Transformation of Industrial Dyes by Manganese Peroxidases from Bjerkandera adusta and Pleurotus eryngii in a Manganese-Independent Reaction

1998 ◽  
Vol 64 (8) ◽  
pp. 2788-2793 ◽  
Author(s):  
A. Heinfling ◽  
M. J. Martínez ◽  
A. T. Martínez ◽  
M. Bergbauer ◽  
U. Szewzyk
Keyword(s):  
White Rot Fungi ◽  
Veratryl Alcohol ◽  
Pleurotus Eryngii ◽  
White Rot ◽  
Reactive Black 5 ◽  
Bjerkandera Adusta ◽  
Independent Manner ◽  
Phthalocyanine Dyes ◽  
Specific Activities ◽  
Dye Oxidation

ABSTRACT We investigated the transformation of six industrial azo and phthalocyanine dyes by ligninolytic peroxidases from Bjerkandera adusta and other white rot fungi. The dyes were not oxidized or were oxidized very little by Phanerochaete chrysosporiummanganese peroxidase (MnP) or by a chemically generated Mn3+-lactate complex. Lignin peroxidase (LiP) from B. adusta also showed low activity with most of the dyes, but the specific activities increased 8- to 100-fold when veratryl alcohol was included in the reaction mixture, reaching levels of 3.9 to 9.6 U/mg. The B. adusta and Pleurotus eryngii MnP isoenzymes are unusual because of their ability to oxidize aromatic compounds like 2,6-dimethoxyphenol and veratryl alcohol in the absence of Mn2+. These MnP isoenzymes also decolorized the azo dyes and the phthalocyanine complexes in an Mn2+-independent manner. The reactions with the dyes were characterized by apparentKm values ranging from 4 to 16 μM and specific activities ranging from 3.2 to 10.9 U/mg. Dye oxidation by these peroxidases was not increased by adding veratryl alcohol as it was in LiP reactions. Moreover, the reaction was inhibited by the presence of Mn2+, which in the case of Reactive Black 5, an azo dye which is not oxidized by the Mn3+-lactate complex, was found to act as a noncompetitive inhibitor of dye oxidation byB. adusta MnP1.

scholarly journals Enhancing the Production of Hydroxyl Radicals by Pleurotus eryngii via Quinone Redox Cycling for Pollutant Removal

2009 ◽  
Vol 75 (12) ◽  
pp. 3954-3962 ◽  
Author(s):  
Víctor Gómez-Toribio ◽  
Ana B. García-Martín ◽  
María J. Martínez ◽  
Ángel T. Martínez ◽  
Francisco Guillén
Keyword(s):  
Fenton Reaction ◽  
White Rot Fungi ◽  
Fold Increase ◽  
Redox Cycling ◽  
Pleurotus Eryngii ◽  
Pollutant Removal ◽  
White Rot ◽  
Reactive Black 5 ◽  
Pollutant Degradation ◽  
Enhanced Production

ABSTRACT The induction of hydroxyl radical (OH) production via quinone redox cycling in white-rot fungi was investigated to improve pollutant degradation. In particular, we examined the influence of 4-methoxybenzaldehyde (anisaldehyde), Mn2+, and oxalate on Pleurotus eryngii OH generation. Our standard quinone redox cycling conditions combined mycelium from laccase-producing cultures with 2,6-dimethoxy-1,4-benzoquinone (DBQ) and Fe3+-EDTA. The main reactions involved in OH production under these conditions have been shown to be (i) DBQ reduction to hydroquinone (DBQH2) by cell-bound dehydrogenase activities; (ii) DBQH2 oxidation to semiquinone (DBQ−) by laccase; (iii) DBQ− autoxidation, catalyzed by Fe3+-EDTA, producing superoxide (O2 −) and Fe2+-EDTA; (iv) O2 − dismutation, generating H2O2; and (v) the Fenton reaction. Compared to standard quinone redox cycling conditions, OH production was increased 1.2- and 3.0-fold by the presence of anisaldehyde and Mn2+, respectively, and 3.1-fold by substituting Fe3+-EDTA with Fe3+-oxalate. A 6.3-fold increase was obtained by combining Mn2+ and Fe3+-oxalate. These increases were due to enhanced production of H2O2 via anisaldehyde redox cycling and O2 − reduction by Mn2+. They were also caused by the acceleration of the DBQ redox cycle as a consequence of DBQH2 oxidation by both Fe3+-oxalate and the Mn3+ generated during O2 − reduction. Finally, induction of OH production through quinone redox cycling enabled P. eryngii to oxidize phenol and the dye reactive black 5, obtaining a high correlation between the rates of OH production and pollutant oxidation.

