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Journal articles on the topic 'Laccase substrates'

Author: Grafiati
Published: 4 June 2021
Last updated: 11 February 2022

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1

Mohit, Elham, Maryam Tabarzad, and Mohammad Ali Faramarzi. "Biomedical and Pharmaceutical-Related Applications of Laccases." Current Protein & Peptide Science 21, no. 1 (2020): 78–98. http://dx.doi.org/10.2174/1389203720666191011105624.

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The oxidation of a vast range of phenolic and non-phenolic substrates has been catalyzed by laccases. Given a wide range of substrates, laccases can be applied in different biotechnological applications. The present review was conducted to provide a broad context in pharmaceutical- and biomedical- related applications of laccases for academic and industrial researchers. First, an overview of biological roles of laccases was presented. Furthermore, laccase-mediated strategies for imparting antimicrobial and antioxidant properties to different surfaces were discussed. In this review, laccase-med
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2

Wang, Feng, Ling Xu, Liting Zhao, Zhongyang Ding, Haile Ma, and Norman Terry. "Fungal Laccase Production from Lignocellulosic Agricultural Wastes by Solid-State Fermentation: A Review." Microorganisms 7, no. 12 (2019): 665. http://dx.doi.org/10.3390/microorganisms7120665.

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Laccases are copper-containing oxidase enzymes found in many fungi. They have received increasing research attention because of their broad substrate specificity and applicability in industrial processes, such as pulp delignification, textile bleaching, phenolic removal, and biosensors. In comparison with traditional submerged fermentation (SF), solid-state fermentation (SSF) is a simpler technique for laccase production and has many advantages, including higher productivity, efficiency, and enzyme stability as well as reduced production costs and environmental pollution. Here, we review recen
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3

Mander, Gerd J., Huaming Wang, Elizabeth Bodie, et al. "Use of Laccase as a Novel, Versatile Reporter System in Filamentous Fungi." Applied and Environmental Microbiology 72, no. 7 (2006): 5020–26. http://dx.doi.org/10.1128/aem.00060-06.

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ABSTRACT Laccases are copper-containing enzymes which oxidize phenolic substrates and transfer the electrons to oxygen. Many filamentous fungi contain several laccase-encoding genes, but their biological roles are mostly not well understood. The main interest in laccases in biotechnology is their potential to be used to detoxify phenolic substances. We report here on a novel application of laccases as a reporter system in fungi. We purified a laccase enzyme from the ligno-cellulolytic ascomycete Stachybotrys chartarum. It oxidized the artificial substrate 2,2′-azino-di-(3-ethylbenzthiazolinsul
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4

Zhang, Ying Long, Hai Bo Zhang, You Shuang Zhu, Ming Le Cao, Ming Qiang Ai, and Feng Huang. "Influences of Organic Compounds on Laccase Activity Tests." Applied Mechanics and Materials 416-417 (September 2013): 1702–7. http://dx.doi.org/10.4028/www.scientific.net/amm.416-417.1702.

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Organic compounds oxalic acid and ethylenediaminetetraacetic acid disodium salt-2-hydrate (EDTA Na2) were described as laccase inhibitors by forming complex compounds with the metal ions of the laccase. Their influence on laccase from Trametes hirsuta lg-9 and Rhus vernificera in different test systems utilizing 2, 2-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) and 2, 6-dimethoxyphenol (DMP) as enzyme substrates were tested. Our study indicated that oxalic acid can influence the laccase activity determination mainly by changing the pH of the reaction system. The influences of both
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5

Trubitsina, Liubov Igorevna, Azat Vadimovich Abdullatypov, Anna Petrovna Larionova, et al. "Expression of thermophilic two-domain laccase from Catenuloplanes japonicus in Escherichia coli and its activity against triarylmethane and azo dyes." PeerJ 9 (June 24, 2021): e11646. http://dx.doi.org/10.7717/peerj.11646.

