Comparative study of in vitro prooxidative properties and genotoxicity induced by aflatoxin B1 and its laccase-mediated detoxification products

Zeinvand-Lorestani, Hamed; Sabzevari, Omid; Setayesh, Neda; Amini, Mohsen; Nili‐Ahmadabadi, Amir; Faramarzi, Mohammad Ali

doi:10.1016/j.chemosphere.2015.03.036

Cited by 73 publications

(42 citation statements)

References 34 publications

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“…The use of other types of enzymes in AF degradation has also been reported in the literature. In the enzymatic AFB 1 degradation by laccase activity, a range of pH values (2.5–7.0) and temperatures (5–65 °C) were evaluated with 80 µg mL −1 AFB 1 and 30 U mL −1 enzyme, resulting in an optimum pH and temperature of 4.5 and 35 °C, respectively . The enzyme MADE (myxobacteria AF degradation enzyme), from the bacterium Myxococcus fulvu s, demonstrated high activity over a wide range of pH (5–7) and temperatures (30–45 °C), obtaining 96.0% and 95.8% degradation for AFG 1 and AFM 1 , respectively, after treatment with purified MADE (100 U mL −1 ) for 48 h .…”

Section: Resultsmentioning

confidence: 99%

Aflatoxin biotransformation by commercial peroxidase and its application in contaminated food

Sibaja

Garcia

Feltrin

et al. 2018

J of Chemical Tech & Biotech

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BACKGROUND Aflatoxin B1 (AFB1) is the most commonly occurring and the most toxic of all aflatoxins (AFs). It is responsible for liver cancer in animals and it is listed as a Group I carcinogen by the International Agency for Research on Cancer. Thus, it is necessary to find decontamination methods that show efficiency, specificity, low cost, and that allow the disposal of contaminated raw materials into the environment. This study evaluated the effects of enzyme concentration, pH, temperature and reaction time on AFB1 biotransformation by commercial peroxidase (POD) in a model solution (100 mmol L−1 phosphate buffer). RESULTS When 0.015 U mL−1 was used to treat 0.5 µg L−1 of AFB1, at pH 7.0–8.0 and 30–40 °C, for 8.0 h, the AFB1 biotransformation reached its maximum (97%). KM value of POD for the biotransformation of AFB1 was 0.0160 µmol L−1 (5 µg L−1) with a VMAX of 6.4 µmol L−1 min−1, which were determined based on Lineweaver‐Burk's plot. POD (0.015 U mL−1) effectively reduces AFB1 (97%) and M1 (65%) in UHT milk and AFB1 (24%) in lager beer samples acquired in markets of Rio Grande‐RS (Brazil). CONCLUSION The use of POD may be a strategy to mitigate the impact of AFs found in food to reduce the risk of consumer exposure. © 2018 Society of Chemical Industry

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Section: Resultsmentioning

confidence: 99%

Aflatoxin biotransformation by commercial peroxidase and its application in contaminated food

Sibaja

Garcia

Feltrin

et al. 2018

J of Chemical Tech & Biotech

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“…Treatment of the AFB1 solution in the presence of recombinant laccases (1 U/mL) decreased the AFB1 level to 12.6% of the initial concentration . Recently, Zeinvand‐Lorestani et al investigated the prooxidant properties and the mutagenicity of the detoxification products obtained from the treatment of AFB1 using the purified laccase of T. versicolor . They reported 67% of the toxic substrate was removed and the mutagenicity of the laccase‐treated product decreased significantly after 48 h incubation of AFB1 in the presence of laccase (30 U/mL) .…”

Section: Biotechnological and Industrial Applications Of Laccasesmentioning

confidence: 99%

“…Recently, Zeinvand‐Lorestani et al investigated the prooxidant properties and the mutagenicity of the detoxification products obtained from the treatment of AFB1 using the purified laccase of T. versicolor . They reported 67% of the toxic substrate was removed and the mutagenicity of the laccase‐treated product decreased significantly after 48 h incubation of AFB1 in the presence of laccase (30 U/mL) . Detoxification of endocrine‐disrupting compounds (EDCs) and different classes of pharmaceutical agents, such as antibiotics, analgesics, anticonvulsants, and sedatives, released from pharmaceutical company wastewaters by laccases from different organisms, has received increased attention during the last few decades .…”

Section: Biotechnological and Industrial Applications Of Laccasesmentioning

confidence: 99%

“…They reported 67% of the toxic substrate was removed and the mutagenicity of the laccase-treated product decreased significantly after 48 h incubation of AFB1 in the presence of laccase (30 U/mL). 137 Detoxification of endocrine-disrupting compounds (EDCs) and different classes of pharmaceutical agents, such as antibiotics, analgesics, anticonvulsants, and sedatives, released from pharmaceutical company wastewaters by laccases from differ-ent organisms, has received increased attention during the last few decades. 92,[138][139][140] In most of these investigations, the laccase-treated products showed lower toxicity compared with the initial compounds.…”

Section: Bioremediation Of Environmental Pollutantsmentioning

confidence: 99%

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Insights into laccase producing organisms, fermentation states, purification strategies, and biotechnological applications

Forootanfar

Faramarzi

2015

Biotechnology Progress

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Laccases are phenol oxidases belonging to the superfamily of multicopper oxidases and are found in bacteria, fungi, lichens, higher plants, and insects. Over the past few decades, laccases and laccase mediator systems (LMS) have found uses in a wide range of technological applications such as textile dye decolorization, industrial wastewater detoxification, pulp bleaching, chemical synthesis, and development of miniaturized biosensors. This has encouraged numerous studies to find and purify laccases with exploitable characteristics. The main aim of the present review is to summarize the rich literature data gained in recent years from the studies on laccases, focusing on the organisms that produce them, the methods used for screening, laccase activity assays, purification strategies, and the application of laccases as eco-friendly biocatalysts.

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“…Detoxification methods using enzymes, such as laccase and manganese peroxidase, have also been suggested for reducing aflatoxin contamination [10,11]. Physical and chemical methods, such as ozone and gamma-irradiation, can also remove aflatoxins from contaminated foodstuffs in an efficient manner [12,13].…”

Section: Introductionmentioning

confidence: 99%

Antifungal and Antiaflatoxigenic Methylenedioxy-Containing Compounds and Piperine-Like Synthetic Compounds

Moon

Choi

Park

et al. 2016

Toxins

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Twelve methylenedioxy-containing compounds including piperine and 10 piperine-like synthetic compounds were assessed to determine their antifungal and antiaflatoxigenic activities against Aspergillus flavus ATCC 22546 in terms of their structure–activity relationships. Piperonal and 1,3-benzodioxole had inhibitory effects against A. flavus mycelial growth and aflatoxin B1 production up to a concentration of 1000 μg/mL. Ten piperine-like synthetic compounds were synthesized that differed in terms of the carbon length in the hydrocarbon backbone and the presence of the methylenedioxy moiety. In particular, 1-(2-methylpiperidin-1-yl)-3-phenylprop-2-en-1-one had potent antifungal and antiaflatoxigenic effects against A. flavus up to a concentration of 1 μg/mL. This synthetic compound was remarkable because the positive control thiabendazole had no inhibitory effect at this concentration. Reverse transcription-PCR analysis showed that five genes involved in aflatoxin biosynthesis pathways were down-regulated in A. flavus, i.e., aflD, aflK, aflQ, aflR, and aflS; therefore, the synthetic compound inhibited aflatoxin production by down-regulating these genes.

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Comparative study of in vitro prooxidative properties and genotoxicity induced by aflatoxin B1 and its laccase-mediated detoxification products

Cited by 73 publications

References 34 publications

Aflatoxin biotransformation by commercial peroxidase and its application in contaminated food

Aflatoxin biotransformation by commercial peroxidase and its application in contaminated food

Insights into laccase producing organisms, fermentation states, purification strategies, and biotechnological applications

Antifungal and Antiaflatoxigenic Methylenedioxy-Containing Compounds and Piperine-Like Synthetic Compounds

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