scholarly journals Enhanced Production of Ligninolytic Enzymes by a Mushroom Stereum ostrea

2014 ◽  
Vol 2014 ◽  
pp. 1-9 ◽  
Author(s):  
K. Y. Usha ◽  
K. Praveen ◽  
B. Rajasekhar Reddy
Keyword(s):  
Solid State ◽  
Copper Sulphate ◽  
White Rot Fungi ◽  
Ligninolytic Enzymes ◽  
Tween 80 ◽  
Veratryl Alcohol ◽  
White Rot ◽  
Tween 20 ◽  
Laccase Production ◽  
Enhanced Production

The white rot fungi Stereum ostrea displayed a wide diversity in their response to supplemented inducers, surfactants, and copper sulphate in solid state fermentation. Among the inducers tested, 0.02% veratryl alcohol increased the ligninolytic enzyme production to a significant extent. The addition of copper sulphate at 300 μM concentration has a positive effect on laccase production increasing its activity by 2 times compared to control. Among the surfactants, Tween 20, Tween 80, and Triton X 100, tested in the studies, Tween 80 stimulated the production of ligninolytic enzymes. Biosorption of dyes was carried out by using two lignocellulosic wastes, rice bran and wheat bran, in 50 ppm of remazol brilliant blue and remazol brilliant violet 5R dyes. These dye adsorbed lignocelluloses were then utilized for the production of ligninolytic enzymes in solid state mode. The two dye adsorbed lignocelluloses enhanced the production of laccase and manganese peroxidase but not lignin peroxidase.

scholarly journals Use of Multiplex Reverse Transcription-PCR To Study the Expression of a Laccase Gene Family in a Basidiomycetous Fungus

2003 ◽  
Vol 69 (12) ◽  
pp. 7083-7090 ◽  
Author(s):  
Tania González ◽  
María C. Terrón ◽  
Ernesto J. Zapico ◽  
Alejandro Téllez ◽  
Susana Yagüe ◽  
...  
Keyword(s):  
Gene Expression ◽  
Reverse Transcription ◽  
White Rot Fungi ◽  
Gene Families ◽  
Veratryl Alcohol ◽  
White Rot ◽  
Laccase Gene ◽  
Reverse Transcription Pcr ◽  
Basidiomycetous Fungus ◽  
Laccase Genes

ABSTRACT Laccases produced by white rot fungi are involved in the degradation of lignin and a broad diversity of other natural and synthetic molecules, having a great potential for biotechnological applications. They are frequently encoded by gene families, as in the basidiomycete Trametes sp. strain I-62, from which the lcc1, lcc2, and lcc3 laccase genes have been cloned and sequenced. A multiplex reverse transcription-PCR method to simultaneously study the expression of these genes was developed in this study. The assay proved to be quick, simple, highly sensitive, and reproducible and is particularly valuable when numerous samples are to be analyzed and/or if the amount of initial mRNA is limited. It was used to analyze the effect of 3,4-dimethoxybenzyl alcohol (veratryl alcohol) and two of its isomers (2,5-dimethoxybenzyl alcohol and 3,5-dimethoxybenzyl alcohol) on differential laccase gene expression in Trametes sp. strain I-62. These aromatic compounds produced different induction patterns despite their chemical similarity. We found 2,5-dimethoxybenzyl alcohol to be the best inducer of laccase activity while also producing the highest increase in gene expression; 3,5-dimethoxybenzyl alcohol was the next best inducer. Transcript amounts of each gene fluctuated dramatically in the presence of these three inducers, while the total amounts of laccase mRNAs seemed to be modulated by a coordinated regulation of the different genes.