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Background Two-domain laccases are copper-containing oxidases found in bacteria in the beginning of 2000ths. Two-domain laccases are known for their thermal stability, wide substrate specificity and, the most important of all, their resistance to so-called «strong inhibitors» of classical fungal laccases (azides, fluorides). Low redox potential was found to be specific for all the two-domain laccases, due to which these enzymes lost the researchers’ interest as potentially applicable for various biotechnological purposes, such as bioremediation. Searching, obtaining and studying the properties
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6

Contato, Alex Graça, Fabíola Dorneles In´ácio, Tatiane Brugnari, et al. "Solid-state fermentation with orange waste: optimization of Laccase production from Pleurotus pulmonarius CCB-20 and decolorization of synthetic dyes." Acta Scientiarum. Biological Sciences 42 (May 19, 2020): e52699. http://dx.doi.org/10.4025/actascibiolsci.v42i1.52699.

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Laccases are oxidoreductase enzymes that have the ability to oxidize phenolic substrates. Its biotechnological potential has been greatly explored in many areas as biotechnology industry, bioremediation of dyes, food industry and environmental microbiology. The aim of this study was maximize the laccase production by Pleurotus pulmonarius (Fr.) Quélet in solid-state fermentation (SSF) using orange waste as substrate. After optimization the capability of the crude laccase to decolorize dyes was analyzed. The fermentation medium in the solid-state was optimized by applying a factorial design. Af
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7

Aza, Pablo, Gonzalo Molpeceres, Francisco Javier Ruiz-Dueñas, and Susana Camarero. "Heterologous Expression, Engineering and Characterization of a Novel Laccase of Agrocybe pediades with Promising Properties as Biocatalyst." Journal of Fungi 7, no. 5 (2021): 359. http://dx.doi.org/10.3390/jof7050359.

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Agaricomycetes fungi responsible for decay of wood and other lignocellulosic substrates constitute a valuable source of lignin-degrading enzymes. Among these enzymes, laccases (multi-copper oxidases) present remarkable biotechnological potential as environmentally friendly biocatalysts able to oxidize a wide range of aromatic compounds using oxygen as the only requirement. Laccases from saprotrophic Agaricales species have been much less studied than laccases from Polyporales, despite the fact that the former fungi are excellent sources of laccases. Here, the gene of a novel laccase of Agrocyb
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8

More, Sunil S., Renuka P. S., Pruthvi K., Swetha M., S. Malini, and Veena S. M. "Isolation, Purification, and Characterization of Fungal Laccase from Pleurotus sp." Enzyme Research 2011 (September 29, 2011): 1–7. http://dx.doi.org/10.4061/2011/248735.

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Laccases are blue copper oxidases (E.C. 1.10.3.2 benzenediol: oxygen oxidoreductase) that catalyze the one-electron oxidation of phenolics, aromatic amines, and other electron-rich substrates with the concomitant reduction of O2 to H2O. They are currently seen as highly interesting industrial enzymes because of their broad substrate specificity. A positive strain was isolated and characterized as nonspore forming Basidiomycetes Pleurotus sp. Laccase activity was determined using ABTS as substrate. Laccase was purified by ionexchange and gel filtration chromatography. The purified laccase was a
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9

Glazunova, Olga, Nikita Trushkin, Konstantin Moiseenko, Ivan Filimonov, and Tatyana Fedorova. "Catalytic Efficiency of Basidiomycete Laccases: Redox Potential versus Substrate-Binding Pocket Structure." Catalysts 8, no. 4 (2018): 152. http://dx.doi.org/10.3390/catal8040152.

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Laccases are copper-containing oxidases that catalyze a one-electron abstraction from various phenolic and non-phenolic compounds with concomitant reduction of molecular oxygen to water. It is well-known that laccases from various sources have different substrate specificities, but it is not completely clear what exactly provides these differences. The purpose of this work was to study the features of the substrate specificity of four laccases from basidiomycete fungi Trametes hirsuta, Coriolopsis caperata, Antrodiella faginea, and Steccherinum murashkinskyi, which have different redox potenti
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10

Rodakiewicz-Nowak, J., J. Haber, N. Pozdnyakova, A. Leontievsky, and L. A. Golovleva. "Effect of Ethanol on Enzymatic Activity of Fungal Laccases." Bioscience Reports 19, no. 6 (1999): 589–600. http://dx.doi.org/10.1023/a:1020223130115.

