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RESEARCH PRODUCT
Characterization of EprA, a major extracellular protein of Oenococcus oeni with protease activity
Hervé AlexandrePatrice FolioFabienne RemizeJean-francois Rittsubject
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 Hydrolasesdescription
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. This O. oeni protease differs from all lactic acid bacteria proteases so far identified, and thus this bacterium possesses at least three proteases for wine protein hydrolysis. (C) 2008 Elsevier B.V. All rights reserved.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2008-01-01 |