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 Onset of Lignin-Modifying Enzymes, Decrease of AOX and Color Removal by White-Rot Fungi Grown on Bleach Plant Effluents

1991 ◽  
Vol 24 (3-4) ◽  
pp. 189-198 ◽  
Author(s):  
V. P. Lankinen ◽  
M. M. Inkeröinen ◽  
J. Pellinen ◽  
A. I. Hatakka
Keyword(s):  
Lignin Peroxidase ◽  
Active Form ◽  
White Rot Fungi ◽  
Pulp Mill ◽  
Color Removal ◽  
Effluent Treatment ◽  
White Rot ◽  
White Rot Fungus ◽  
Lignin Peroxidases ◽  
Pulp Mill Effluents

Decrease of adsorbable organic chlorine (AOX) is becoming the most important criterion for the efficiency of pulp mill effluent treatment in the 1990s. Two methods, designated MYCOR and MYCOPOR which utilize the white-rot fungus Phanerochaete chrysosporium have earlier been developed for the color removal of pulp mill effluents, but the processes have also a capacity to decrease the amount of chlorinated organic compounds. Lignin peroxidases (ligninases) produced by P. chrvsosporium may dechlorinate chlorinated phenols. In this work possibilities to use selected white-rot fungi in the treatment of E1-stage bleach plant effluent were studied. Phlebia radiata. Phanerochaete chrvsosporium and Merulius (Phlebia) tremellosus were compared in shake flasks for their ability to produce laccase, lignin peroxidase(s) and manganese-dependent peroxidase(s) and to remove color from a medium containing effluent. Softwood bleaching effluents were treated by carrier-immobilized P. radiata in 2 1 bioreactors and a 10 1 BiostatR -fermentor. Dechlorination was followed using Cl ion and AOX determinations. All fungi removed the color of the effluent. In P. radiata cultivations AOX decrease was ca. 4 mg l−1 in one day. Apparent lignin peroxidase activities as determined by veratryl alcohol oxidation method were negligible or zero in a medium with AOX content of ca. 60 mg l−1, prepared using about 20 % (v/v) of softwood effluent. However, the purification of extracellular enzymes implied that large amounts of lignin peroxidases were present in the medium and, after the purification, in active form. Enzyme proteins were separated using anion exchange chromatography, and they were further characterized by electrophoresis (SDS-PAGE) to reveal the kind of enzymes that were present during AOX decrease and color removal. The most characteristic lignin peroxidase isoenzymes in effluent media were LiP2 and LiP3.

scholarly journals Identification of white rot fungus CP9 and its potential application in biopulping

2018 ◽  
Vol 14 (4) ◽  
pp. 721-726
Author(s):  
Nguyen Thi Hong Lien ◽  
Nguyen Van Hieu ◽  
Luong Thi Hong ◽  
Hy Tuan Anh ◽  
Phan Thi Hong Thao
Keyword(s):  
Rice Straw ◽  
Lignin Peroxidase ◽  
Paper Industry ◽  
Morphological Characteristics ◽  
White Rot Fungi ◽  
White Rot ◽  
White Rot Fungus ◽  
Wood Block ◽  
New Production ◽  
Cellulosic Fibers

Wood-rotting fungi represent an important component of forest ecosystems. Among them, white-rot fungi are the most efficient lignin degraders. Biopulping using white-rot fungi in pretreatment of the materials, is one of the solutions to overcome disadvantages of traditional production methods. Today, the isolation and screening of lignin degrading fungi capable for application in biopulping are of keen interest in Vietnam. The use of non–wood, plant fibres in pulp and paper industry, special, agricultural residuces such as rice and wheat straw, sugarcane baggase, cornstalks etc is the new production toward, potential, serving sustainable development. The fungus CP9, which possessed high ligninolytic activity, was identified and studied in pretreatment of rice straw for biopulping. The fruiting bodies of strain CP9 were effuse on trunk. The hymenium was porous and brown white with short tubes, the white mycelia penetrated wood block. The colony was off-white, blossom, irregularly circular. The mycelia were thick and closely bound together. Beside lignin, this fungus could degrade other substrates such as casein, carboxymethyl cellulose and starch. Biological and morphological characteristics of the fungus CP9 suggested its placement in subdivision Basidiomycota. Combined with the results of phylogenetic analysis, which showed 99% similarity of the fungus with species Leiotrametes lactinea, our strain was named as Leiotrametes lactinea CP9. This fungus could grow well on rice straw under solid state fermentation. Pretreatment of rice straw using L. lactinea CP9 was based on the activity of fungal lignin peroxidase and laccase. After 20 days, the residual enzyme activity was of 21.6 and 18.4 nkat/g material for lignin peroxidase and laccase, respectively. Pretreatment significantly improved the quality of straw, as lignin loss of 38% while cellulosic fibers were comparatively well preserved.

