scholarly journals Decolourisation Capabilities of Ligninolytic Enzymes Produced byMarasmius cladophyllusUMAS MS8 on Remazol Brilliant Blue R and Other Azo Dyes

2017 ◽  
Vol 2017 ◽  
pp. 1-8 ◽  
Author(s):  
Ngieng Ngui Sing ◽  
Ahmad Husaini ◽  
Azham Zulkharnain ◽  
Hairul Azman Roslan
Keyword(s):  
Azo Dyes ◽  
Culture Medium ◽  
Laccase Activity ◽  
Dye Degradation ◽  
Ligninolytic Enzymes ◽  
Brilliant Blue ◽  
Remazol Brilliant Blue R ◽  
Orange G ◽  
Dye Decolourisation

Marasmius cladophylluswas examined for its ability to degradatively decolourise the recalcitrant dye Remazol Brilliant Blue R (RBBR) and screened for the production of ligninolytic enzymes using specific substrates. Monitoring dye decolourisation by the decrease in absorbance ratio ofA592/A500shows that the decolourisation of RBBR dye was associated with the dye degradation.Marasmius cladophyllusproduces laccase and lignin peroxidase in glucose minimal liquid medium containing RBBR. Both enzyme activities were increased, with laccase activity recorded 70 times higher reaching up to 390 U L−1on day 12. Further in vitro RBBR dye decolourisation using the culture medium shows that laccase activity was correlated with the dye decolourisation. Fresh RBBR dye continuously supplemented into the decolourised culture medium was further decolourised much faster in the subsequent round of the RBBR dye decolourisation. In vitro dye decolourisation using the crude laccase not only decolourised 76% of RBBR dye in just 19 hours but also decolourised 54% of Orange G and 33% of Congo red at the same period of time without the use of any exogenous mediator. This rapid dye decolourisation ability of the enzymes produced byM. cladophyllusthus suggested its possible application in the bioremediation of dye containing wastewater.

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

2009 ◽  
Vol 52 (5) ◽  
pp. 1075-1082 ◽  
Author(s):  
Sérgio Luiz Moreira Neto ◽  
Dácio Roberto Matheus ◽  
Kátia Maria Gomes Machado
Keyword(s):  
Culture Medium ◽  
Laccase Activity ◽  
Fungal Growth ◽  
Brilliant Blue ◽  
Enzymatic System ◽  
Industrial Residues ◽  
Optimum Ph ◽  
Influence Of Ph ◽  
Basidiomycete Fungi

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.

scholarly journals Optimization of Laccase from Ganoderma lucidum Decolorizing Remazol Brilliant Blue R and Glac1 as Main Laccase-Contributing Gene

Molecules ◽  
2019 ◽  
Vol 24 (21) ◽  
pp. 3914 ◽  
Author(s):  
Peng Qin ◽  
Yuetong Wu ◽  
Bilal Adil ◽  
Jie Wang ◽  
Yunfu Gu ◽  
...  
Keyword(s):  
Ganoderma Lucidum ◽  
Reactive Dye ◽  
White Rot ◽  
Brilliant Blue ◽  
White Rot Fungus ◽  
Protein Mass ◽  
Remazol Brilliant Blue R ◽  
Protein Mass Spectrometry ◽  
Laccase Enzyme

Many dyes and pigments are used in textile and printing industries, and their wastewater has been classed as a top source of pollution. Biodegradation of dyes by fungal laccase has great potential. In this work, the influence of reaction time, pH, temperature, dye concentration, metal ions, and mediators on laccase-catalyzed Remazol Brilliant Blue R dye (RBBR) decolorization were investigated in vitro using crude laccase from the white-rot fungus Ganoderma lucidum. The optimal decolorization percentage (50.3%) was achieved at 35 °C, pH 4.0, and 200 ppm RBBR in 30 min. The mediator effects from syringaldehyde, 1-hydroxybenzotriazole, and vanillin were compared, and 0.1 mM vanillin was found to obviously increase the decolorization percentage of RBBR to 98.7%. Laccase-mediated decolorization percentages significantly increased in the presence of 5 mM Na+ and Cu2+, and decolorization percentages reached 62.4% and 62.2%, respectively. Real-time fluorescence-quantitative PCR (RT-PCR) and protein mass spectrometry results showed that among the 15 laccase isoenzyme genes, Glac1 was the main laccase-contributing gene, contributing the most to the laccase enzyme activity and decolorization process. These results also indicate that under optimal conditions, G. lucidum laccases, especially Glac1, have a strong potential to remove RBBR from reactive dye effluent.