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Blue laccase from Coriolus versicolor and blue and yellow laccases from Panus tigrinus were isolated, purified and studied in acetate buffer solutions, with and without addition of various amounts of ethanol, using syringaldazine and 2,6-dimethoxyphenol as substrates. Effect of ethanol on blue laccases could be successfully described using the mixed inhibition model, over the range of 0–2.5 M ethanol concentrations. Yellow laccase from P. tigrinus behaves differently, which may be explained by the presence of some extra molecules in its structure, which possibly stabilize the enzyme and might
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11

Milovanovic, Jelena, Miyase Gözde Gündüz, Anastasia Zerva, et al. "Synthesis and Laccase-Mediated Oxidation of New Condensed 1,4-Dihydropyridine Derivatives." Catalysts 11, no. 6 (2021): 727. http://dx.doi.org/10.3390/catal11060727.

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We describe herein the synthesis and laccase mediated oxidation of six novel 1,4-dihydropyridine (DHP)-based hexahydroquinolines (DHP1-DHP3) and decahydroacridines (DHP4-DHP6). We employed different laccase enzymes with varying redox potential to convert DHP1-DHP3 and DHP4-DHP6 to the corresponding pyridine-containing tetrahydroquinoline and octahydroacridine derivatives, respectively. Intensively coloured products were detected in all biocatalytic reactions using laccase from Trametes versicolor (TvLacc), possibly due to the presence of conjugated chromophores formed in products after oxidati
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12

Glazunova, Olga A., Konstantin M. Polyakov, Tatyana V. Fedorova, Pavel V. Dorovatovskii, and Olga V. Koroleva. "Elucidation of the crystal structure ofCoriolopsis caperatalaccase: restoration of the structure and activity of the native enzyme from the T2-depleted form by copper ions." Acta Crystallographica Section D Biological Crystallography 71, no. 4 (2015): 854–61. http://dx.doi.org/10.1107/s1399004715001595.

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Laccases are members of a large family of multicopper oxidases that catalyze the oxidation of a wide range of organic and inorganic substrates accompanied by the reduction of dioxygen to water. A new laccase was isolated from the basidiomyceteCoriolopsis caperatastrain 0677 and its amino-acid sequence was determined. According to its physicochemical properties and spectroscopic features, the laccase fromC. caperatais a high redox-potential blue laccase. Attempts to crystallize the native enzyme were unsuccessful. The copper type 2-depleted (T2D) laccase was prepared and crystallized. The struc
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13

Du, Dong Xia, Shi Ping Shan, De Yuan Zhang, and Yue Lin He. "Homology Modeling of Aeromonas hydrophila Laccase and its Molecular Docking with the 2,5-Xylidine." Advanced Materials Research 798-799 (September 2013): 83–86. http://dx.doi.org/10.4028/www.scientific.net/amr.798-799.83.

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Laccases belonging to multicopper oxidase family oxidize a broad range of reducing substrates, especially industrial effluents-derived polyphenols, which causing major effect on human health as well as environment. In order to investigate the molecular mechanism of interaction between laccase and its substrate, it is a good idea to analyze three-dimensional structure of laccase. Based on crystal structure ofEscherichia colilaccase CueO, the three-dimensional structure ofAeromonas hydrophilaLaccase (Ah-lac) was constructed by homology modeling and further evaluated using PROSA energy and ERRAT.
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14

Legerská, Barbora, Daniela Chmelová, and Miroslav Ondrejovič. "Degradation of Synthetic Dyes by Laccases – A Mini-Review." Nova Biotechnologica et Chimica 15, no. 1 (2016): 90–106. http://dx.doi.org/10.1515/nbec-2016-0010.

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Abstract Laccases provide a promising future as a tool to be used in the field of biodegradation of synthetic dyes with different chemical structures. These enzymes are able to oxidize a wide range of phenolic substrates without the presence of additional co-factors. Laccases have been confirmed for their potential of synthetic dye degradation from wastewater and degradation products of these enzymatic reactions become less toxic than selected dyes. This study discusses the potential of laccase enzymes as agents for laccase-catalyzed degradation in terms of biodegradation efficiency of synthet
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15

Tetianec, Lidija, and Juozas Kulys. "Kinetics of N-substituted phenothiazines and N-substituted phenoxazines oxidation catalyzed by fungal laccases." Open Life Sciences 4, no. 1 (2009): 62–67. http://dx.doi.org/10.2478/s11535-008-0050-5.

