Transformation pathway of Remazol Brilliant Blue R by immobilised laccase

Osma, Johann F.; Toca-Herrera, José L.; Rodríguez‐Couto, Susana

doi:10.1016/j.biortech.2010.06.074

Cited by 133 publications

(92 citation statements)

References 44 publications

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“…However, current decolourization experiments with immobilized Lac showed that this enzyme is able to operate during 15 decolouration cycles loosing only 50% of its original activity (Osma et al 2010). Commercial Lac formulation (0.010 × 10 3 U/mL) was also tested in the presence of 5.7 mM violuric acid to treat the RBBR and in this test the Lac capacity was confirmed to achieve 90% of decolourization in 20 min (Soares et al 2001).…”

Section: Discussionmentioning

confidence: 97%

Enzyme production by immobilized Phanerochaete chrysosporium using airlift reactor

et al. 2014

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Enzyme production by immobilized Phanerochaete chrysosporium was evaluated in airlift bioreactor and agitated cultures. Free mycelium and immobilized mycelium on alginate beads were tested in the decolourization of 50 and 500 mg/L of Remazol Brilliant Blue R. Dye concentration did not inhibit the fungi development in all tests. In addition, high decolourization percentage of dye was found with free mycelium (99%) in agitated flasks and with immobilized mycelium in airlift (98%). However, decolourization period by immobilized mycelium (120 h) was greater than that by the free mycelium (14 h). Important manganese peroxidase, lignine peroxidase and laccase activities were identified in decolourization process. Manganese peroxidase appeared to be promoted by high dye concentrations during the treatment with immobilized mycelium, but this enzyme was not detected with free mycelium in airlift. Bioreactor prompted also laccase and lignine peroxidase actions in both tests; free mycelium registered a maximum laccase action of 31.569 × 10 3 U/L in 70 h, whereas immobilized mycelium registered 1.680 × 10 3 U/L in 170 h, while lignine peroxidase secretion by free P. chrysosporium was higher (1.300 × 10 3 U/L) than immobilized mycelium (1.250 × 10 3 U/L). Maximum laccase activity coincided with the maximum percentage of decolourization, however, high peroxidase activity was identified from the start of dye treatment.

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Section: Discussionmentioning

confidence: 97%

Enzyme production by immobilized Phanerochaete chrysosporium using airlift reactor

et al. 2014

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“…Several species have been traditionally used for evaluating phytotoxicity. However there are no standardised seed species in use worldwide (Osma et al, 2010;Warman, 1999).…”

Section: Resultsmentioning

confidence: 99%

“…However, most of these did not analyse the toxicity of the final residues. Thus, it is also relevant to assess the phytotoxicity of these wastes before and after degradation (Osma et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

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Aerobic biotransformation of 2, 4, 6–trichlorophenol by <i>Penicillium chrysogenum</i> in aqueous batch culture: Degradation and residual phytotoxicity

Aranciaga¹,

Durruty²,

Gonzalez³

et al. 2012

WSA

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Abstract2,4,6-trichlorophenol (TCP) is a toxic compound widespread in the environment, with numerous applications. There are many fungi capable of degrading it, although little attention has been paid to non wood-degrading species. Penicillium chrysogenum ERK1 was able to degrade 85% of TCP in batch cultures in the presence of sodium acetate. Degradation rate was fitted to a specific first-order kinetic and the growth rate was fitted to a Gompertz model. Hydroquinone and benzoquinone were identified as degradation intermediates. The phytotoxicity of the residues was reduced by half after fungal treatment. These results suggest that Penicillium chrysogenum can be applied successfully to biodegrade TCP.

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“…The optimum pH was between pH 3 and 5 because the pH range is suitable for the growth and enzymatic production by white-rot fungi (O'Mahony et al 2002). On the other hand, the biodegradation of synthetic dye by white-rot fungus Lentinus polychrous was optimum at pH 3 (Osma et al 2010). The pH of the liquid medium will change the charge of the enzyme thus influences the adsorption of charge dye groups to it.…”

Section: Effect Of Initial Dye Concentration On the Decolorization Ofmentioning

confidence: 99%

Microbial Decolorization of an Azo Dye Reactive Black 5 Using White-Rot Fungus Pleurotus eryngii F032

Hadibarata

Adnan

Yusoff

et al. 2013

Water Air Soil Pollut

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The growth of white-rot fungus Pleurotus eryngii F032 in a suitable medium can degrade an azo dye Reactive Black 5 (RB5), because of its ability to produce ligninolytic enzymes such as lignin peroxidase (LiP), manganese peroxidase (MnP), and laccase that able to degrade and transform the complex structure of the dye into a less toxic compound. The effect of environmental factors such as initial concentration of Reactive Black 5, pH, temperature of growth medium, surfactant (Tween 80), and agitation were also investigated. The productions of ligninolytic enzymes were enhanced by increasing the white-rot fungi growth in optimum conditions. The decolorization of Reactive Black 5 were analyzed by using UV-vis spectrophotometer at the maximum absorbance of 596 nm. The whiterot fungus, P. eryngii F032 culture exhibited 93.56 % decolorization of 10 mg/L RB5 within 72 h of incubation in dark condition with agitation. The optimum pH and temperature for the decolorizing activity was recorded at pH 3 and 40°C, respectively. The addition of surfactant (Tween 80) increased the decolorization to 93.57 % and agitation of growth medium at 120 rpm enhanced the distribution of nutrients to the fungus thus optimized the enzymatic reaction that resulted maximum decolorization of RB5 which was 93.57 %. The molecular docking studies were performed using Chimera visualization software as to analyze the decolorization mechanism of RB5 at molecular level.

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Transformation pathway of Remazol Brilliant Blue R by immobilised laccase

Cited by 133 publications

References 44 publications

Enzyme production by immobilized Phanerochaete chrysosporium using airlift reactor

Enzyme production by immobilized Phanerochaete chrysosporium using airlift reactor

Aerobic biotransformation of 2, 4, 6–trichlorophenol by <i>Penicillium chrysogenum</i> in aqueous batch culture: Degradation and residual phytotoxicity

Microbial Decolorization of an Azo Dye Reactive Black 5 Using White-Rot Fungus Pleurotus eryngii F032

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