbations. Rapid cell dehydration induced the formation of many PM invaginations followed by membrane internalization of low sterol content PM regions with time. Permeabilization of the plasma membrane occ…

Saccharomyces cerevisiae Proteins[SDV.BIO]Life Sciences [q-bio]/BiotechnologyRecombinant Fusion Proteinsmedia_common.quotation_subjectCellBiophysicsSaccharomyces cerevisiaeBiologyBiochemistryCell survivallaw.invention[SPI]Engineering Sciences [physics][ SDV.MP ] Life Sciences [q-bio]/Microbiology and ParasitologylawElectron microscopymedicine[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringMicrodomainDehydration kineticInternalizationEisosomemedia_commonDehydrationOsmotic concentrationCell MembraneOsmolar ConcentrationLipid microdomainMembrane ProteinsWaterCell BiologyEndocytosisCell biologyConfocal microscopy[SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitologymedicine.anatomical_structureMembraneUltrastructureElectron microscopeBiochimica et Biophysica Acta (BBA) - Biomembranes
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Peptidases specific for proline-containing peptides and their unusual peptide-dependent regulation in Oenococcus oeni

2009

International audience; Growth of the lactic acid bacterium (LAB) Oenococcus oeni, which is involved in malolactic fermentation during the winemaking process, is stimulated by peptides originating from yeast. In this study, we investigated the impact of peptides on O. oeni growth, peptidase activity and the expression of genes encoding the studied peptidases. Low levels of PepN activity and very high levels of PepI activity were observed in O. oeni, whereas levels of PepX activity were intermediate. The level of biosynthesis of these O. oeni peptidases was shown to depend on peptides present in the culture medium. These results were confirmed by transcriptional analyses of putative pep gene…

NitrogenPeptideElectrophoretic Mobility Shift AssayBiologyApplied Microbiology and Biotechnology[ CHIM ] Chemical Sciences03 medical and health scienceschemistry.chemical_compoundBiosynthesisGene expressionMalolactic fermentation[CHIM]Chemical SciencesPromoter Regions GeneticChromatography High Pressure LiquidOenococcus030304 developmental biologyOenococcus oeniDNA Primerschemistry.chemical_classification0303 health sciences030306 microbiologyReverse Transcriptase Polymerase Chain ReactionGeneral MedicineSequence Analysis DNAbiology.organism_classificationYeastEnzymechemistryBiochemistryGene Expression RegulationFermentationBiotechnologyPeptide Hydrolases
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