Decolourization and detoxification of monoazo dyes by laccase from the white-rot fungus Trametes versicolor

Legerská, Barbora; Chmelová, Daniela; Ondrejovič, Miroslav

doi:10.1016/j.jbiotec.2018.08.011

Cited by 63 publications

(27 citation statements)

References 40 publications

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“…The microbial growth of P. syringae, M. luteus, B. subtilis, E. coli and P. aeruginosa strains, using orange 2 dye treated with Trametes versicolor laccase, was increased higher than that without laccase added 49 . Also, Ashrafi et al 32 proved that the growth of M. luteus, S. aureus, B. subtilis, E. coli, P. aeruginosa and S. typhi strains was significantly increased in the presence of laccase-treated Direct Blue 71.…”

Section: Sulfa Drug and Dye Toxicity Studiesmentioning

confidence: 86%

Detoxification and Bioremediation of Sulfa Drugs and Synthetic Dyes by Streptomyces mutabilis A17 Laccase Produced in Solid State Fermentation

Reda¹,

El-Mekkawy²,

Hassan³

2019

J Pure Appl Microbiol

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Laccase enzyme has many important applications as bioremediation and removal of environmental wastes and also in industrial processes. Therefore, large-scale of novel producers of laccase is demanded to use cheap and low cost substrates. Hence, solid state fermentation is the best strategy to achieve this proposes. The present study is designed to optimize laccase production by Streptomyces mutabilis A17 using agro-wastes including rice bran, castor seed cake, wheat bran, wheat straw, soybeans cake, peanut cake, cotton seed cake and chicken feathers. Cotton seed cake significantly enhanced S. mutabilis A17 laccase production when it was incubated for 6 days at 37°C and 70% moisture content in presence of yeast extract and glucose as the best nitrogen and carbon sources, respectively. After purification steps, the purified laccase showed maximum activity at 40°C and pH 8.0 within stability pH range of 7.0 to 9.0. Laccase activity was highly increased to 195, 180 and 166% by the addition of Ba +2 , Cu +2 and Mn +2 , respectively. Sulfa drugs and synthetic dyes cause various pollutants due to their toxic effects in different environments. Therefore, a purified laccase was utilized for removal of sulfa drugs as sulfadiazine (SDZ) and sulfathiazole (STZ) and also synthetic dyes. The results showed that the maximal enzymatic removal of SDZ and STZ was attained at 50°C and pH 6.0 for 1 h at presence of 1mM HBT(1-hydroxybenzotriazole) as a laccase mediator by removal percentage of 73% and 90%, respectively. Detoxification effects of laccase-treated sulfa drugs and two synthetic dyes; congo red and malachite green solutions, were investigated using microbial toxicity test. Our results indicated that the toxicity of these laccase-treated samples against tested bacterial strains were significantly decreased. It was concluded from this study that SSF laccase is playing an important role for decreasing the toxic effects of pharmaceutical wastes and organic pollutants.

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Section: Sulfa Drug and Dye Toxicity Studiesmentioning

confidence: 86%

Detoxification and Bioremediation of Sulfa Drugs and Synthetic Dyes by Streptomyces mutabilis A17 Laccase Produced in Solid State Fermentation

Reda¹,

El-Mekkawy²,

Hassan³

2019

J Pure Appl Microbiol

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“…5 This enzyme catalyzes the oxidation of a wide number of phenolic compounds and aromatic amines but its substrate range have been extended to non-phenolic compounds in the presence of low molecular mass compounds acting as mediators. 6,7 Most of the studies have been carried out with laccases from eukaryotes, principally with enzymes secreted by basidiomycetes being their distribution in prokaryotes more recently. Different industrial purposes for fungal laccases have been insinuated and they include paper processing, inhibition of wine decolouration, detoxification of ecological pollutants, oxidation of dye and their precursors, enzymatic translation of chemical intermediates, and production of chemicals from lignin.…”

Section: Among Othersmentioning

confidence: 99%

Pleurotus ostreatus Laccase Decolorization of Remazol Brilliant Violet 5R Dye: Statistical Optimization and Toxicity Studies on Microbes and its Kinetics

