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      Screening of Basidiomycetes with laccase activity for lignin degradation on POME

      IOP Conference Series: Earth and Environmental Science
      IOP Publishing

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          Abstract

          Laccase producing Basidiomycetes were selected to degrade lignin on Palm Oil Mill Effluent (POME). The selection to obtain fungal isolates which produce high activity ligninolytic enzymes has been done continuously. The objective of the research was to isolate high activity enzymes producing fungus and obtain the data on enzyme activity changes after the addition of inducer. Fruiting body of fungus were collected in surrounding area of Cibinong Sciences Centre and Bogor Botanical Garden. Twelve isolates were obtained and all of the isolates could grow on Poly R-478. Isolate Mycena sp J24 produced the highest laccase activity. The fungus was able to decolorize Poly R-478 as much as 89.73% in 21 days incubation. The addition of CuSO 4 increased decolorization rate as much as 2.32%. Mycena sp J24 reduced 33.82% of POME color in fifteen days incubation. The addition of CuSO 4 increased POME decolorization as much as 72.11%. This fungus could also reduce COD level on POME as much as 33.14% in fifteen days incubation. The addition of veratryl alcohol increased the reduction of COD level as much as 55.15%. Mycena sp J24 produced the highest amount of laccase and could be applied on POME degradation as well.

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          Most cited references24

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          Laccase: new functions for an old enzyme

          A. Mayer (2002)
          Laccases occur widely in fungi; they have been characterized less frequently in higher plants. Here we have focused on more recent reports on the occurrence of laccase and its functions in physiological development and industrial utility. The reports of molecular weights, pH optima, and substrate specificity are extremely diverse. Conclusive proof of the occurrence of laccase in a tissue must demonstrate that the enzyme be able to oxidize quinol with concomitant uptake of oxygen. Laccase is involved in the pigmentation process of fungal spores, the regeneration of tobacco protoplasts, as fungal virulence factors, and in lignification of cell walls and delignification during white rot of wood. Commercially, laccases have been used to delignify woody tissues, produce ethanol, and to distinguish between morphine and codeine. A very wide variety of bioremediation processes employ laccase in order to protect the environment from damage caused by industrial effluents. Research in recent years has been intense, much of it elicited by the wide diversity of laccases, their utility and their very interesting enzymology.
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            The structure and function of fungal laccases

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              White-rot fungi and their enzymes for the treatment of industrial dye effluents.

              White-rot fungi produce various isoforms of extracellular oxidases including laccase, Mn peroxidase and lignin peroxidase (LiP), which are involved in the degradation of lignin in their natural lignocellulosic substrates. This ligninolytic system of white-rot fungi (WRF) is directly involved in the degradation of various xenobiotic compounds and dyes. This review summarizes the state of the art in the research and prospective use of WRF and their enzymes (lignin-modifying enzymes, LME) for the treatment of industrial effluents, particularly dye containing effluents. The textile industry, by far the most avid user of synthetic dyes, is in need of ecoefficient solutions for its colored effluents. The decolorization and detoxification potential of WRF can be harnessed thanks to emerging knowledge of the physiology of these organisms as well as of the biocatalysis and stability characteristics of their enzymes. This knowledge will need to be transformed into reliable and robust waste treatment processes.
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                Author and article information

                Journal
                IOP Conference Series: Earth and Environmental Science
                IOP Conf. Ser.: Earth Environ. Sci.
                IOP Publishing
                1755-1307
                1755-1315
                August 01 2019
                August 01 2019
                : 308
                : 1
                : 012013
                Article
                10.1088/1755-1315/308/1/012013
                dd5284e0-7a68-47c2-b13b-53545ff404d7
                © 2019

                http://creativecommons.org/licenses/by/3.0/

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