Decolorization of Orange G and Remazol Brilliant Blue R by the white rot fungus Dichomitus squalens: Toxicological evaluation and morphological study

Chemosphere ◽  
2007 ◽  
Vol 69 (5) ◽  
pp. 795-802 ◽  
Author(s):  
Ivana Eichlerová ◽  
Ladislav Homolka ◽  
Oldřich Benada ◽  
Olga Kofroňová ◽  
Tomáš Hubálek ◽  
...  
Keyword(s):  
Morphological Study ◽  
White Rot ◽  
Brilliant Blue ◽  
White Rot Fungus ◽  
Toxicological Evaluation ◽  
Remazol Brilliant Blue R ◽  
Dichomitus Squalens ◽  
Orange G

To the Mechanism of Horseradish Peroxidase-Mediated Degradation of a Recalcitrant Dye Remazol Brilliant Blue R

2001 ◽  
Vol 66 (4) ◽  
pp. 663-675 ◽  
Author(s):  
Markéta Mikšanová ◽  
Jiří Hudeček ◽  
Jan Páca ◽  
Marie Stiborová
Keyword(s):  
Molecular Weight ◽  
Horseradish Peroxidase ◽  
Oxidation Products ◽  
Brilliant Blue ◽  
Radical Mechanism ◽  
Remazol Brilliant Blue R ◽  
Radical Trapping ◽  
Optimum Ph ◽  
Mediated Oxidation

Thein vitroenzymatic metabolism of a recalcitrant dye Remazol Brilliant Blue R (RBBR) was investigated using horseradish peroxidase (HRP). At optimum pH (4.5), the apparent Michaelis constant (KM) value for the oxidation of RBBR catalyzed by HRP is 14.8 μmol l-1. HRP-mediated conversion of RBBR proceedsviaa conventional peroxidase reaction, by a sequential one-electron oxidation of two molecules of RBBR by the peroxidase Compounds I and II. The oxidation is inhibited by radical trapping agents (nicotinamide adenine dinucleotide reduced (NADH), ascorbate, glutathione). This confirms that the peroxidase-mediated oxidation of RBBR proceedsviaradical mechanism. Gel permeation profile of the RBBR oxidation products shows that the pattern of molecular weight distribution was shifted to the higher molecular weight region indicating formation of RBBR oligomers. In addition to HRP, the RBBR dye is also oxidized by another peroxidase, the mammalian lactoperoxidase.

scholarly journals Aktivitas ligninolitik Omphalina sp. hasil isolasi dari TKKS dan aplikasinya untuk dekolorisasi limbah kosmetik Ligninolytic activity of Omphalina sp. isolated from EFB and its application for decolorization of cosmetic waste

2016 ◽  
Vol 80 (2) ◽  
Author(s):  
. SUHARYANTO ◽  
Irma KRESNAWATY ◽  
Haryo Tejo PRAKOSO ◽  
Deden Dewantara ERIS
Keyword(s):  
White Rot Fungi ◽  
Ligninolytic Enzymes ◽  
White Rot ◽  
Brilliant Blue ◽  
Optimum Dose ◽  
Optimum Conditions ◽  
Ligninolytic Activity ◽  
Remazol Brilliant Blue R ◽  
Peroxidase Enzyme ◽  
Oxidation System

