Laccase Production from <i>Agrocybe pediades</i>: Purification and Functional Characterization of a Consistent Laccase Isoenzyme in Liquid Culture
Laccases are valuable enzymes as an excellent ecological alternative for bioremediation issues because they can oxidize persistent xenobiotic compounds. The production and characterization of extracellular laccases from saprotrophic fungi from disturbed environments have been scarcely explored, even...
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| Format: | Article |
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MDPI AG
2023-02-01
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| Series: | Microorganisms |
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| Online Access: | https://www.mdpi.com/2076-2607/11/3/568 |
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| author | Paulina González-González Saúl Gómez-Manzo Araceli Tomasini José Luis Martínez y Pérez Edelmira García Nieto Arely Anaya-Hernández Elvia Ortiz Ortiz Rosa Angélica Castillo Rodríguez Jaime Marcial-Quino Alba Mónica Montiel-González |
| author_facet | Paulina González-González Saúl Gómez-Manzo Araceli Tomasini José Luis Martínez y Pérez Edelmira García Nieto Arely Anaya-Hernández Elvia Ortiz Ortiz Rosa Angélica Castillo Rodríguez Jaime Marcial-Quino Alba Mónica Montiel-González |
| author_sort | Paulina González-González |
| collection | DOAJ |
| description | Laccases are valuable enzymes as an excellent ecological alternative for bioremediation issues because they can oxidize persistent xenobiotic compounds. The production and characterization of extracellular laccases from saprotrophic fungi from disturbed environments have been scarcely explored, even though this could diversify their functional characteristics and expand the conditions in which they carry out their catalysis. <i>Agrocybe pediades</i>, isolated from a disturbed forest, produces an extracellular laccase in liquid culture. The enzyme was purified, identified and characterized. Copper and hexachlorobenzene do not function as inducers for the laccase produced. Partial amino acid sequences were obtained by LC-MS/MS that share similarity with laccases from other fungi. Purified laccase is a monomer with a molecular mass between 55–60 kDa and had an optimum activity at pH 5.0 and the optimum temperature at 45 °C using 2,6-dimethoxyphenol (2,6-DMP) as substrate. The <i>K</i><sub>m</sub> and <i>V</i><sub>max</sub> also determined with 2,6-DMP were 100 μM and 285 μmol∙min<sup>−1</sup>∙mg<sup>−1</sup>, respectively, showing that the laccase of <i>A</i>. <i>pediades</i> has a higher affinity for this substrate than that of other Agaricales. These features could provide a potential catalyst for different toxic substrates and in the future laccase could be used in environmental recovery processes. |
| first_indexed | 2024-03-09T11:00:29Z |
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| id | doaj.art-b7f54cf9b0c44f50aef1aa016ed43de0 |
| institution | Directory Open Access Journal |
| issn | 2076-2607 |
| language | English |
| last_indexed | 2024-03-09T11:00:29Z |
| publishDate | 2023-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Microorganisms |
| spelling | doaj.art-b7f54cf9b0c44f50aef1aa016ed43de02023-12-01T01:20:23ZengMDPI AGMicroorganisms2076-26072023-02-0111356810.3390/microorganisms11030568Laccase Production from <i>Agrocybe pediades</i>: Purification and Functional Characterization of a Consistent Laccase Isoenzyme in Liquid CulturePaulina González-González0Saúl Gómez-Manzo1Araceli Tomasini2José Luis Martínez y Pérez3Edelmira García Nieto4Arely Anaya-Hernández5Elvia Ortiz Ortiz6Rosa Angélica Castillo Rodríguez7Jaime Marcial-Quino8Alba Mónica Montiel-González9Maestría en Ciencias en Sistemas del Ambiente, Centro de Investigación en Genética y Ambiente, Universidad Autónoma de Tlaxcala, Tlaxcala 90120, MexicoLaboratorio de Bioquímica Genética, Instituto Nacional de Pediatría, Secretaría de Salud, Ciudad de Mexico 04530, MexicoDepartamento de