scholarly journals A Search for Ligninolytic Peroxidases in the FungusPleurotus eryngii Involving α-Keto-γ-Thiomethylbutyric Acid and Lignin Model Dimers

1999 ◽  
Vol 65 (3) ◽  
pp. 916-922 ◽  
Author(s):  
Lucília Caramelo ◽  
María Jesús Martínez ◽  
Ángel T. Martínez
Keyword(s):  
Liquid Culture ◽  
Catalytic Properties ◽  
Ligninolytic Enzymes ◽  
Veratryl Alcohol ◽  
Pleurotus Eryngii ◽  
Extracellular Proteins ◽  
Terminal Sequence ◽  
The Third ◽  
Lignin Model ◽  
Structural Aspects

ABSTRACT Because there is some controversy concerning the ligninolytic enzymes produced by Pleurotus species, ethylene release from α-keto-γ-thiomethylbutyric acid (KTBA), as described previously for Phanerochaete chrysosporium lignin peroxidase (LiP), was used to assess the oxidative power ofPleurotus eryngii cultures and extracellular proteins. Lignin model dimers were used to confirm the ligninolytic capabilities of enzymes isolated from liquid and solid-state fermentation (SSF) cultures. Three proteins that oxidized KTBA in the presence of veratryl alcohol and H2O2 were identified (two proteins were found in liquid cultures, and one protein was found in SSF cultures). These proteins are versatile peroxidases that act on Mn2+, as well as on simple phenols and veratryl alcohol. The two peroxidases obtained from the liquid culture were able to degrade a nonphenolic β-O-4 dimer, yielding veratraldehyde, as well as a phenolic dimer which is not efficiently oxidized by P. chrysosporium peroxidases. The former reaction is characteristic of LiP. The third KTBA-oxidizing peroxidase oxidized only the phenolic dimer (in the presence of Mn2+). Finally, a fourth Mn2+-oxidizing peroxidase was identified in the SSF cultures on the basis of its ability to oxidize KTBA in the presence of Mn2+. This enzyme is related to the Mn-dependent peroxidase of P. chrysosporium because it did not exhibit activity with veratryl alcohol and Mn-independent activity with dimers. These results show that P. eryngii produces three types of peroxidases that have the ability to oxidize lignin but lacks a typical LiP. Similar enzymes (in terms of N-terminal sequence and catalytic properties) are produced by other Pleurotus species. Some structural aspects of P. eryngii peroxidases related to the catalytic properties are discussed.

scholarly journals Efficient Degradation of Zearalenone by Dye-Decolorizing Peroxidase from Streptomyces thermocarboxydus Combining Catalytic Properties of Manganese Peroxidase and Laccase

Toxins ◽  
2021 ◽  
Vol 13 (9) ◽  
pp. 602
Author(s):  
Xing Qin ◽  
Yanzhe Xin ◽  
Xiaoyun Su ◽  
Xiaolu Wang ◽  
Yaru Wang ◽  
...  
Keyword(s):  
Manganese Peroxidase ◽  
Catalytic Properties ◽  
Degradation Products ◽  
Ligninolytic Enzymes ◽  
Veratryl Alcohol ◽  
Degradation Pathway ◽  
Promising Candidate ◽  
Anthraquinone Dye ◽  
Food And Feed ◽  
Encoding Gene

Ligninolytic enzymes, including laccase, manganese peroxidase, and dye-decolorizing peroxidase (DyP), have attracted much attention in the degradation of mycotoxins. Among these enzymes, the possible degradation pathway of mycotoxins catalyzed by DyP is not yet clear. Herein, a DyP-encoding gene, StDyP, from Streptomyces thermocarboxydus 41291 was identified, cloned, and expressed in Escherichia coli BL21/pG-Tf2. The recombinant StDyP was capable of catalyzing the oxidation of the peroxidase substrate 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), phenolic lignin compounds 2,6-dimethylphenol, and guaiacol, non-phenolic lignin compound veratryl alcohol, Mn2+, as well as anthraquinone dye reactive blue 19. Moreover, StDyP was able to slightly degrade zearalenone (ZEN). Most importantly, we found that StDyP combined the catalytic properties of manganese peroxidase and laccase, and could significantly accelerate the enzymatic degradation of ZEN in the presence of their corresponding substrates Mn2+ and 1-hydroxybenzotriazole. Furthermore, the biological toxicities of the main degradation products 15-OH-ZEN and 13-OH-ZEN-quinone might be remarkably removed. These findings suggested that DyP might be a promising candidate for the efficient degradation of mycotoxins in food and feed.