Kinetics of decolorization and mineralization of the azo dye Reactive Black 5 by hydrogen peroxide and UV light

2001 ◽  
Vol 44 (5) ◽  
pp. 295-301 ◽  
Author(s):  
A. Mohey El-Dein ◽  
J.A. Libra ◽  
U. Weismann
Keyword(s):  
Hydrogen Peroxide ◽  
Uv Light ◽  
Anaerobic Bacteria ◽  
White Rot Fungi ◽  
White Rot ◽  
Aerobic Biodegradation ◽  
Reactive Black 5 ◽  
Sulfate Reducing ◽  
Facultative Anaerobic Bacteria ◽  
Kinetics Of

C.I. Reactive Black 5 is one of the most used reactive dyes for textile finishing. It is a diazo dye, which can be decolorized by facultative anaerobic bacteria, sulfate reducing bacteria and aerobic white rot fungi. Mineralization by microorganisms has proven difficult. Advanced oxidation processes are promising alternatives for the decolorization and mineralization of Reactive Black 5, alone and in combination with aerobic biodegradation. The kinetics of the decolorization of Reactive Black 5 using a combination of hydrogen peroxide and UV radiation have been investigated. The rate of decolorization is first order with respect to dye concentration. It is enhanced with increasing hydrogen peroxide concentrations up to an optimum value. In our model we have correlated an empirical reaction rate expression which considers the contribution of both hydrogen peroxide and UV flux radiation based on the reaction kinetics. This empirical correlation agrees well with the experimental data for these conditions. Complete decolorization corresponded with 40-50% mineralization of the dye. Further mineralization can be achieved with extended radiation time.

scholarly journals 2-Chloro-1,4-Dimethoxybenzene as a Novel Catalytic Cofactor for Oxidation of Anisyl Alcohol by Lignin Peroxidase

1998 ◽  
Vol 64 (3) ◽  
pp. 830-835 ◽  
Author(s):  
Pauline J. M. Teunissen ◽  
Jim A. Field
Keyword(s):  
Lignin Peroxidase ◽  
Natural Compound ◽  
De Novo ◽  
White Rot Fungi ◽  
Veratryl Alcohol ◽  
White Rot ◽  
Molar Ratio ◽  
High Molar Ratio

ABSTRACT 2-Chloro-1,4-dimethoxybenzene (2Cl-14DMB) is a natural compound produced de novo by several white rot fungi. This chloroaromatic metabolite was identified as a cofactor superior to veratryl alcohol (VA) in the oxidation of anisyl alcohol (AA) by lignin peroxidase (LiP). Our results reveal that good LiP substrates, such as VA and tryptophan, are comparatively poor cofactors in the oxidation of AA. Furthermore, we show that a good cofactor does not necessarily serve a role in protecting LiP against H2O2inactivation. 2Cl-14DMB was not a direct mediator of AA oxidation, since increasing AA concentrations did not inhibit the oxidation of 2Cl-14DMB at all. However, the high molar ratio of anisaldehyde formed to 2Cl-14DMB consumed, up to 13:1, indicates that a mechanism which recycles the cofactor is present.

