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Novel bioactive peptides from enzymatic hydrolysate of Sardinelle (Sardinella aurita) muscle proteins hydrolysed by Bacillus subtilis A26 proteases

AuthorsJemil, Ines; Abdelhedi, Ola; Nasri, Rim; Mora, Leticia CSIC ORCID; Jridi, Mourad; Aristoy, María Concepción CSIC ORCID; Toldrá Vilardell, Fidel CSIC ORCID; Nasri, Moncef
KeywordsSardinella aurita
Protein hydrolysate
Issue Date7-Jun-2017
CitationFood Research International 100 (1): 121-133 (2017)
AbstractSardinelle protein hydrolysate (SPH), prepared by treatment with Bacillus subtilis A26 proteases, was found to exhibit antibacterial, antioxidant and ACE-inhibitory activities. SPH, with a degree of hydrolysis of 4%, was fractionated by size exclusion chromatography on a Sephadex G-25 into five major fractions (F1–F5). F2, which exhibited the highest antibacterial and ACE-inhibitory activities, and F4, which exhibited the highest antibacterial and antioxidant activities, were further fractionated by reverse phase-high performance liquid chromatography (RP-HPLC) and then analysed using nano-ESI-LC-MS/MS to identify the sequences of peptides. Eight peptides were identified in the sub-fraction F2-A, nine peptides in the sub-fraction F4-B, and 45 peptides in F4-C. Identified peptides were found to share sequences with previously described bioactive peptides based on Biopep database. The results of this study suggest that SPH is a good source of natural bioactive peptides. Hence, it can be used as a potential ingredient in nutraceutical field.
Publisher version (URL)https://doi.org/10.1016/j.foodres.2017.06.018
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