Abstract White-rot fungi (WRF) are belong to Basidiomycetes group that capable to degrade lignin, because they produce extracelullar ligninolytic enzymes such as lignin peroxsidase (Li-P), mangan peroxidase (Mn-P) and laccase. The ligninolytic activity can be used in bioprocess oxidation system such as biopulping, biobleaching and bioremediation.  The purposes of this research were to determine the optimum conditions of growth and ligni-nolytic activity of  Omphalina and to observe its potential to decolorize cosmetics wastewater.  Omphalina sp. was grown on media of PDA-Remazol Brilliant Blue R (RBBR) and PDA-Guaiacol (GU) at various pH and temperature conditions. The decolorization of cosmetic effluent was conducted by applying Omphalina sp. at various dose of inoculum.  Decolorization rate and change of COD were observed for eight days. The  results  showed that Ompha-lina sp. could grow and produce peroxidase enzyme both on RBBR and GU media at pH 4.5-8.5  and temperature 23-350C. Optimum dose of inoculum was as much as 5%  w/v at which the fungus was able to  decolorize cosmetic factory effluent up to 92.79% and to decrease COD value up to  48.57 % after eight days of incubation.Abstrak Jamur pelapuk putih (JPP) merupakan jamur kelompok Basidiomycetes yang mampu mendegradasi lignin karena memproduksi enzim-enzim ligninolitik ekstraseluler seperti lignin peroksidase (Li-P), mangan peroksidase (Mn-P) dan lakase.  Kemampuan ligninolitik JPP dapat dimanfaatkan dalam sistem oksidasi bioproses seperti biopulping, biobleaching dan bioremediasi. Pene-litian bertujuan menetapkan kondisi optimum pertumbuhan Omphalina sp. dan aktivitas ligninolitik yang dihasilkan-nya serta mempelajari potensinya dalam mendekolorisasi limbah cair kosmetik. Omphalina sp. ditumbuhkan dalam media PDA-Remazol Brilliant Blue R (RBBR) dan PDA-Guaiakol (GU)  pada  berbagai variasi pH dan suhu. Percobaan dekolorisasi limbah cair kosmetik dilakukan dengan aplikasi inokulum dalam berbagai dosis. Laju dekolorisasi dan perubahan COD diamati selama delapan hari. Hasil penelitian menunjukkan Omphalina sp. tumbuh dan menghasilkan enzim peroksidase, baik pada  media RBBR maupun GU pada pH 4,5-8,5 dan suhu 25-350C. Dosis optimum aplikasi Omphalina sp. adalah 5% (b/v) yang mampu mendekolorisasi limbah cair pabrik kosmetik hingga 92,79%  dan menurunkan COD 48,57% setelah delapan hari.

scholarly journals Coculture of white rot fungi enhance laccase activity and its dye decolorization capacity

2020 ◽  
Vol 9 (11) ◽  
pp. e88191110643
Author(s):  
Katielle Vieira Avelino ◽  
Marisangela Isabel Wietzikoski Halabura ◽  
Renan Alberto Marim ◽  
Nelma Lopes Araújo ◽  
Maria Graciela Iecher Faria Nunes ◽  
...  
Keyword(s):  
Biomass Production ◽  
Extracellular Enzymes ◽  
Laccase Activity ◽  
Dye Degradation ◽  
White Rot Fungi ◽  
White Rot ◽  
Mycelial Biomass ◽  
Pycnoporus Sanguineus ◽  
Biochemical Alterations

Fungal cocultures can promote complex interactions that result in physiological and biochemical alterations that favor the synergic and more efficient action of extracellular enzymes such as laccase. Thus, coculture can be used as a strategy to increase enzymatic activity, dye degradation, and bioremediation of textile effluents. This study aimed to evaluate the coculture effect of Lentinus crinitus, Pleurotus ostreatus, Pycnoporus sanguineus, and Trametes polyzona on laccase activity, mycelial biomass production, and in vitro decolorization of azo, anthraquinone, and triphenylmethane dyes. The species were cultivated in liquid medium in monoculture and coculture in paired combinations for 15 days to determine the laccase activity and produced mycelial biomass. The enzymatic extracts of fungal cultivations were used in decolorization tests of reactive blue 220 (RB220), malachite green (MG), and remazol brilliant blue R (RBBR). Pleurotus-Trametes, Lentinus-Pleurotus, and Lentinus-Trametes cocultures increase laccase activity compared to respective monocultures. Lentinus-Pycnoporus, Lentinus-Trametes, Lentinus-Pleurotus, and Pleurotus-Trametes cocultures stimulate mycelial biomass production in relation to their respective monocultures. The enzymatic extracts of monocultures and cocultures promoted the decolorization of all dyes. RB220 dye presented fast decolorization. In 24 h, all extracts reached maximum decolorization and the greatest color reduction percentage was 90% for Pleurotus-Trametes coculture extract. Pleurotus-Trametes extract also increased the decolorization of MG and RBBR dyes when compared to their respective monocultures in 48 h and 72 h, respectively. However, RBBR dye presented the greatest resistance to decolorization.

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