Biotecnología, CBS, Universidad Autónoma Metropolitana-Iztapalapa, Ciudad de Mexico 09340, MexicoCentro de Investigación en Genética y Ambiente, Universidad Autónoma de Tlaxcala, Tlaxcala 90120, MexicoCentro de Investigación en Genética y Ambiente, Universidad Autónoma de Tlaxcala, Tlaxcala 90120, MexicoCentro de Investigación en Genética y Ambiente, Universidad Autónoma de Tlaxcala, Tlaxcala 90120, MexicoFacultad de Odontología, Universidad Autónoma de Tlaxcala, Tlaxcala 90000, MexicoCICATA Unidad Morelos, Instituto Politécnico Nacional. Boulevard de la Tecnología, 1036 Z-1, P 2/2, Atlacholoaya 62790, MexicoCentro de Investigación en Genética y Ambiente, Universidad Autónoma de Tlaxcala, Tlaxcala 90120, MexicoCentro de Investigación en Genética y Ambiente, Universidad Autónoma de Tlaxcala, Tlaxcala 90120, MexicoLaccases are valuable enzymes as an excellent ecological alternative for bioremediation issues because they can oxidize persistent xenobiotic compounds. The production and characterization of extracellular laccases from saprotrophic fungi from disturbed environments have been scarcely explored, even though this could diversify their functional characteristics and expand the conditions in which they carry out their catalysis. <i>Agrocybe pediades</i>, isolated from a disturbed forest, produces an extracellular laccase in liquid culture. The enzyme was purified, identified and characterized. Copper and hexachlorobenzene do not function as inducers for the laccase produced. Partial amino acid sequences were obtained by LC-MS/MS that share similarity with laccases from other fungi. Purified laccase is a monomer with a molecular mass between 55–60 kDa and had an optimum activity at pH 5.0 and the optimum temperature at 45 °C using 2,6-dimethoxyphenol (2,6-DMP) as substrate. The <i>K</i><sub>m</sub> and <i>V</i><sub>max</sub> also determined with 2,6-DMP were 100 μM and 285 μmol∙min<sup>−1</sup>∙mg<sup>−1</sup>, respectively, showing that the laccase of <i>A</i>. <i>pediades</i> has a higher affinity for this substrate than that of other Agaricales. These features could provide a potential catalyst for different toxic substrates and in the future laccase could be used in environmental recovery processes.https://www.mdpi.com/2076-2607/11/3/568<i>Agrocybe pediades</i>extracellular laccase2,6-dimethoxyphenolkinetic parameters |
| spellingShingle | Paulina González-González Saúl Gómez-Manzo Araceli Tomasini José Luis Martínez y Pérez Edelmira García Nieto Arely Anaya-Hernández Elvia Ortiz Ortiz Rosa Angélica Castillo Rodríguez Jaime Marcial-Quino Alba Mónica Montiel-González Laccase Production from <i>Agrocybe pediades</i>: Purification and Functional Characterization of a Consistent Laccase Isoenzyme in Liquid Culture Microorganisms <i>Agrocybe pediades</i> extracellular laccase 2,6-dimethoxyphenol kinetic parameters |
| title | Laccase Production from <i>Agrocybe pediades</i>: Purification and Functional Characterization of a Consistent Laccase Isoenzyme in Liquid Culture |
| title_full | Laccase Production from <i>Agrocybe pediades</i>: Purification and Functional Characterization of a Consistent Laccase Isoenzyme in Liquid Culture |
| title_fullStr | Laccase Production from <i>Agrocybe pediades</i>: Purification and Functional Characterization of a Consistent Laccase Isoenzyme in Liquid Culture |
| title_full_unstemmed | Laccase Production from <i>Agrocybe pediades</i>: Purification and Functional Characterization of a Consistent Laccase Isoenzyme in Liquid Culture |
| title_short | Laccase Production from <i>Agrocybe pediades</i>: Purification and Functional Characterization of a Consistent Laccase Isoenzyme in Liquid Culture |
| title_sort | laccase production from i agrocybe pediades i purification and functional characterization of a consistent laccase isoenzyme in liquid culture |
| topic | <i>Agrocybe pediades</i> extracellular laccase 2,6-dimethoxyphenol kinetic parameters |
| url | https://www.mdpi.com/2076-2607/11/3/568 |
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