Journal article Open Access

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


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    <subfield code="a">Antimicrobial peptides Antifungal activity Lactobacillus plantarum Spoilage fungi</subfield>
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    <subfield code="c">2017-03-31</subfield>
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    <subfield code="p">LWT - Food Science and Technology</subfield>
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    <subfield code="u">a     Laboratory of Food Chemistry and Toxicology, Faculty of Pharmacy, University of Valencia, Av. Vicent Andrés Estellés s/n, 46100 Burjassot, Spain  b     School of Life Sciences, Pontifícia Universidade Católica do Paraná, Curitiba, Paraná, Brazil</subfield>
    <subfield code="a">C.LuzaF.SaladinoaF.B.LucianobJ.MañesaG.Mecaa</subfield>
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    <subfield code="a">In vitro antifungal activity of bioactive peptides produced by Lactobacillus plantarum against Aspergillus parasiticus and Penicillium expansum</subfield>
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    <subfield code="c">678781</subfield>
    <subfield code="a">Integrated and innovative key actions for mycotoxin management in the food and feed chain</subfield>
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    <subfield code="a">Creative Commons Attribution 4.0 International</subfield>
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    <subfield code="a">&lt;p&gt;&lt;a href=""&gt;Food spoilage&lt;/a&gt; caused by mycotoxigenic moulds represents an important problem in food security. The &lt;a href=""&gt;antimicrobial peptides&lt;/a&gt; are compounds of natural origin constituted by a variable number (5&amp;ndash;100) of amino acids held together through &lt;a href=""&gt;peptide&lt;/a&gt; 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 &lt;a href=""&gt;antifungal&lt;/a&gt; activity against &lt;em&gt;&lt;a href=""&gt;Aspergillus Parasiticus&lt;/a&gt;&lt;/em&gt; and &lt;em&gt;&lt;a href=""&gt;Penicillium&lt;/a&gt;&lt;/em&gt; expansum. CFS obtained by &lt;em&gt;Lactobacillus plantarum&lt;/em&gt; showed the highest inhibition activity. CFS was fractionated by &lt;a href=""&gt;size exclusion chromatography&lt;/a&gt; and injected into the &lt;a href=""&gt;liquid chromatography&lt;/a&gt; coupled to &lt;a href=""&gt;diode array detector&lt;/a&gt;. 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 &lt;em&gt;&lt;a href=""&gt;A.&amp;nbsp;Parasiticus&lt;/a&gt;&lt;/em&gt; and &lt;em&gt;P.&amp;nbsp;expansum&lt;/em&gt; in liquid medium. The MALDI-TOF/TOF &lt;a href=""&gt;mass spectrometry&lt;/a&gt; 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 &lt;em&gt;P.&amp;nbsp;expansum&lt;/em&gt; and &lt;em&gt;A.&amp;nbsp;parasiticus&lt;/em&gt;, respectively, in liquid medium after 48&amp;nbsp;h incubation.&lt;/p&gt;</subfield>
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    <subfield code="a">10.1016/j.lwt.2017.03.053</subfield>
    <subfield code="2">doi</subfield>
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    <subfield code="a">publication</subfield>
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