scholarly journals Comparing Ligninolytic Capabilities of Bacterial and Fungal Dye-Decolorizing Peroxidases and Class-II Peroxidase-Catalases

2021 ◽  
Vol 22 (5) ◽  
pp. 2629
Author(s):  
Dolores Linde ◽  
Iván Ayuso-Fernández ◽  
Marcos Laloux ◽  
José E. Aguiar-Cervera ◽  
Antonio L. de Lacey ◽  
...  
Keyword(s):  
Veratryl Alcohol ◽  
Flow Measurements ◽  
Reduction Potentials ◽  
Rate Limiting Step ◽  
Lower Extent ◽  
Lignin Model ◽  
Bacteria And Fungi ◽  
Compound Ii ◽  
Rate Limiting ◽  
Lignin Macromolecule

We aim to clarify the ligninolytic capabilities of dye-decolorizing peroxidases (DyPs) from bacteria and fungi, compared to fungal lignin peroxidase (LiP) and versatile peroxidase (VP). With this purpose, DyPs from Amycolatopsis sp., Thermomonospora curvata, and Auricularia auricula-judae, VP from Pleurotus eryngii, and LiP from Phanerochaete chrysosporium were produced, and their kinetic constants and reduction potentials determined. Sharp differences were found in the oxidation of nonphenolic simple (veratryl alcohol, VA) and dimeric (veratrylglycerol-β- guaiacyl ether, VGE) lignin model compounds, with LiP showing the highest catalytic efficiencies (around 15 and 200 s−1·mM−1 for VGE and VA, respectively), while the efficiency of the A. auricula-judae DyP was 1–3 orders of magnitude lower, and no activity was detected with the bacterial DyPs. VP and LiP also showed the highest reduction potential (1.28–1.33 V) in the rate-limiting step of the catalytic cycle (i.e., compound-II reduction to resting enzyme), estimated by stopped-flow measurements at the equilibrium, while the T. curvata DyP showed the lowest value (1.23 V). We conclude that, when using realistic enzyme doses, only fungal LiP and VP, and in much lower extent fungal DyP, oxidize nonphenolic aromatics and, therefore, have the capability to act on the main moiety of the native lignin macromolecule.

Synthesis and application of Co(salen) complexes containing proximal imidazolium ionic liquid cores

2012 ◽  
Vol 90 (1) ◽  
pp. 60-70 ◽  
Author(s):  
Swapnil Sonar ◽  
Kenson Ambrose ◽  
Arthur D. Hendsbee ◽  
Jason D. Masuda ◽  
Robert D. Singer
Keyword(s):  
Ionic Liquid ◽  
Ionic Liquids ◽  
Model Compound ◽  
Veratryl Alcohol ◽  
Oxidation Catalysts ◽  
Imidazolium Ionic Liquid ◽  
Lignin Model Compound ◽  
Salen Complexes ◽  
Lignin Model ◽  
Salen Ligand

Ionic ligands derived from a salen ligand containing two proximal 1,3-disubstituted imidazolium ionic liquid cores form cobalt(III) complexes capable of selectively oxidizing veratryl alcohol, a lignin model compound, to veratraldehyde using air as the source of oxygen. These complexes are easy to prepare, inexpensive, water stable, and soluble in ionic liquids, making them viable candidates for use as oxidation catalysts.

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.

