Use of laccase together with redox mediators to decolourize Remazol Brilliant Blue R

Soares, Graça M. B.; Amorim, Maria João; Costa‐Ferreira, Maria

doi:10.1016/s0168-1656(01)00302-9

Cited by 195 publications

(100 citation statements)

References 28 publications

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“…This finding demonstrated the capacity of the enzymatic extracts of these fungi to decolorize RBBR without the addition of hydrogen peroxide, indicating the action of laccase-type oxidases in this process. The identity of the enzymes involved in the degradation of RBBR has not been completely established but degradation is believed to result from the coordinated action of peroxidases and hydrogen peroxide-producing oxidases (Soares et al, 2001;Shin 2004). Recent studies also indicated the involvement of laccases alone or in the presence of specific mediators (Baldrian, 2004;Champagne and Ramsay, 2005;Lu et al, 2007;Murugesan et al, 2007).…”

Section: Resultsmentioning

confidence: 99%

Influence of pH on the growth, laccase activity and RBBR decolorization by tropical basidiomycetes

Neto

Matheus

Machado

2009

Braz. arch. biol. technol.

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The basidiomycete fungi Lentinus crinitus and Psilocybe castanella are being evaluated in a bioremediation process of soils contaminated with organochlorine industrial residues in the Baixada Santista, São Paulo. The aim of the present study was to determine the influence of pH on the fungal growth, in vitro decolorization of anthraquinonic dye Remazol Brilliant Blue R (RBBR) and laccase activity. The pH of the culture medium influenced the growth of L. crinitus and P. castanella, which presented less growth at pH 5.9 and pH 2.7, respectively. The fungi were able to modify the pH of the culture medium, adjusting it to the optimum pH for growth which was close to 4.5. Decolorization of the RBBR was maximal at a pH of 2.5 to 3.5. Higher laccase activity was observed at pH 3.5 and pH 4.5 for L. crinitus and P. castanella, respectively. pH was found to be an important parameter for both the growth of these fungi and the enzymatic system involved in RBBR decolorization.

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Section: Resultsmentioning

confidence: 99%

Influence of pH on the growth, laccase activity and RBBR decolorization by tropical basidiomycetes

Neto

Matheus

Machado

2009

Braz. arch. biol. technol.

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“…Enzyme action response from LiP and MnP could be explained by high ionization potential of these enzymes to readily oxidized non-phenolics compounds, whereas Lac may be able to oxidize these compounds but with a relatively low ionization potential (Soares et al 2001;Shim & Kawamoto 2002). Wesenberg et al (2003) showed that the role of LiP in ligninolysis is additional to action of MnP, since transformation of lignin fragments is initially released by MnP.…”

Section: Discussionmentioning

confidence: 99%

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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“…However, recently a correlation has been described between ligninolytic activity and the degradation of various azo dyes by the basidiomycete PV002 (26). The presence of mediators was essential for the decolorization of RBBR by a commercial formulation of laccase used in the textile industry (24).…”

Section: Initial Activity Of the Enzymatic Extractsmentioning

confidence: 99%

“…It is the raw material in the production of polymeric dyes and, as a derivative of anthracene, represents an important member of toxic and recalcitrant organopollutants. The identity of enzymes involved in the degradation of RBBR is still not completely established, with evidence indicating the involvement of lignin peroxidase and laccases (4,17,24).…”

Section: Introductionmentioning

confidence: 99%

Biodegradation of remazol brilliant blue R by ligninolytic enzymatic complex produced by Pleurotus ostreatus

Machado¹,

Matheus²

2006

Braz. J. Microbiol.

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Pleurotus ostreatus ("shimeji") is produced in Brazil on a commercial scale using various lignocellulosic residues. Efforts have been made to reuse the culture residue to obtain products of greater aggregate value such as enzymes or in processes of bioremediation. We evaluated the Remazol brilliant blue R (RBBR) degradation potential of extracts from solid substrate colonized by P. ostreatus and extracts from residue of the "shimeji" mushroom yield. Colonized substrates and residue were provided by Toyobo do Brasil Ltda. Extraction was performed with sodium acetate buffer (50 mM, pH 4.6). RBBR decolorization was monitored at 592 nm and peroxidase and laccase activities were measured by monitoring the oxidation of ABTS. Horseradish peroxidase was used as reference. The time of growth of P. ostreatus influenced RBBR degradation and peroxidase and laccase activities. Concentration of 1 mM H2O2 and pH 4.0 were the best for RBBR decolorization. Complete RBBR decolorization was obtained with the addition of only one aliquot of 50 µL of 1 mM H2O2. The stability of the extracts was higher when they were kept under refrigeration than when stored frozen. The potential application of the ligninolytic complex derived from P. ostreatus and mushroom residue for xenobiotic degradation was demonstrated.

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Use of laccase together with redox mediators to decolourize Remazol Brilliant Blue R

Cited by 195 publications

References 28 publications

Influence of pH on the growth, laccase activity and RBBR decolorization by tropical basidiomycetes

Influence of pH on the growth, laccase activity and RBBR decolorization by tropical basidiomycetes

Enzyme production by immobilized Phanerochaete chrysosporium using airlift reactor

Biodegradation of remazol brilliant blue R by ligninolytic enzymatic complex produced by Pleurotus ostreatus

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