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AbstractLaccase-catalyzed oxidation of N-substituted phenothiazines and N-substituted phenoxazines was investigated at pH 5.5 and 25°C. The recombinant laccase from Polyporus pinsitus (rPpL) and the laccase from Myceliophthora thermophila (rMtL) were used. The dependence of initial reaction rate on substrate concentration was analyzed by applying the laccase action scheme in which the laccase native intermediate (NI) reacts with a substrate forming reduced enzyme. The reduced laccase produces peroxide intermediate (PI) which in turn decays to the NI. The calculated constant (kox) values of the
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16

Sousa, Ana Catarina, Lígia O. Martins, and M. Paula Robalo. "Laccases: Versatile Biocatalysts for the Synthesis of Heterocyclic Cores." Molecules 26, no. 12 (2021): 3719. http://dx.doi.org/10.3390/molecules26123719.

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Laccases are multicopper oxidases that have shown a great potential in various biotechnological and green chemistry processes mainly due to their high relative non-specific oxidation of phenols, arylamines and some inorganic metals, and their high redox potentials that can span from 500 to 800 mV vs. SHE. Other advantages of laccases include the use of readily available oxygen as a second substrate, the formation of water as a side-product and no requirement for cofactors. Importantly, addition of low-molecular-weight redox mediators that act as electron shuttles, promoting the oxidation of co
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17

Muthukumarasamy, Narayanan P., Beenie Jackson, Antony Joseph Raj, and Murugan Sevanan. "Production of Extracellular Laccase fromBacillus subtilisMTCC 2414 Using Agroresidues as a Potential Substrate." Biochemistry Research International 2015 (2015): 1–9. http://dx.doi.org/10.1155/2015/765190.

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Laccases are the model enzymes for multicopper oxidases and participate in several applications such as bioremediation, biopulping, textile, and food industries. Laccase producing bacterium,Bacillus subtilisMTCC 2414, was subjected to optimization by conventional techniques and was partially purified using ammonium salt precipitation method. The agroresidue substrates used for higher yield of laccase were rice bran and wheat bran. Maximum production was achieved at temperature 30°C (270 ± 2.78 U/mL), pH 7.0 (345 ± 3.14 U/mL), and 96 h (267 ± 2.64 U/mL) of incubation. The carbon and nitrogen so
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18

Jamwal, Shivani, Dharamender Kumar, Sunita Ranote, and Ghanshyam S. Chauhan. "New Nanoaggregates of Crosslinked Laccase for Reactive Red Bioremediation." Journal of Nanoscience and Nanotechnology 19, no. 11 (2019): 7205–14. http://dx.doi.org/10.1166/jnn.2019.16667.

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Environmental concerns have led to an increased interest in developing green technologies for bioremediation of wastewater pollutants. In view of this, laccases have emerged as attractive green catalysts due to their applicability in oxidizing broad range of substrates. In the present work laccase was extracted from Coriolus versicolor (MTCC 138) and stabilized by formation of new crosslinked laccase nanoaggregates (CLNAs) using two different crosslinkers-N,N-methylenebisacrylamide (N, N-MBAAm) and ethyleneglycol dimethacrylate (EGDMA). Evaluation of laccase activity profile of the free as wel
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19

Mehra, Rukmankesh, and Kasper P. Kepp. "Contribution of substrate reorganization energies of electron transfer to laccase activity." Physical Chemistry Chemical Physics 21, no. 28 (2019): 15805–14. http://dx.doi.org/10.1039/c9cp01012b.

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20

Rangelov and Nicell. "Laccase-Catalyzed Oxidation of Mixed Aqueous Phenolic Substrates at Low Concentrations." Catalysts 9, no. 4 (2019): 368. http://dx.doi.org/10.3390/catal9040368.

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It has been proposed that Trametes versicolor laccase can be used to detoxify wastewaters that are contaminated with phenolic pollutants. However, the oxidation of phenols at low concentrations may be impacted if other substrates tend to interfere with or enhance the oxidation of the target substrate. To test this, experiments were conducted to evaluate effects arising from the simultaneous presence of mixed substrates including phenol (P), estradiol (E2), cumylphenol (CP), and triclosan (TCL), each of which are characterized by different rates of oxidation and tendencies to inactivate laccase
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21

Zhao, J., and H. S. Kwan. "Characterization, Molecular Cloning, and Differential Expression Analysis of Laccase Genes from the Edible MushroomLentinula edodes." Applied and Environmental Microbiology 65, no. 11 (1999): 4908–13. http://dx.doi.org/10.1128/aem.65.11.4908-4913.1999.

