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      Producción de enzimas ligninolíticas durante la degradación del herbicida paraquat por hongos de la pudrición blanca Translated title: Ligninolytic enzyme production by white rot fungi during paraquat (herbicide) degradation

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          Translated abstract

          El paraquat es un herbicida utilizado ampliamente en la agricultura. Debido a su gran distribución y uso inadecuado, representa un problema grave de contaminación del suelo y el agua. Se ha encontrado que los hongos de la podredumbre blanca son capaces de degradar compuestos contaminantes que poseen estructuras similares a la lignina, como es el caso del paraquat. En el presente trabajo se evaluó la degradación de este herbicida y su efecto en la producción de enzimas ligninolíticas por parte de algunos hongos de la podredumbre blanca aislados del sur de México. Seis cepas fúngicas mostraron tolerancia al herbicida durante el cultivo en medio sólido. Tres de las 6 cepas evaluadas, correspondientes a las especies Polyporus tricholoma, Cilindrobasidium laeve y Deconica citrispora, mostraron niveles de degradación del 32, el 26 y el 47%, en ese orden, a los 12 días de cultivo en presencia del xenobiótico. Se detectó un incremento en las actividades de las enzimas lacasa y Mn-peroxidasa en las cepas que presentaron el mayor porcentaje de degradación, probablemente asociado a la disminución del herbicida. Adicionalmente, se realizaron ensayos con extractos enzimáticos procedentes del medio de cultivo extracelular de las 2 cepas que presentaron mayor degradación. Después de 24 h de incubación, se obtuvo una degradación del 49% del paraquat inicial con los extractos de D. citrispora. Los resultados obtenidos indican que la degradación del herbicida estaría asociada a la presencia de enzimas extracelulares en los hongos de la podredumbre blanca. En este trabajo se muestran las primeras evidencias del potencial de biodegradación de diferentes especies de hongos de la pudrición blanca.

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          Manganese(II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. Kinetic mechanism and role of chelators.

          Manganese oxidation by manganese peroxidase (MnP) was investigated. Stoichiometric, kinetic, and MnII binding studies demonstrated that MnP has a single manganese binding site near the heme, and two MnIII equivalents are formed at the expense of one H2O2 equivalent. Since each catalytic cycle step is irreversible, the data fit a peroxidase ping-pong mechanism rather than an ordered bi-bi ping-pong mechanism. MnIII-organic acid complexes oxidize terminal phenolic substrates in a second-order reaction. MnIII-lactate and -tartrate also react slowly with H2O2, with third-order kinetics. The latter slow reaction does not interfere with the rapid MnP oxidation of phenols. Oxalate and malonate are the only organic acid chelators secreted by the fungus in significant amounts. No relationship between stimulation of enzyme activity and chelator size was found, suggesting that the substrate is free MnII rather than a MnII-chelator complex. The enzyme competes with chelators for free MnII. Optimal chelators, such as malonate, facilitate MnIII dissociation from the enzyme, stabilize MnIII in aqueous solution, and have a relatively low MnII binding constant.
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            Biodegradation of lignocellulosics: microbial, chemical, and enzymatic aspects of the fungal attack of lignin

            Wood is the main renewable material on Earth and is largely used as building material and in paper-pulp manufacturing. This review describes the composition of lignocellulosic materials, the different processes by which fungi are able to alter wood, including decay patterns caused by white, brown, and soft-rot fungi, and fungal staining of wood. The chemical, enzymatic, and molecular aspects of the fungal attack of lignin, which represents the key step in wood decay, are also discussed. Modern analytical techniques to investigate fungal degradation and modification of the lignin polymer are reviewed, as are the different oxidative enzymes (oxidoreductases) involved in lignin degradation. These include laccases, high redox potential ligninolytic peroxidases (lignin peroxidase, manganese peroxidase, and versatile peroxidase), and oxidases. Special emphasis is given to the reactions catalyzed, their synergistic action on lignin, and the structural bases for their unique catalytic properties. Broadening our knowledge of lignocellulose biodegradation processes should contribute to better control of wood-decaying fungi, as well as to the development of new biocatalysts of industrial interest based on these organisms and their enzymes.
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              Global diversity and distribution of macrofungi

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                Author and article information

                Contributors
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Journal
                ram
                Revista argentina de microbiología
                Rev. argent. microbiol.
                Asociación Argentina de Microbiología (Ciudad Autónoma de Buenos Aires, , Argentina )
                0325-7541
                1851-7617
                June 2017
                : 49
                : 2
                : 189-196
                Affiliations
                [01] Tapachula Chiapas orgnameEl Colegio de la Frontera Sur México
                Article
                S0325-75412017000200013
                10.1016/j.ram.2016.11.004
                8623bc0a-6c6e-4b59-ae75-0e8795dbc222

                This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.

                History
                : 30 November 2016
                : 24 June 2016
                Page count
                Figures: 0, Tables: 0, Equations: 0, References: 50, Pages: 8
                Product

                SciELO Argentina


                Paraquat,Bioremediation,Pesticides,Extracellular enzymes,Biorremediación,Plaguicidas,Enzimas extracelulares

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