Peptidomic analysis of bioactive peptides in zebra blenny (Salaria basilisca) muscle protein hydrolysate exhibiting antimicrobial activity obtained by fermentation with Bacillus mojavensis A21

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...

Descripción completa

Detalles Bibliográficos
Autores: Jemil, Ines, Abdelhedi, Ola, Mora, Leticia, Nasri, Rim, Aristoy, María Concepción, Jridi, Mourad, Hajji, Mohamed, Toldrá Vilardell, Fidel, Nasri, Moncef
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2016
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/149139
Acceso en línea:http://hdl.handle.net/10261/149139
Access Level:acceso abierto
Palabra clave:Salaria basilisca
Fermentation
Bacillus mojavensis A21
Protein hydrolysates
Antibacterial peptides
Descripción
Sumario: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.