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Bovine hemoglobin: an attractive source of antibacterial peptides
Authors:Nedjar-Arroume Naïma  Dubois-Delval Véronique  Adje Estelle Yaba  Traisnel Jonathan  Krier François  Mary Patrice  Kouach Mostafa  Briand Gilbert  Guillochon Didier
Affiliation:

aLaboratoire de Procédés Biologiques Génie Enzymatique et Microbien, IUT“A”, Polytech’Lille, Lille I, BP 179, 59653 Villeneuve d’Ascq Cedex, France

bLaboratoire d’Application de Spectrométrie de Masse, Service Commun de Physicochimie, Faculté de Médecine H. Warembourg, Pôle Recherche, Place de Verdun, Lille II, France

Abstract:A peptic hemoglobin hydrolysate was fractioned by a semi-preparative reversed-phase HPLC and some fractions have an antibacterial activity against four bacteria strains: Micrococcus luteus A270, Listeria innocua, Escherichia coli and Salmonella enteritidis. These fractions were analyzed by ESI/MS and ESI/MS/MS, in order to characterize the peptides in these fractions. Each fraction contains at least three peptides and some fractions contain five peptides. All these fractions were purified several times by HPLC to obtain pure peptides. Thirty antibacterial peptides were identified. From the isolated antibacterial peptides, 24 peptides were derived from the chains of hemoglobin and 6 peptides were derived from the β chains of hemoglobin. The lowest concentration of these peptides (minimum inhibitory concentration (MIC)) necessary to completely inhibit the growth of four bacteria strain was determined. The cell population of all of the tested bacteria species decreased by at least 97% after a 24-h incubation with any of the peptides at the minimum inhibitory concentration.
Keywords:Bovine hemoglobin   Antibacterial peptides   Pepsin   Hydrolysate   Active peptides
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