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Analysis of the biodegradation of synthetic testosterone and 17α-ethynylestradiol using the edible mushroom Lentinula edodes

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      Abstract

      The mycelium of Lentinula edodes produces enzymes which may degrade xenobiotics including steroid hormones. The aim of the study was to determine whether the mycelium from in vitro cultures of L. edodes are able to degrade endocrine disruptors such as testosterone and 17α-ethynylestradiol. To prove the possibility of xenobiotics degradation, cultures of L. edodes were cultivated in an Oddoux liquid medium with the addition of synthetic 17α-ethynylestradiol and synthetic testosterone. The endocrine disruptors were extracted from the mycelium and determined qualitatively by RP-HPLC. The degradation products of testosterone and 17α-ethynylestradiol were identified using a UPLC/MS/MS analysis. Undegraded testosterone was determined at the amount of 2.97 mg/g dry weight but only in one of the L. edodes extracts from in vitro cultures supplemented with 50 mg of this compound. In turn, 17α-ethynylestradiol was not determined in any samples. Additionally in all extracts, mushroom sterols (ergosterol peroxide and ergosterol) were determined. Their total amounts were significantly lower in samples containing the abovementioned steroids than in extracts from mycelium L. edodes without the addition of steroid hormones. The results demonstrated that the mycelium of L. edodes can be used in the biodegradation process of a water environment contaminated with endocrine disruptors.

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      Most cited references 29

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        Review: lignin conversion by manganese peroxidase (MnP)

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          Structure and action mechanism of ligninolytic enzymes.

          Lignin is the most abundant renewable source of aromatic polymer in nature, and its decomposition is indispensable for carbon recycling. It is chemically recalcitrant to breakdown by most organisms because of the complex, heterogeneous structure. The white-rot fungi produce an array of extracellular oxidative enzymes that synergistically and efficiently degrade lignin. The major groups of ligninolytic enzymes include lignin peroxidases, manganese peroxidases, versatile peroxidases, and laccases. The peroxidases are heme-containing enzymes with catalytic cycles that involve the activation by H2O2 and substrate reduction of compound I and compound II intermediates. Lignin peroxidases have the unique ability to catalyze oxidative cleavage of C-C bonds and ether (C-O-C) bonds in non-phenolic aromatic substrates of high redox potential. Manganese peroxidases oxidize Mn(II) to Mn(III), which facilitates the degradation of phenolic compounds or, in turn, oxidizes a second mediator for the breakdown of non-phenolic compounds. Versatile peroxidases are hybrids of lignin peroxidase and manganese peroxidase with a bifunctional characteristic. Laccases are multi-copper-containing proteins that catalyze the oxidation of phenolic substrates with concomitant reduction of molecular oxygen to water. This review covers the chemical nature of lignin substrates and focuses on the biochemical properties, molecular structures, reaction mechanisms, and related structures/functions of these enzymes.
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            Author and article information

            Affiliations
            [1 ]ISNI 0000 0001 2162 9631, GRID grid.5522.0, Department of Pharmaceutical Botany, Faculty of Pharmacy, , Jagiellonian University Medical College, ; 30-688 Kraków, Poland
            [2 ]ISNI 0000 0001 2162 9631, GRID grid.5522.0, Department of Medicinal Chemistry, Faculty of Pharmacy, , Jagiellonian University Medical College, ; 30-688 Kraków, Poland
            [3 ]ISNI 0000 0001 2162 9631, GRID grid.5522.0, Department of Inorganic and Analytical Chemistry, Faculty of Pharmacy, , Jagiellonian University Medical College, ; 30-688 Kraków, Poland
            Contributors
            ORCID: http://orcid.org/0000-0002-5007-1486, muchon@poczta.fm
            Journal
            3 Biotech
            3 Biotech
            3 Biotech
            Springer International Publishing (Cham )
            2190-572X
            2190-5738
            28 September 2018
            28 September 2018
            October 2018
            : 8
            : 10
            6162194 1458 10.1007/s13205-018-1458-x
            © The Author(s) 2018

            Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

            Funding
            Funded by: Jagiellonian University Medical College
            Award ID: K/ZDS/007860
            Award Recipient :
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            Original Article
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            © Springer-Verlag GmbH Germany, part of Springer Nature 2018

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