Enhanced Production of Ligninolytic Enzymes by Ganoderma lucidum IBL-06 Using Lignocellulosic Agricultural Wastes

2010 ◽  
Vol 8 (1) ◽  
Author(s):  
Muhammad Asgher ◽  
Yasir Sharif ◽  
H.N. Bhatti
Keyword(s):  
Rice Straw ◽  
Lignin Peroxidase ◽  
Ganoderma Lucidum ◽  
Ligninolytic Enzymes ◽  
Tween 80 ◽  
Veratryl Alcohol ◽  
Inoculum Size ◽  
Enhanced Production ◽  
Lignocellulosic Substrates ◽  
Ssf Process

An indigenous novel strain of Ganoderma lucidum IBL-06 was investigated for the production of ligninolytic enzymes including lignin peroxidase (LiP), manganese peroxidase (MnP) and laccase using different lignocellulosic substrates in still culture solid-state fermentation (SSF). The fermentation flasks were inoculated and incubated at 35°C for 14 days. Samples were harvested after every 48 h to study the profile of ligninolytic enzymes produced by the fungus on different substrates. Maximum enzyme activities were noted on 10th day of incubation on rice straw. Ganoderma lucidum IBL-06 produced highest activities of lignin peroxidase (LiP) among the lignolytic enzymes. By optimizing the SSF process, maximum activities of LiP (2185 IU/ml), MnP (1972 IU/ml) and laccase (338 IU/ml) were achieved after three days incubation of rice straw at pH 4.5; temperature, 35°C; moisture, 75% and inoculum size, 6 ml, using fructose as carbon source, urea as nitrogen source, Tween-80 as surfactant and veratryl alcohol as mediator.

scholarly journals Effects of Different Substrates on Lignocellulosic Enzyme Expression, Enzyme Activity, Substrate Utilization and Biological Efficiency of Pleurotus Eryngii

2016 ◽  
Vol 39 (4) ◽  
pp. 1479-1494 ◽  
Author(s):  
Chunliang Xie ◽  
Li Yan ◽  
Wenbing Gong ◽  
Zuohua Zhu ◽  
Senwei Tan ◽  
...  
Keyword(s):  
Expression Profiles ◽  
Carbon Sources ◽  
Pleurotus Eryngii ◽  
Extracellular Proteins ◽  
Biological Efficiency ◽  
Biomass Degradation ◽  
Lignocellulosic Substrates ◽  
Proteomic Approach ◽  
Lignocellulosic Enzymes ◽  
Lignin Depolymerization

Background/Aims: Pleurotus eryngii is one of the most valued and delicious mushrooms which are commercially cultivated on various agro-wastes. How different substrates affect lignocellulosic biomass degradation, lignocellulosic enzyme production and biological efficiency in Pleurotus eryngii was unclear. Methods and Results: In this report, Pleurotus eryngii was cultivated in substrates including ramie stalks, kenaf stalks, cottonseed hulls and bulrush stalks. The results showed that ramie stalks and kenaf stalks were found to best suitable to cultivate Pleurotus eryngii with the biological efficiency achieved at 55% and 57%, respectively. In order to establish correlations between different substrates and lignocellulosic enzymes expression, the extracellular proteins from four substrates were profiled with high throughput TMT-based quantitative proteomic approach. 241 non-redundant proteins were identified and 74 high confidence lignocellulosic enzymes were quantified. Most of the cellulases, hemicellulases and lignin depolymerization enzymes were highly up-regulated when ramie stalks and kenaf stalks were used as carbon sources. The enzyme activities results suggested cellulases, hemicellulases and lignin depolymerization enzymes were significantly induced by ramie stalks and kenaf stalks. Conclusion: The lignocelluloses degradation, most of the lignocellulosic enzymes expressions and activities of Pleurotus eryngii had positive correlation with the biological efficiency, which depend on the nature of lignocellulosic substrates. In addition, the lignocellulosic enzymes expression profiles during Pleurotus eryngii growth in different substrates were obtained. The present study suggested that most of the lignocellulosic enzymes expressions and activities can be used as tools for selecting better performing substrates for commercial mushroom cultivation.

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