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ABSTRACT The effect of different substrates and various developmental stages (mycelium growth, primordium appearance, and fruiting-body formation) on laccase production in the edible mushroom Lentinula edodes was studied. The cap of the mature mushroom showed the highest laccase activity, and laccase activity was not stimulated by some well-known laccase inducers or sawdust. For our molecular studies, two genomic DNA sequences, representing allelic variants of theL. edodes lac1 gene, were isolated, and DNA sequence analysis demonstrated that lac1 encodes a putative polypeptide of 526 amino aci
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22

Polyakov, Konstantin M., Sergei Gavryushov, Tatiana V. Fedorova, Olga A. Glazunova, and Alexander N. Popov. "The subatomic resolution study of laccase inhibition by chloride and fluoride anions using single-crystal serial crystallography: insights into the enzymatic reaction mechanism." Acta Crystallographica Section D Structural Biology 75, no. 9 (2019): 804–16. http://dx.doi.org/10.1107/s2059798319010684.

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Laccases are enzymes that catalyze the oxidation of a wide range of organic and inorganic substrates accompanied by the reduction of molecular oxygen to water. Here, a subatomic resolution X-ray crystallographic study of the mechanism of inhibition of the laccase from the basidiomycete fungus Steccherinum murashkinskyi by chloride and fluoride ions is presented. Three series of X-ray diffraction data sets were collected with increasing doses of absorbed X-ray radiation from a native S. murashkinskyi laccase crystal and from crystals of complexes of the laccase with chloride and fluoride ions.
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23

Larrondo, Luis F., Loreto Salas, Francisco Melo, Rafael Vicuña, and Daniel Cullen. "A Novel Extracellular Multicopper Oxidase from Phanerochaete chrysosporium with Ferroxidase Activity." Applied and Environmental Microbiology 69, no. 10 (2003): 6257–63. http://dx.doi.org/10.1128/aem.69.10.6257-6263.2003.

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ABSTRACT Lignin degradation by the white rot basidiomycete Phanerochaete chrysosporium involves various extracellular oxidative enzymes, including lignin peroxidase, manganese peroxidase, and a peroxide-generating enzyme, glyoxal oxidase. Recent studies have suggested that laccases also may be produced by this fungus, but these conclusions have been controversial. We identified four sequences related to laccases and ferroxidases (Fet3) in a search of the publicly available P. chrysosporium database. One gene, designated mco1, has a typical eukaryotic secretion signal and is transcribed in defi
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Polyakov, K. M., S. Gavryushov, S. Ivanova, et al. "Structural study of the X-ray-induced enzymatic reduction of molecular oxygen to water bySteccherinum murashkinskyilaccase: insights into the reaction mechanism." Acta Crystallographica Section D Structural Biology 73, no. 5 (2017): 388–401. http://dx.doi.org/10.1107/s2059798317003667.

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The laccase fromSteccherinum murashkinskyiis a member of the large family of multicopper oxidases that catalyze the oxidation of a wide range of organic and inorganic substrates, accompanied by the reduction of dioxygen to water. The reducing properties of X-ray radiation and the high quality of the laccase crystals allow the study of the catalytic reduction of dioxygen to water directly in a crystal. A series of diffraction data sets with increasing absorbed radiation dose were collected from a single crystal ofSteccherinum murashkinskyilaccase at 1.35 Å resolution. Changes in the active-site
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25

Gáspár, Szilveszter, Elena Brinduse, and Alina Vasilescu. "Electrochemical Evaluation of Laccase Activity in Must." Chemosensors 8, no. 4 (2020): 126. http://dx.doi.org/10.3390/chemosensors8040126.

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As laccase (produced by Botrytis cinerea) can significantly alter the properties of wine, winemakers frequently use commercially available colorimetric kits and spectrophotometers to measure the activity of this enzyme in grapes, must and wine. Although the used kits are based on electrochemically active substrates (such as syringaldazine and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), ABTS), the electrochemical determination of laccase activity as an alternative to the colorimetric determination was not thoroughly investigated up to now. Therefore, in the present work, we explored
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26

Bassanini, Ivan, Erica Elisa Ferrandi, Sergio Riva, and Daniela Monti. "Biocatalysis with Laccases: An Updated Overview." Catalysts 11, no. 1 (2020): 26. http://dx.doi.org/10.3390/catal11010026.

