Journal article Open Access

In vitro antifungal activity of bioactive peptides produced by Lactobacillus plantarum against Aspergillus parasiticus and Penicillium expansum

C.LuzaF.SaladinoaF.B.LucianobJ.MañesaG.Mecaa


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{
  "DOI": "10.1016/j.lwt.2017.03.053", 
  "container_title": "LWT - Food Science and Technology", 
  "title": "In vitro antifungal activity of bioactive peptides produced by Lactobacillus plantarum against Aspergillus parasiticus and Penicillium expansum", 
  "issued": {
    "date-parts": [
      [
        2017, 
        3, 
        31
      ]
    ]
  }, 
  "abstract": "<p><a href=\"https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/food-spoilage\">Food spoilage</a> caused by mycotoxigenic moulds represents an important problem in food security. The <a href=\"https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/antimicrobial-peptides\">antimicrobial peptides</a> are compounds of natural origin constituted by a variable number (5&ndash;100) of amino acids held together through <a href=\"https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/peptide\">peptide</a> bonds. In this work, the cell free supernatants (CFSs) containing peptides obtained from four strains of LAB were lyophilized, filtered and tested to determine the <a href=\"https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/antifungal-medication\">antifungal</a> activity against <em><a href=\"https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/aspergillus-parasiticus\">Aspergillus Parasiticus</a></em> and <em><a href=\"https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/penicillium\">Penicillium</a></em> expansum. CFS obtained by <em>Lactobacillus plantarum</em> showed the highest inhibition activity. CFS was fractionated by <a href=\"https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/size-exclusion-chromatography\">size exclusion chromatography</a> and injected into the <a href=\"https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/chromatography\">liquid chromatography</a> coupled to <a href=\"https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/chromatography-detector\">diode array detector</a>. One of the recollected fractions resulted interesting for the presence of three peaks that were purified by the technique of the LC-DAD using a semi preparative C18 column. Finally, the antifungal activity of the purified peptides was studied against <em><a href=\"https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/aspergillus-parasiticus\">A.&nbsp;Parasiticus</a></em> and <em>P.&nbsp;expansum</em> in liquid medium. The MALDI-TOF/TOF <a href=\"https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/mass-spectrometry\">mass spectrometry</a> was used for the peptides identification. The three purified peptides presented an amino acidic sequence identified by a bioinformatics program of SGADTTFLTK, LVGKKVQTF, and GTLIGQDYK. The first peptide purified reduced 58% and 73% the growth of <em>P.&nbsp;expansum</em> and <em>A.&nbsp;parasiticus</em>, respectively, in liquid medium after 48&nbsp;h incubation.</p>", 
  "author": [
    {
      "family": "C.LuzaF.SaladinoaF.B.LucianobJ.Ma\u00f1esaG.Mecaa"
    }
  ], 
  "type": "article-journal", 
  "id": "1167602"
}
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