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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  <identifier identifierType="URL">https://zenodo.org/record/1167602</identifier>
  <creators>
    <creator>
      <creatorName>C.LuzaF.SaladinoaF.B.LucianobJ.MañesaG.Mecaa</creatorName>
      <affiliation>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</affiliation>
    </creator>
  </creators>
  <titles>
    <title>In vitro antifungal activity of bioactive peptides produced by Lactobacillus plantarum against Aspergillus parasiticus and Penicillium expansum</title>
  </titles>
  <publisher>Zenodo</publisher>
  <publicationYear>2017</publicationYear>
  <subjects>
    <subject>Antimicrobial peptides Antifungal activity Lactobacillus plantarum Spoilage fungi</subject>
  </subjects>
  <dates>
    <date dateType="Issued">2017-03-31</date>
  </dates>
  <resourceType resourceTypeGeneral="Text">Journal article</resourceType>
  <alternateIdentifiers>
    <alternateIdentifier alternateIdentifierType="url">https://zenodo.org/record/1167602</alternateIdentifier>
  </alternateIdentifiers>
  <relatedIdentifiers>
    <relatedIdentifier relatedIdentifierType="DOI" relationType="IsIdenticalTo">10.1016/j.lwt.2017.03.053</relatedIdentifier>
  </relatedIdentifiers>
  <rightsList>
    <rights rightsURI="http://creativecommons.org/licenses/by/4.0/legalcode">Creative Commons Attribution 4.0 International</rights>
    <rights rightsURI="info:eu-repo/semantics/openAccess">Open Access</rights>
  </rightsList>
  <descriptions>
    <description descriptionType="Abstract">&lt;p&gt;&lt;a href="https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/food-spoilage"&gt;Food spoilage&lt;/a&gt; caused by mycotoxigenic moulds represents an important problem in food security. The &lt;a href="https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/antimicrobial-peptides"&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="https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/peptide"&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="https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/antifungal-medication"&gt;antifungal&lt;/a&gt; activity against &lt;em&gt;&lt;a href="https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/aspergillus-parasiticus"&gt;Aspergillus Parasiticus&lt;/a&gt;&lt;/em&gt; and &lt;em&gt;&lt;a href="https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/penicillium"&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="https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/size-exclusion-chromatography"&gt;size exclusion chromatography&lt;/a&gt; and injected into the &lt;a href="https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/chromatography"&gt;liquid chromatography&lt;/a&gt; coupled to &lt;a href="https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/chromatography-detector"&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="https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/aspergillus-parasiticus"&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="https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/mass-spectrometry"&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;</description>
  </descriptions>
  <fundingReferences>
    <fundingReference>
      <funderName>European Commission</funderName>
      <funderIdentifier funderIdentifierType="Crossref Funder ID">10.13039/501100000780</funderIdentifier>
      <awardNumber awardURI="info:eu-repo/grantAgreement/EC/H2020/678781/">678781</awardNumber>
      <awardTitle>Integrated and innovative key actions for mycotoxin management in the food and feed chain</awardTitle>
    </fundingReference>
  </fundingReferences>
</resource>
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