Decolorization of azo dyes by Phanerochaete chrysosporium and Pleurotus sajorcaju

Chagas, Eliana Pereira; Durrant, Lúcia Regina

doi:10.1016/s0141-0229(01)00405-7

Cited by 163 publications

(74 citation statements)

References 15 publications

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“…Several other lignolytic fungi were shown to degrade azo dyes investigated including P. chrysosporium [47,48], T. versicolor [49], T. modesta [50] and Aspergillus niger [51]. Previously, a purified laccase from A. niger was shown to decolourize one of four diazo dyes tested, demonstrating a specificity for the type or position of substituents on the phenolic ring of the dye structure [14].…”

Section: Dye Decolourizationmentioning

confidence: 99%

An acid-stable laccase from Sclerotium rolfsii with potential for wool dye decolourization

Ryan

Schnitzhofer

Tzanov

et al. 2003

Enzyme and Microbial Technology

108

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The plant pathogen basidiomycete S. rolfsii secretes two laccases (SRL1 and SRL2) with molecular weights of 55 and 86 kDa, respectively. Laccase production was shown to be inducible by the addition of 2,5-xylidine to the cultural media. After treatment with a combination of chitinase and ␤-1,3-glucanase, two different laccases were isolated from the sclerotia depending on the stage of sclerotia development.The more prominent laccase, SRL1, was purified and found to decolourize the industrially important wool azo dye Diamond Black PV 200 without the addition of redox mediators. The enzyme (pI 5.2) was active in the acidic pH range, showing an optimal activity at pH 2.4, with ABTS as substrate. The optimum temperature for activity was determined to be 62 • C. Enzyme stability studies revealed that SRL1 was notably stable at 18 • C and pH 4.5, retaining almost full activity after a week. Oxidation of tyrosine was not detectable under the reaction conditions but the enzyme did oxidize a variety of the usual laccase substrates. SRL1 was strongly inhibited by sodium azide and fluoride. Dye solutions decolourized with the immobilized laccase were successfully used for redyeing.

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Section: Dye Decolourizationmentioning

confidence: 99%

An acid-stable laccase from Sclerotium rolfsii with potential for wool dye decolourization

Ryan

Schnitzhofer

Tzanov

et al. 2003

Enzyme and Microbial Technology

108

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“…Especially Phanerochaete chrysosporium has been the subject of intensive research related to degradation of a wide range of recalcitrant xenobiotic compounds and mineralising persistent aromatic pollutants (Chagas & Durrant 2001;Gao et al 2006;Yu et al 2006;Zhang et al 2008). Degradation capacity of P. chrysosporium on different synthetic dyes, such as azo, anthraquinone, heterocyclic triphenylmethane and polymeric, has also been showed in several researches (Peralta-Zamora et al 1999;Faraco et al 2009;Sharma et al 2009).…”

Section: Introductionmentioning

confidence: 98%

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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“…White rot fungi have been studied for their ability to degrade recalcitrant organo-pollutants such as polycyclic aromatic hydrocarbons (Bogan & Lamar, 1996), chlorinated phenols (Ruckenstein & Wang, 1994), PCBs (Sasek et al, 1993, Beaudette et al, 1998, dioxins (Takada et al, 1996), pesticides (Kullman & Matsumura, 1996), explosives (Gorontzy et al, 1994), dichloroaniline (Arjmand & Sandermann, 1985) and dyes (Kirby et al, 1995, Shin et al, 1997, Rodriguez et al, 1999. From the analysis of literature it is found that many authors used white rot fungi for decolorization of textile effluents (Chagas & Durrant, 2001 Though the number of studies on the biodegradation of dyestuffs have been steadily increasing in recent years, very few researches are reported for biodegradation of azo dyes, such as Cibacron Yellow S-3R using white rot fungi (Yesilada et al, 1998) and hence in this present research an attempt has been made to investigate the biological decolorization of the azo dye Cibacron Yellow S-3R using Coriolus Versicolor (MTCC 138).…”

Section: Introductionmentioning

confidence: 99%

Decolorization of Cibacron Yellow S-3R Using Coriolus Versicolor (MTCC 138)

Venkatachalam¹,

Venkatachalam²

2008

MAS

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The aim of the present study is to analyze the ability of the white rot fungi Coriolus Versicolor (MTCC 138) in the decolorization of Cibacron Yellow S-3R, a recalcitrant azo reactive textile dye. The influencing parameters that affect the percentage of decolorization rates are optimized in batch mode. The optimal values of the parameters such as mycelia age, temperature, pH, initial dye concentration and carbon source concentration are found to be 7 days, 30°C, 5.4, 100 mg/l and 2 mg/l respectively. The maximum percentage of decolorization at the optimized conditions is found to be 90%. It is also conferred that there is substrate inhibition to fungal decolorization when initial dye concentration is greater than 100 mg/l.

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Decolorization of azo dyes by Phanerochaete chrysosporium and Pleurotus sajorcaju

Cited by 163 publications

References 15 publications

An acid-stable laccase from Sclerotium rolfsii with potential for wool dye decolourization

An acid-stable laccase from Sclerotium rolfsii with potential for wool dye decolourization

Enzyme production by immobilized Phanerochaete chrysosporium using airlift reactor

Decolorization of Cibacron Yellow S-3R Using Coriolus Versicolor (MTCC 138)

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