The role of peroxidases, radical cations and oxygen in the degradation of lignin

1987 ◽  
Vol 321 (1561) ◽  
pp. 495-505 ◽  
Keyword(s):  
Radical Cation ◽  
Active Oxygen Species ◽  
Bond Cleavage ◽  
White Rot Fungi ◽  
Radical Cations ◽  
Veratryl Alcohol ◽  
White Rot ◽  
Oxygen Species ◽  
Lignin Model

Ligninase is an extracellular peroxidase produced by several species of white-rot fungi. It is able to oxidize methoxylated substrates to radical cation intermediates that can undergo C—H or C—C bond cleavage, thereby providing the basis for the oxidation of veratryl alcohol or degradation of lignin model compounds respectively. In some cases, the radical cation intermediate can act as an oxidant, accepting an electron from a suitable donor. It can thus function as a mediator, causing oxidation in a polymer not immediately accessible to the enzyme. This could be important in the degradation of natural lignocellulose substrates. However, the removal of a single electron by a mediator would leave a radical in the polymer. We propose that oxygen will bind to this radical to generate active oxygen species. This provides a potential mechanism for the auto-oxidation of lignin at a distance from the enzyme. A scheme is presented to account for the observation that ligninase can open the ring of veratryl alcohol.

scholarly journals Oxygen Activation during Oxidation of Methoxyhydroquinones by Laccase from Pleurotus eryngii

2000 ◽  
Vol 66 (1) ◽  
pp. 170-175 ◽  
Author(s):  
Francisco Guillén ◽  
Carmen Muñoz ◽  
Víctor Gómez-Toribio ◽  
Angel T. Martínez ◽  
María Jesús Martínez
Keyword(s):  
Superoxide Anion ◽  
White Rot Fungi ◽  
Oxygen Activation ◽  
Pleurotus Eryngii ◽  
White Rot ◽  
Maximal Velocity ◽  
Reaction Conditions ◽  
Aromatic Radicals ◽  
Activation Of Oxygen ◽  
Superoxide Anion Radicals

ABSTRACT Oxygen activation during oxidation of the lignin-derived hydroquinones 2-methoxy-1,4-benzohydroquinone (MBQH2) and 2,6-dimethoxy-1,4-benzohydroquinone (DBQH2) by laccase fromPleurotus eryngii was examined. Laccase oxidized DBQH2 more efficiently than it oxidized MBQH2; both the affinity and maximal velocity of oxidation were higher for DBQH2 than for MBQH2. Autoxidation of the semiquinones produced by laccase led to the activation of oxygen, producing superoxide anion radicals (Q·− + O2 ↔ Q + O2 ·−). As this reaction is reversible, its existence was first noted in studies of the effect of systems consuming and producing O2 ·− on quinone formation rates. Then, the production of H2O2 in laccase reactions, as a consequence of O2 ·− dismutation, confirmed that semiquinones autoxidized. The highest H2O2levels were obtained with DBQH2, indicating that DBQ·− autoxidized to a greater extent than did MBQ·−. Besides undergoing autoxidation, semiquinones were found to be transformed into quinones via dismutation and laccase oxidation. Two ways of favoring semiquinone autoxidation over dismutation and laccase oxidation were increasing the rate of O2 ·− consumption with superoxide dismutase (SOD) and recycling of quinones with diaphorase (a reductase catalyzing the divalent reduction of quinones). These two strategies made the laccase reaction conditions more natural, since O2 ·−, besides undergoing dismutation, reacts with Mn2+, Fe3+, and aromatic radicals. In addition, quinones are continuously reduced by the mycelium of white-rot fungi. The presence of SOD in laccase reactions increased the extent of autoxidation of 100 μM concentrations of MBQ·− and DBQ·− from 4.5 to 30.6% and from 19.6 to 40.0%, respectively. With diaphorase, the extent of MBQ·− autoxidation rose to 13.8% and that of DBQ·− increased to 39.9%.

Microbial Decolorization of an Azo Dye Reactive Black 5 Using White-Rot Fungus Pleurotus eryngii F032

2013 ◽  
Vol 224 (6) ◽  
Author(s):  
Tony Hadibarata ◽  
Liyana Amalina Adnan ◽  
Abdull Rahim Mohd Yusoff ◽  
Adhi Yuniarto ◽  
Rubiyatno ◽  
...  
Keyword(s):  
Azo Dye ◽  
Pleurotus Eryngii ◽  
White Rot ◽  
White Rot Fungus ◽  
Reactive Black 5 ◽  
Microbial Decolorization
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