Isolation and characterization of four antibacterial peptides from bovine hemoglobin |
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| Authors: | Nedjar-Arroume Naima Dubois-Delval Véronique Miloudi Khalil Daoud Rachid Krier François Kouach Mostafa Briand Gilbert Guillochon Didier |
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| Affiliation: | Laboratoire de Procédés Biologiques Génie Enzymatique et Microbien, IUT A, Polytech'Lille-Lille I, BP 179, 59653 Villeneuve d'Ascq Cedex, France. Naima.Arroume@univ-lille1.fr |
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| Abstract: | Peptic digestion of bovine hemoglobin at low degree of hydrolysis yields several intermediate peptide fractions after separation by reversed phase HPLC exhibiting antibacterial activity against Micrococcus luteus A270, Listeria innocua, Escherichia coli, and Salmonella enteritidis. From these fractions, four new antibacterial peptides were isolated and analyzed by ESI-MS/MS. Three of these peptides correspond to fragments of the alpha-chain of bovine hemoglobin: alpha107-141, alpha137-141, and alpha133-141, and one peptide to the beta-chain: beta126-145. The minimum inhibitory concentrations (MIC) of these peptides towards the four strains and their hemolytic activity towards bovine erythrocytes were determined. |
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