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Laccases are multicopper oxidases, which have been widely investigated in recent decades thanks to their ability to oxidize organic substrates to the corresponding radicals while producing water at the expense of molecular oxygen. Besides their successful (bio)technological applications, for example, in textile, petrochemical, and detoxifications/bioremediations industrial processes, their synthetic potentialities for the mild and green preparation or selective modification of fine chemicals are of outstanding value in biocatalyzed organic synthesis. Accordingly, this review is focused on repo
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27

Kim, Seonghun. "Mushroom Ligninolytic Enzymes―Features and Application of Potential Enzymes for Conversion of Lignin into Bio-Based Chemicals and Materials." Applied Sciences 11, no. 13 (2021): 6161. http://dx.doi.org/10.3390/app11136161.

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Mushroom ligninolytic enzymes are attractive biocatalysts that can degrade lignin through oxido-reduction. Laccase, lignin peroxidase, manganese peroxidase, and versatile peroxidase are the main enzymes that depolymerize highly complex lignin structures containing aromatic or aliphatic moieties and oxidize the subunits of monolignol associated with oxidizing agents. Among these enzymes, mushroom laccases are secreted glycoproteins, belonging to a polyphenol oxidase family, which have a powerful oxidizing capability that catalyzes the modification of lignin using synthetic or natural mediators
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Wang, Xiaolu, Bin Yao, and Xiaoyun Su. "Linking Enzymatic Oxidative Degradation of Lignin to Organics Detoxification." International Journal of Molecular Sciences 19, no. 11 (2018): 3373. http://dx.doi.org/10.3390/ijms19113373.

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The major enzymes involved in lignin degradation are laccase, class II peroxidases (lignin peroxidase, manganese peroxidase, and versatile peroxidase) and dye peroxidase, which use an oxidative or peroxidative mechanism to deconstruct the complex and recalcitrant lignin. Laccase and manganese peroxidase directly oxidize phenolic lignin components, while lignin peroxidase and versatile peroxidase can act on the more recalcitrant non-phenolic lignin compounds. Mediators or co-oxidants not only increase the catalytic ability of these enzymes, but also largely expand their substrate scope to those
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29

Viswanath, Buddolla, Bandi Rajesh, Avilala Janardhan, Arthala Praveen Kumar, and Golla Narasimha. "Fungal Laccases and Their Applications in Bioremediation." Enzyme Research 2014 (May 15, 2014): 1–21. http://dx.doi.org/10.1155/2014/163242.

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Laccases are blue multicopper oxidases, which catalyze the monoelectronic oxidation of a broad spectrum of substrates, for example, ortho- and para-diphenols, polyphenols, aminophenols, and aromatic or aliphatic amines, coupled with a full, four-electron reduction of O2 to H2O. Hence, they are capable of degrading lignin and are present abundantly in many white-rot fungi. Laccases decolorize and detoxify the industrial effluents and help in wastewater treatment. They act on both phenolic and nonphenolic lignin-related compounds as well as highly recalcitrant environmental pollutants, and they
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30

Sun, Jian, Qing-Jun Chen, Qing-Qin Cao, et al. "A Laccase with Antiproliferative and HIV-I Reverse Transcriptase Inhibitory Activities from the Mycorrhizal FungusAgaricus placomyces." Journal of Biomedicine and Biotechnology 2012 (2012): 1–8. http://dx.doi.org/10.1155/2012/736472.

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A novel 68 kDa laccase was purified from the mycorrhizal fungusAgaricus placomycesby utilizing a procedure that comprised three successive steps of ion exchange chromatography and gel filtration as the final step. The monomeric enzyme exhibited the N-terminal amino acid sequence of DVIGPQAQVTLANQD, which showed only a low extent of homology to sequences of other fungal laccases. The optimal temperature forA. placomyceslaccase was 30°C, and optimal pH values for laccase activity towards the substrates 2,7′-azinobis[3-ethylbenzothiazolone-6-sulfonic acid] diammonium salt (ABTS) and hydroquinone
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31

Morón, Carlos, Alfonso Garcia, Enrique Tremps, and Jose Andrés Somolinos. "Building Functional Surfaces for Biosensors Development." Key Engineering Materials 543 (March 2013): 204–7. http://dx.doi.org/10.4028/www.scientific.net/kem.543.204.

