Next Article in Journal
The Dinoflagellate Toxin 20-Methyl Spirolide-G Potently Blocks Skeletal Muscle and Neuronal Nicotinic Acetylcholine Receptors
Next Article in Special Issue
Effects of Milk Yield, Feed Composition, and Feed Contamination with Aflatoxin B1 on the Aflatoxin M1 Concentration in Dairy Cows’ Milk Investigated Using Monte Carlo Simulation Modelling
Previous Article in Journal
Occurrence of Fusarium langsethiae and T-2 and HT-2 Toxins in Italian Malting Barley
Previous Article in Special Issue
Essential Oils Modulate Gene Expression and Ochratoxin A Production in Aspergillus carbonarius
Open AccessArticle

Aflatoxin B1 and M1 Degradation by Lac2 from Pleurotus pulmonarius and Redox Mediators

1
Institute of Sciences of Food Production, National Research Council of Italy (CNR), via Amendola 122/O, Bari 70126, Italy
2
Department of Economics, University of Foggia, via Napoli 25, Foggia 71122, Italy
3
Department of Biomedical Sciences, University of Cagliari, Cittadella Universitaria, Complesso Universitario, SP Monserrato-Sestu Km 0.700, Monserrato 09042, Italy
*
Author to whom correspondence should be addressed.
Academic Editors: Sarah De Saeger, Siska Croubels and Kris Audenaert
Toxins 2016, 8(9), 245; https://doi.org/10.3390/toxins8090245
Received: 12 July 2016 / Revised: 3 August 2016 / Accepted: 15 August 2016 / Published: 23 August 2016
Laccases (LCs) are multicopper oxidases that find application as versatile biocatalysts for the green bioremediation of environmental pollutants and xenobiotics. In this study we elucidate the degrading activity of Lac2 pure enzyme form Pleurotus pulmonarius towards aflatoxin B1 (AFB1) and M1 (AFM1). LC enzyme was purified using three chromatographic steps and identified as Lac2 through zymogram and LC-MS/MS. The degradation assays were performed in vitro at 25 °C for 72 h in buffer solution. AFB1 degradation by Lac2 direct oxidation was 23%. Toxin degradation was also investigated in the presence of three redox mediators, (2,2′-azino-bis-[3-ethylbenzothiazoline-6-sulfonic acid]) (ABTS) and two naturally-occurring phenols, acetosyringone (AS) and syringaldehyde (SA). The direct effect of the enzyme and the mediated action of Lac2 with redox mediators univocally proved the correlation between Lac2 activity and aflatoxins degradation. The degradation of AFB1 was enhanced by the addition of all mediators at 10 mM, with AS being the most effective (90% of degradation). AFM1 was completely degraded by Lac2 with all mediators at 10 mM. The novelty of this study relies on the identification of a pure enzyme as capable of degrading AFB1 and, for the first time, AFM1, and on the evidence that the mechanism of an effective degradation occurs via the mediation of natural phenolic compounds. These results opened new perspective for Lac2 application in the food and feed supply chains as a biotransforming agent of AFB1 and AFM1. View Full-Text
Keywords: laccase; Pleurotus; mycotoxins; aflatoxin B1; aflatoxin M1; biodegradation; redox mediators laccase; Pleurotus; mycotoxins; aflatoxin B1; aflatoxin M1; biodegradation; redox mediators
Show Figures

Graphical abstract

MDPI and ACS Style

Loi, M.; Fanelli, F.; Zucca, P.; Liuzzi, V.C.; Quintieri, L.; Cimmarusti, M.T.; Monaci, L.; Haidukowski, M.; Logrieco, A.F.; Sanjust, E.; Mulè, G. Aflatoxin B1 and M1 Degradation by Lac2 from Pleurotus pulmonarius and Redox Mediators. Toxins 2016, 8, 245.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop