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      Aflatoxin B 1 Conversion by Black Soldier Fly ( Hermetia illucens) Larval Enzyme Extracts

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          Abstract

          The larvae of the black soldier fly ( Hermetia illucens L., BSFL) have received increased industrial interest as a novel protein source for food and feed. Previous research has found that insects, including BSFL, are capable of metabolically converting aflatoxin B 1 (AFB 1), but recovery of total AFB 1 is less than 20% when accounting for its conversion to most known metabolites. The aim of this study was to examine the conversion of AFB 1 by S9 extracts of BSFL reared on substrates with or without AFB 1. Liver S9 of Aroclor-induced rats was used as a reference. To investigate whether cytochrome P450 enzymes are involved in the conversion of AFB 1, the inhibitor piperonyl butoxide (PBO) was tested in a number of treatments. The results showed that approximately 60% of AFB 1 was converted to aflatoxicol and aflatoxin P 1. The remaining 40% of AFB 1 was not converted. Cytochrome P450s were indeed responsible for metabolic conversion of AFB 1 into AFP 1, and a cytoplasmic reductase was most likely responsible for conversion of AFB 1 into aflatoxicol.

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          Cytochromes P450 and insecticide resistance.

          Jeffrey G Scott (1999)
          The cytochrome P450-dependent monooxygenases (monooxygenases) are an extremely important metabolic system involved in the catabolism and anabolism of xenobiotics and endogenous compounds. Monooxygenase-mediated metabolism is a common mechanism by which insects become resistant to insecticides as evidenced by the numerous insect species and insecticides affected. This review begins by presenting background information about P450s, the role of monooxygenases in insects, and the different techniques that have been used to isolate individual insect P450s. Next, insecticide resistance is briefly described, and then historical information about monooxygenase-mediated insecticide resistance is reviewed. For any case of monooxygenase-mediated resistance, identification of the P450(s) involved, out of the dozens that are present in an insect, has proven very challenging. Therefore, the next section of the review focuses on the minimal criteria for establishing that a P450 is involved in resistance. This is followed by a comprehensive examination of the literature concerning the individual P450s that have been isolated from insecticide resistant strains. In each case, the history of the strain and the evidence for monooxygenase-mediated resistance are reviewed. The isolation and characterization of the P450(s) from the strain are then described, and the evidence of whether or not the isolated P450(s) is involved in resistance is summarized. The remainder of the review summarizes our current knowledge of the molecular basis of monooxygenase-mediated resistance and the implications for the future. The importance of these studies for development of effective insecticide resistance management strategies is discussed.
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            Review of mycotoxin reduction in food and feed: from prevention in the field to detoxification by adsorption or transformation.

            G Jard, T Liboz, F. Mathieu … (2011)
            Mycotoxins are secondary metabolites present worldwide in agricultural commodities and produced by filamentous fungi that cause a toxic response (mycotoxicosis) when ingested by animals. Prevention of mycotoxicoses includes pre- and post-harvest strategies. The best way to reduce the mycotoxin content in food and feed is the prevention of mycotoxin formation in the field, but this is often not sufficient, so other methods are needed. To decontaminate and/or detoxify mycotoxin-contaminated food and feed, the most prevalent approach in the feed industry is the inclusion of sorbent materials in the feed thus obtaining more or less selective removal of toxins by adsorption during passage through the gastrointestinal tract. Another reliable approach is to add enzymes or microorganisms capable of detoxifying some mycotoxins. Through a comprehensive review of published reports on the strategies for mycotoxin removal, this present work aims to update our understanding of mycotoxin removal. It provides an insight into the detoxification of mycotoxin present in food and feed. In the future, more emphasis needs to be placed on adsorption of mycotoxins in the gastrointestinal tract. Concerning the enzymatic transformation of mycotoxins, further efforts are required in understanding detoxification reactions, the toxicity of transformation products and in the characterization of enzymes responsible for transformations.
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              Metabolism of aflatoxins: key enzymes and interindividual as well as interspecies differences.

              Vlastimil Dohnal, Qinghua Wu, Kamil Kuca (2014)
              Aflatoxins are potent hepatocarcinogen in animal models and suspected carcinogen in humans. The most important aflatoxin in terms of toxic potency and occurrence is aflatoxin B1 (AFB1). In this review, we mainly summarized the key metabolizing enzymes of AFB1 in animals and humans. Moreover, the interindividual and the interspecies differences in AFB1 metabolism are highly concerned. In human liver, CYP3A4 plays an important role in biotransforming AFB1 to the toxic product AFB1-8,9-epoxide. In human lung, CYP2A13 has a significant activity in metabolizing AFB1 to AFB1-8,9-epoxide and AFM1-8,9-epoxide. The epoxide of AFB1-8,9-epoxide could conjugate with glutathione to reduce the toxicity by glutathione-S-transferase (GST). In poultry species, CYP2A6, CYP3A37, CYP1A5, and CYP1A1 are responsible for bioactivation of AFB1. There are interindividual variations in the rate of activation of aflatoxins in various species, and there are also differences between children and adults. The age and living regions are important factors affecting resistance of species to AFB1. The rate of AFB1-8,9-epoxide formation and its conjugation with glutathione are key parameters in interspecies and interindividual differences in sensitivity to the toxic effect of AFB1. This review provides an important information for key metabolizing enzymes and the global metabolism of aflatoxins in different species.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Toxins (Basel)
                Journal ID (iso-abbrev): Toxins (Basel)
                Journal ID (publisher-id): toxins
                Title: Toxins
                Publisher: MDPI
                ISSN (Electronic): 2072-6651
                Publication date (Electronic): 12 September 2019
                Publication date Collection: September 2019
                Volume: 11
                Issue: 9
                Electronic Location Identifier: 532
                Affiliations
                [1 ]Wageningen Food Safety Research, Wageningen Campus P.O. Box 230, 6700 AE Wageningen, The Netherlands; geert.stoopen@ 123456wur.nl
                [2 ]Wageningen University, Department of Plant Sciences, Laboratory of Entomology, Wageningen Campus P.O. Box 16, 6700 AA Wageningen, The Netherlands; joop.vanloon@ 123456wur.nl
                [3 ]Mars, Incorporated, McLean, VA 22101, USA, john.carney@ 123456effem.com
                [4 ]JMC Consulting, Portland, OR 972229, USA
                [5 ]Wageningen University, Department of Animal Sciences, Animal Nutrition Group, Wageningen Campus P.O. Box 338, 6700 AH Wageningen, The Netherlands; guido.bosch@ 123456wur.nl
                Author notes
                [* ]Correspondence: nathan.meijer@ 123456wur.nl (N.M.); ine.vanderfels@ 123456wur.nl (H.J.v.d.F.-K.)
                Author information
                https://orcid.org/0000-0002-7801-394X
                https://orcid.org/0000-0002-4260-0501
                https://orcid.org/0000-0002-5714-9506
                Article
                Publisher ID: toxins-11-00532
                DOI: 10.3390/toxins11090532
                PMC ID: 6784232
                PubMed ID: 31547476
                SO-VID: 38b3cee4-3fb0-449c-a0cb-04cdeea4b1cb
                Copyright © © 2019 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 24 July 2019
                Date accepted : 10 September 2019
                Categories
                Subject: Article

                ScienceOpen disciplines: Molecular medicine
                Keywords: aflatoxin,mycotoxin,black soldier fly,bsfl,hermetia illucens,s9 fraction,cytochrome p450,metabolic conversion,enzyme induction
                Data availability:
                ScienceOpen disciplines: Molecular medicine
                Keywords: aflatoxin, mycotoxin, black soldier fly, bsfl, hermetia illucens, s9 fraction, cytochrome p450, metabolic conversion, enzyme induction

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