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Título: | Peptidomic analysis of bioactive peptides in zebra blenny (Salaria basilisca) muscle protein hydrolysate exhibiting antimicrobial activity obtained by fermentation with Bacillus mojavensis A21 |
Autor: | Jemil, Ines; Abdelhedi, Ola; Mora, Leticia CSIC ORCID; Nasri, Rim; Aristoy, María Concepción CSIC ORCID; Jridi, Mourad; Hajji, Mohamed; Toldrá Vilardell, Fidel CSIC ORCID; Nasri, Moncef | Palabras clave: | Salaria basilisca Fermentation Bacillus mojavensis A21 Protein hydrolysates Antibacterial peptides |
Fecha de publicación: | 17-ago-2016 | Editor: | Elsevier | Citación: | Process Biochemistry 51 (12): 2186-2197 (2016) | Resumen: | The present study investigates the antibacterial activity of zebra blenny (Salaria basilisca) protein hydrolysates obtained by fermentation with a proteolytic bacterium, Bacillus mojavensis A21. The fermentative zebra blenny protein hydrolysate (FZPH), with a degree of hydrolysis (DH) of 17.35%, was fractionated by size exclusion chromatography on a Sephadex G-25 into six major fractions (F1-F6). Fraction F2, which exhibited antibacterial activity against several Gram-positive and Gram-negative bacteria, was further fractionated by reversed-phase high performance liquid chromatography (RP-HPLC). Fractions A and B from RP-HPLC exhibiting the highest antibacterial activity, were analysed using nano ESI-LC–MS/MS to identify the sequences of the peptides. A total of 28 and 41 peptides, containing from 8 to 31 amino acid residues, were identified in sub-fractions A and B, respectively. Further, identified bioactive peptides sharing sequences with previously identified peptides were reported. The results of this study suggest that FZPH is a good source of natural antimicrobial peptides and therefore, they could serve as a beneficial ingredient for nutraceuticals. | Versión del editor: | https://doi.org/10.1016/j.procbio.2016.08.021 | URI: | http://hdl.handle.net/10261/149139 | DOI: | 10.1016/j.procbio.2016.08.021 | ISSN: | 1359-5113 |
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Process Biochem 2016 51-2186-2197.pdf | Artículo principal | 666,83 kB | Adobe PDF | Visualizar/Abrir |
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