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


MARC21 XML Export

<?xml version='1.0' encoding='UTF-8'?>
<record xmlns="http://www.loc.gov/MARC21/slim">
  <leader>00000nam##2200000uu#4500</leader>
  <datafield tag="653" ind1=" " ind2=" ">
    <subfield code="a">Antimicrobial peptides Antifungal activity Lactobacillus plantarum Spoilage fungi</subfield>
  </datafield>
  <controlfield tag="005">20191101191415.0</controlfield>
  <controlfield tag="001">1167602</controlfield>
  <datafield tag="856" ind1="4" ind2=" ">
    <subfield code="s">1229432</subfield>
    <subfield code="z">md5:b3c60d94e35c2e2ea69dc9ea43c9e16a</subfield>
    <subfield code="u">https://zenodo.org/record/1167602/files/s12864-017-4116-5.pdf</subfield>
  </datafield>
  <datafield tag="542" ind1=" " ind2=" ">
    <subfield code="l">open</subfield>
  </datafield>
  <datafield tag="260" ind1=" " ind2=" ">
    <subfield code="c">2017-03-31</subfield>
  </datafield>
  <datafield tag="909" ind1="C" ind2="O">
    <subfield code="o">oai:zenodo.org:1167602</subfield>
  </datafield>
  <datafield tag="909" ind1="C" ind2="4">
    <subfield code="p">LWT - Food Science and Technology</subfield>
  </datafield>
  <datafield tag="100" ind1=" " ind2=" ">
    <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>
  </datafield>
  <datafield tag="245" ind1=" " ind2=" ">
    <subfield code="a">In vitro antifungal activity of bioactive peptides produced by Lactobacillus plantarum against Aspergillus parasiticus and Penicillium expansum</subfield>
  </datafield>
  <datafield tag="536" ind1=" " ind2=" ">
    <subfield code="c">678781</subfield>
    <subfield code="a">Integrated and innovative key actions for mycotoxin management in the food and feed chain</subfield>
  </datafield>
  <datafield tag="540" ind1=" " ind2=" ">
    <subfield code="u">http://creativecommons.org/licenses/by/4.0/legalcode</subfield>
    <subfield code="a">Creative Commons Attribution 4.0 International</subfield>
  </datafield>
  <datafield tag="650" ind1="1" ind2="7">
    <subfield code="a">cc-by</subfield>
    <subfield code="2">opendefinition.org</subfield>
  </datafield>
  <datafield tag="520" ind1=" " ind2=" ">
    <subfield code="a">&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;</subfield>
  </datafield>
  <datafield tag="024" ind1=" " ind2=" ">
    <subfield code="a">10.1016/j.lwt.2017.03.053</subfield>
    <subfield code="2">doi</subfield>
  </datafield>
  <datafield tag="980" ind1=" " ind2=" ">
    <subfield code="a">publication</subfield>
    <subfield code="b">article</subfield>
  </datafield>
</record>
21
104
views
downloads
Views 21
Downloads 104
Data volume 127.9 MB
Unique views 21
Unique downloads 96

Share

Cite as