Valliyaparambil

Kaliyaperumal

Narendrakumar

2019

J Apple Biotechnol Rep

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Introduction: Nowadays, enzyme-based removal of hazardous dyes that pollute the environment has been considered as a substitute and ecofriendly method compared to the physical and chemical method. The present study was conceived in order to obtain the optimal condition for laccase-mediated (purified from the Pleurotus ostreatus PKN04) decolorization of Remazol Brilliant Violet 5R dye; a mono-azo dye, using the central composite design of response surface methodology (RSM). Materials and Methods: The design of experiment was suggested with 6 variables including pH, temperature, incubation time, agitation, dye concentration, and enzyme concentration, which were applied in order to optimize the decolorization process. The kinetic and energetic factors of laccases for the enzymatic removal of Remazol Brilliant Violet 5R dye was investigated. Results: Decolorization of Remazol Brilliant Violet 5R was maximally 95.72%, which had occurred at 6.0 pH, 40°C temperature, 60 minutes incubation time, 50 rpm agitation, 50 ppm dye concentration, and 100 IU/mL enzyme concentration. The obtained results of kinetic introduced the laccase-catalyzed decolorization of Remazol Brilliant Violet 5R as an endothermic reaction with K m and V max values of 0.801 mM and 387 mM/ mg/min, respectively. In addition to the above results, the toxicity study against bacteria revealed that the toxicity of laccase-treated dye drastically reduced to the untreated dye. Conclusions:The results of the present analysis reveal that the Pleurotus ostreatus laccase is an efficient biocatalyst for decolorization of synthetic dye Remazol Brilliant Violet 5R dye. Citation: Valliyaparambil PT, Kaliyaperumal KA, Gopakumaran N. Pleurotus ostreatus laccase decolorization of Remazol Brilliant Violet 5R dye: statistical optimization and toxicity studies on microbes and its kinetics. J Appl Biotechnol Rep. 2019;6(3):88-95.

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“…They have the catalytic ability to oxidize a wide range of aromatic substrates with a concomitant reduction of dioxygen to water (Zhang et al., 2012). Globally, fungal laccase have better pH/or temperature stability, higher metal tolerance, and are able to oxidize a wider range of substrates from different origin (Legerska, Chmelova, & Ondrejovic, 2018). The use of laccases may result in rapid and significant recalcitrant substrate degradation (Ruiz‐Duenas & Martinez, 2009).…”

Section: Introductionmentioning

confidence: 99%

Molecular docking studies and in vitro degradation of four aflatoxins (AFB₁, AFB₂, AFG₁, and AFG₂) by a recombinant laccase from Saccharomyces cerevisiae

Liu

Mao

et al. 2020

Journal of Food Science

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Here, molecular docking simulation was used to predict and compare interactions between a recombinant Trametes sp. C30 laccase from Saccharomyces cerevisiae and four aflatoxins (AFB 1 , AFB 2 , AFG 1 , and AFG 2 ) as well as their degradation at a molecular level. The computational result of docking simulation indicates that each of the aflatoxins tested can interact with laccase with a binding ability of AFB 1 >AFG 2 >AFG 1 >AFB 2 . Simultaneously, it also demonstrated that aflatoxin B 1 , B 2 , G 1 , G 2 may interact near the T1 copper center of the enzyme through H-bonds and hydrophobic interactions with amino acid residues His481 and Asn288; His481; Asn288, and Asp230; His481 and Asn288. Biological degradation test was performed in vitro in the presence of a recombinant laccase. Degradation increased as incubation time increased from 12 to 60 hr and the maximum degradation obtained for AFB 1 , AFB 2 , AFG 1 , and AFG 2 was 90.33%, 74.23%, 85.24%, and 87.58%, respectively. Maximum degradation of aflatoxins was determined with a total activity 3 U laccase at 30°C in 0.1 M phosphate buffer, pH 5.7 after 48-hr incubation. The experimental results are consistent with that of docking calculation on the biological degradation test of four aflatoxins by laccase.Practical Application: In this study, the degradation efficiencies of laccase for B and G series of aflatoxins were determined by computer simulation and verified by performing in vitro experiments. It can provide reference for rapid screening of aflatoxin degradation-related enzymes.

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Decolourization and detoxification of monoazo dyes by laccase from the white-rot fungus Trametes versicolor

Cited by 63 publications

References 40 publications

Detoxification and Bioremediation of Sulfa Drugs and Synthetic Dyes by Streptomyces mutabilis A17 Laccase Produced in Solid State Fermentation

Detoxification and Bioremediation of Sulfa Drugs and Synthetic Dyes by Streptomyces mutabilis A17 Laccase Produced in Solid State Fermentation

Pleurotus ostreatus Laccase Decolorization of Remazol Brilliant Violet 5R Dye: Statistical Optimization and Toxicity Studies on Microbes and its Kinetics

Molecular docking studies and in vitro degradation of four aflatoxins (AFB₁, AFB₂, AFG₁, and AFG₂) by a recombinant laccase from Saccharomyces cerevisiae

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Decolourization and detoxification of monoazo dyes by laccase from the white-rot fungus Trametes versicolor

Cited by 63 publications

References 40 publications

Detoxification and Bioremediation of Sulfa Drugs and Synthetic Dyes by Streptomyces mutabilis A17 Laccase Produced in Solid State Fermentation

Detoxification and Bioremediation of Sulfa Drugs and Synthetic Dyes by Streptomyces mutabilis A17 Laccase Produced in Solid State Fermentation

Pleurotus ostreatus Laccase Decolorization of Remazol Brilliant Violet 5R Dye: Statistical Optimization and Toxicity Studies on Microbes and its Kinetics

Molecular docking studies and in vitro degradation of four aflatoxins (AFB1, AFB2, AFG1, and AFG2) by a recombinant laccase from Saccharomyces cerevisiae

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Product

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Molecular docking studies and in vitro degradation of four aflatoxins (AFB₁, AFB₂, AFG₁, and AFG₂) by a recombinant laccase from Saccharomyces cerevisiae