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 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.

scholarly journals The Influence of Inducers on the Coltricia cinnamomea Laccase Activity and its Ability to Degrade POME

2021 ◽  
Vol 13 (2) ◽  
pp. 243-249
Author(s):  
Yohanes Bernard Subowo ◽  
Arwan Sugiharto
Keyword(s):  
Palm Oil ◽  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Laccase Activity ◽  
Ligninolytic Enzymes ◽  
Veratryl Alcohol ◽  
White Rot ◽  
Growth Media ◽  
Palm Oil Mill ◽  
Low Activity

Some species of Basidiomycetes, specifically white rot groups, produce three ligninolytic enzymes, namely, Lignin Peroxidase (LiP), Manganese Peroxidase (MnP) and Laccase (Lac), which have low activity in degrading Palm Oil Mill Effluent (POME). The research objective was to obtain the data on the ability of the Coltricia cinnamomea to produce LiP, MnP, and Lac enzymes to degrade POME. This research also studied the effect of sucrose, alcohol, veratryl alcohol, CuSO4 and ZnSO4,as inducers. Isolates of Coltricia cinnamomea, which were stored in a PDA media at -20℃ were obtained from the Microbiology section of the Research Center for Biology (LIPI). Furthermore, the growth media used were DM, Bean sprout Extract (TE) and PDB. The result indicated that PDB is the most suitable growth media for the production of ligninolytic enzymes, because in this medium these enzymes showed the highest activity. It was also observed that sucrose increased the laccase activity by 40.80%. Furthermore, Coltricia cinnamomea was able to reduce the concentration of Poly R-478 by 60.74%, after the addition of ZnSO4. In addition, it degraded and decreased the color and COD of POME, by 72.63% and 91.19% respectively, after the addition of veratryl alcohol, and incubation for 10 days. Therefore, this fungus can be used to degrade POME in order to prevent environmental pollution. Coltricia cinnamomea has not been used for POME degradation. By using Coltricia cinnamomea, we  obtained new data regarding the activity of laccase and its ability to degrade POME. 

scholarly journals Screening for lignin peroxidase genes in natural isolates of white rot fungi

1992 ◽  
Vol 39 (1) ◽  
pp. 17-18
Author(s):  
V. Cifuentes ◽  
C. Martinez ◽  
G. Pincheira
Keyword(s):  
Lignin Peroxidase ◽  
White Rot Fungi ◽  
White Rot ◽  
Natural Isolates

scholarly journals Directed evolution of a temperature-, peroxide- and alkaline pH-tolerant versatile peroxidase

2011 ◽  
Vol 441 (1) ◽  
pp. 487-498 ◽  
Author(s):  
Eva Garcia-Ruiz ◽  
David Gonzalez-Perez ◽  
Francisco J. Ruiz-Dueñas ◽  
Angel T. Martínez ◽  
Miguel Alcalde
Keyword(s):  
Directed Evolution ◽  
Fusion Gene ◽  
White Rot Fungi ◽  
Catalytic Efficiency ◽  
Biochemical Properties ◽  
White Rot ◽  
Molar Ratio ◽  
Golgi Compartment ◽  
Enhanced Secretion ◽  
Natural Decay

The VPs (versatile peroxidases) secreted by white-rot fungi are involved in the natural decay of lignin. In the present study, a fusion gene containing the VP from Pleurotus eryngii was subjected to six rounds of directed evolution, achieving a level of secretion in Saccharomyces cerevisiae (21 mg/l) as yet unseen for any ligninolytic peroxidase. The evolved variant for expression harboured four mutations and increased its total VP activity 129-fold. The signal leader processing by the STE13 protease at the Golgi compartment changed as a consequence of overexpression, retaining the additional N-terminal sequence Glu-Ala-Glu-Ala that enhanced secretion. The engineered N-terminally truncated variant displayed similar biochemical properties to those of the non-truncated counterpart in terms of kinetics, stability and spectroscopic features. Additional cycles of evolution raised the T50 8°C and significantly increased the enzyme's stability at alkaline pHs. In addition, the Km for H2O2 was enhanced up to 15-fold while the catalytic efficiency was maintained, and there was an improvement in peroxide stability (with half-lives for H2O2 of 43 min at a H2O2/enzyme molar ratio of 4000:1). Overall, the directed evolution approach described provides a set of strategies for selecting VPs with improvements in secretion, activity and stability.

scholarly journals Lignin-degrading activity and ligninolytic enzymes of different white-rot fungi: effects of manganese and malonate

1997 ◽  
Vol 75 (1) ◽  
pp. 61-71 ◽  
Author(s):  
Tamara Vares ◽  
Annele Hatakka
Keyword(s):  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
White Rot Fungi ◽  
Ligninolytic Enzymes ◽  
Growth Conditions ◽  
Fungal Species ◽  
White Rot ◽  
Trametes Hirsuta ◽  
Air Atmosphere ◽  
Trametes Trogii

Ten species of white-rot fungi, mainly belonging to the family Polyporaceae (Basidiomycotina), were studied in terms of their ability to degrade14C-ring labelled synthetic lignin and secrete ligninolytic enzymes in liquid cultures under varying growth conditions. Lignin mineralization by the fungi in an air atmosphere did not exceed 14% within 29 days. Different responses to the elevated Mn2+concentration and the addition of a manganese chelator (sodium malonate) were observed among various fungal species. This could be related with the utilization of either lignin peroxidase (LiP) or manganese peroxidase (MnP) for lignin depolymerization, i.e., some fungi apparently had an LiP-dominating ligninolytic system and others an MnP-dominating ligninolytic system. The LiP isoforms were purified from Trametes gibbosa and Trametes trogii. Isoelectric focusing of purified ligninolytic enzymes revealed the expression of numerous MnP isoforms in Trametes gibbosa, Trametes hirsuta, Trametes trogii, and Abortiporus biennis grown under a high (50-fold) Mn2+level (120 μM) with the addition of the chelator. In addition, two to three laccase isoforms were detected. Key words: white-rot fungi, lignin degradation, lignin peroxidase, manganese peroxidase, manganese, malonate.

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