Bioremediation Potential of Mixed White Rot Culture of Pleurotus Ostreatus IBL-02 and Coriolus Versicolor IBL-04 for Textile Industry Wastewater

Asgher, Muhammad; Jamil, F.

doi:10.4172/2155-6199.s1-007

Cited by 14 publications

(12 citation statements)

References 43 publications

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“…WRF grown in synthetic textile dye solutions and industrial effluents take more time to decolorize dyes, compared to isolated enzymes, because of the necessary lag phase before they grow and secrete ligninolytic enzymes for dye degradation. Recently, in another effluent decolorization study, we have noted a significant time reduction and effluent colour loss (98.47%) in 48 h by the addition of MnSO 4 , followed by ABTS and varatryl alcohol as mediators for MnP, laccase and LiP respectively [8]. The variation in effluent composition is also responsible for variation in its decolorization by enzyme extracts from different fungi [15].…”

Section: Resultsmentioning

confidence: 99%

“…Over the past several years, there has been great interest among researchers in the production of ligninolytic- and cellulose-degrading enzymes from various agro-industrial waste materials and their by-products, such as wheat straw, rice husk, banana waste, citrus peel, rice straw, corncobs, corn stover, apple pomace, and sugar cane bagasse [1-8]. These wastes are not properly disposed off in developing countries and have become a major source of ecological pollution.…”

Section: Introductionmentioning

confidence: 99%

“…These wastes are not properly disposed off in developing countries and have become a major source of ecological pollution. Significant efforts have been made to convert lignocellulosic residues to valuable products such as bio-fuels, chemicals and animal feed with the help of ligninolytic enzymes of WRF, many of which have been successful [2,4-8]. To degrade all the components of lignocellulosic materials and phenolic organic substrates, white rot fungi (WRF) are so far exclusive in their strong oxidative capabilities due to their extracellular nonspecific enzyme system [3].…”

Section: Introductionmentioning

confidence: 99%

“…e ., extracellular peroxidases (manganese peroxidase, MnP; manganese independent peroxidase, MIP; lignin peroxidase, LiP; and versatile peroxidase, VP) and phenol oxidases (laccases). MnP and laccases have been applied frequently in various bio-technological processes such as lignocellulosic biomass delignification for ethanol production, oxidation of pollutants, bioremediation processes, textile bio-finishing, beverage processing, bio-bleaching of pulps and detergent manufacturing [1-3,6-8]. MnPs are heme-containing glycoproteins having capability to catalyze the oxidation of Mn 2+ to Mn 3+ .…”

Section: Introductionmentioning

confidence: 99%

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Decolorization applicability of sol–gel matrix immobilized manganese peroxidase produced from an indigenous white rot fungal strain Ganoderma lucidum

Iqbal

Asgher

2013

BMC Biotechnol

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BackgroundAn eco-friendly treatment of industrial effluents is a major environmental concern of the modern world in the face of stringent environmental legislations. By keeping in mind the extensive industrial applications of ligninolytic enzymes, this study was performed to purify, and immobilize the manganese peroxidase (MnP) produced from an indigenous strain of Ganoderma lucidum. The present study was also focused on investigating the capability of immobilized MnP for decolorization of dye containing textile effluents.ResultsA large magnitude of an indigenous MnP (882±13.3 U/mL) was obtained from white rot fungal strain G. lucidum in solid state bio-processing of wheat straw under optimized fermentation conditions (moisture, 50%; substrate, 5 g; pH, 5.5; temperature, 30°C; carbon source, 2% fructose; nitrogen source, 0.02% yeast extract; C: N ratio, 25:1; fungal spore suspension, 5 mL and fermentation time period, 4 days). After ammonium sulfate fractionation and Sephadex-G-100 gel filtration chromatography, MnP was 4.7-fold purified with specific activity of 892.9 U/mg. G. lucidum MnP was monomeric protein as evident by single band corresponding to 48 kDa on native and denaturing SDS-PAGE. The purified MnP (2 mg/mL) was immobilized using a sol–gel matrix of tetramethoxysilane (TMOS) and proplytrimethoxysilane (PTMS). The oxidation of MnSO4 for up to 10 uninterrupted cycles demonstrated the stability and reusability of the immobilized MnP. Shelf life profile revealed that enzyme may be stored for up to 60 days at 25°C without losing much of its activity. To explore the industrial applicability of MnP produced by G. lucidum, the immobilized MnP was tested against different textile effluents. After 4 h reaction time, the industrial effluents were decolorized to different extents (with a maximum of 99.2%). The maximally decolorized effluent was analyzed for formaldehyde and nitroamines and results showed that the toxicity parameters were below the permissible limits.ConclusionsIn conclusion, G. lucidum MnP was immobilized by sol–gel matrix entrapment with an objective to enhance its practical efficiencies. The MnP was successfully entrapped into a sol- gel matrix of TMOS and PTMS with an overall immobilization efficiency of 93.7%. The sol- gel entrapped MnP seems to have prospective capabilities which can be useful for industrial purposes, especially for bioremediation of industrial effluents.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Decolorization applicability of sol–gel matrix immobilized manganese peroxidase produced from an indigenous white rot fungal strain Ganoderma lucidum

Iqbal

Asgher

2013

BMC Biotechnol

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show abstract

“…[199] Endocrine Disrupters Laccase Cerrena unicolor [200] Textile effluent Laccase Pleurotus ostreatus IBL-02 and Coriolus versicolor [201] Dyes Peroxidase P.ostreatus [202] Olive [208] Methylene blue Mangenese peroxidase Phanerochaete chrysosporium [209] Versatile peroxidase and laccase Pleurotus ostreatus [210] coracryl brilliant blue, Ligninolytic enzymes Phanerochaete chrysosporium, Phlebia brevispora and Phlebia floridensis [211] graphene Lignin peroxidase White rot fungi [212] Sweet Sorghum Bagasse…”

Section: Compound Enzyme Organism Referencementioning

confidence: 99%