Journal article Open Access

Aflatoxin B1 andM1 Degradation by Lac2 from Pleurotus pulmonarius and Redox Mediators

Martina Loi, Francesca Fanelli, Paolo Zucca, Vania Liuzzi, Laura Quintieri, Maria Cimmarusti, Linda Monaci, Miriam Haidukowski, Antonio Logrieco, Enrico Sanjust, Giuseppina Mulè


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    <subfield code="a">laccase; Pleurotus; mycotoxins; aflatoxin B1; aflatoxin M1; biodegradation; redox mediators</subfield>
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    <subfield code="c">2016-08-23</subfield>
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    <subfield code="a">Martina Loi, Francesca Fanelli, Paolo Zucca, Vania Liuzzi, Laura Quintieri, Maria Cimmarusti, Linda Monaci, Miriam Haidukowski, Antonio Logrieco, Enrico Sanjust, Giuseppina Mulè</subfield>
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    <subfield code="a">Aflatoxin B1 andM1 Degradation by Lac2 from Pleurotus pulmonarius and Redox Mediators</subfield>
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    <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">&lt;p&gt;Laccases (LCs) are multicopper oxidases that find application as versatile biocatalysts&lt;br&gt;
for the green bioremediation of environmental pollutants and xenobiotics. In this study we&lt;br&gt;
elucidate the degrading activity of Lac2 pure enzyme form Pleurotus pulmonarius towards aflatoxin&lt;br&gt;
B1 (AFB1) and M1 (AFM1). LC enzyme was purified using three chromatographic steps and&lt;br&gt;
identified as Lac2 through zymogram and LC-MS/MS. The degradation assays were performed&lt;br&gt;
in vitro at 25 C for 72 h in buffer solution. AFB1 degradation by Lac2 direct oxidation&lt;br&gt;
was 23%. Toxin degradation was also investigated in the presence of three redox mediators,&lt;br&gt;
(2,20-azino-bis-[3-ethylbenzothiazoline-6-sulfonic acid]) (ABTS) and two naturally-occurring phenols,&lt;br&gt;
acetosyringone (AS) and syringaldehyde (SA). The direct effect of the enzyme and the mediated&lt;br&gt;
action of Lac2 with redox mediators univocally proved the correlation between Lac2 activity and&lt;br&gt;
aflatoxins degradation. The degradation of AFB1 was enhanced by the addition of all mediators at&lt;br&gt;
10 mM, with AS being the most effective (90% of degradation). AFM1 was completely degraded by&lt;br&gt;
Lac2 with all mediators at 10 mM. The novelty of this study relies on the identification of a pure&lt;br&gt;
enzyme as capable of degrading AFB1 and, for the first time, AFM1, and on the evidence that the&lt;br&gt;
mechanism of an effective degradation occurs via the mediation of natural phenolic compounds.&lt;br&gt;
These results opened new perspective for Lac2 application in the food and feed supply chains as a&lt;br&gt;
biotransforming agent of AFB1 and AFM1.&lt;/p&gt;</subfield>
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    <subfield code="a">10.3390/toxins8090245</subfield>
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