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Polyelectrolyte multilayers (PEM) built by layer-by-layer technique have been extensively studied over the last years, resulting in a wide variety of current and potential applications. This technique can be used to construct thin films with different functionalities, or to functionalize surfaces with substantial different properties of those of the underlying substrates. The multilayering process is achieved by the alternate adsorption of oppositely charged polyelectrolytes. In this work we get advantage of the protein resistant property of the Poly (l-lysine)-graft-(polyethyleneglycol) to cr
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Shraddha, Ravi Shekher, Simran Sehgal, Mohit Kamthania, and Ajay Kumar. "Laccase: Microbial Sources, Production, Purification, and Potential Biotechnological Applications." Enzyme Research 2011 (June 21, 2011): 1–11. http://dx.doi.org/10.4061/2011/217861.

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Laccase belongs to the blue multicopper oxidases and participates in cross-linking of monomers, degradation of polymers, and ring cleavage of aromatic compounds. It is widely distributed in higher plants and fungi. It is present in Ascomycetes, Deuteromycetes and Basidiomycetes and abundant in lignin-degrading white-rot fungi. It is also used in the synthesis of organic substance, where typical substrates are amines and phenols, the reaction products are dimers and oligomers derived from the coupling of reactive radical intermediates. In the recent years, these enzymes have gained application
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33

Lund, M., M. Eriksson, and C. Felby. "Reactivity of a Fungal Laccase Towards Lignin in Softwood Kraft Pulp." Holzforschung 57, no. 1 (2003): 21–26. http://dx.doi.org/10.1515/hf.2003.004.

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SummaryThe reactivity of a fungal laccase to lignin of six different spruce kraft pulps with kappa numbers ranging from 15 to 110 was studied. Enzymatic oxidation of lignin was investigated by monitoring the oxygen consumption in a suspension of the pulp and the number of radicals generated in the pulp, as measured by electron paramagnetic resonance spectroscopy. The laccase catalyzed oxidation of lignin in kraft pulp followed a double exponential function. This indicates the presence of two types of substrates oxidized by the enzyme at different rates. The two substrates were interpreted as l
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34

Yadav, Mukesh, Garima Bista, Rocky Maharjan, et al. "Secretory Laccase from Pestalotiopsis Species CDBT-F-G1 Fungal Strain Isolated from High Altitude: Optimization of Its Production and Characterization." Applied Sciences 9, no. 2 (2019): 340. http://dx.doi.org/10.3390/app9020340.

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Microorganisms producing laccases may be used for the pretreatment of lignocellulosic biomass to recover fermentable sugar. Very few fungi and other microbes growing in high altitudes have been tested for this purpose. As part of this study, we have collected soil samples from different parts of the Kathmandu Valley and the Rautah at district of Nepal (1600 to 2303 m above sea level) and successfully cultured 53 different isolates of microorganisms. Among the 53 isolates obtained 30 were Actinomycetes, 20 were Streptomycetes, and three were fungi). These isolates were tested for laccase expres
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35

Kersten, P. J., B. Kalyanaraman, K. E. Hammel, B. Reinhammar, and T. K. Kirk. "Comparison of lignin peroxidase, horseradish peroxidase and laccase in the oxidation of methoxybenzenes." Biochemical Journal 268, no. 2 (1990): 475–80. http://dx.doi.org/10.1042/bj2680475.

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Lignin peroxidase oxidizes non-phenolic substrates by one electron to give aryl-cation-radical intermediates, which react further to give a variety of products. The present study investigated the possibility that other peroxidative and oxidative enzymes known to catalyse one-electron oxidations may also oxidize non-phenolics to cation-radical intermediates and that this ability is related to the redox potential of the substrate. Lignin peroxidase from the fungus Phanerochaete chrysosporium, horseradish peroxidase (HRP) and laccase from the fungus Trametes versicolor were chosen for investigati
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36

Reena, Purnima Dhall, Rita Kumar, and Anil Kumar. "Validation of computationally predicted substrates for laccase." Brazilian Archives of Biology and Technology 57, no. 5 (2014): 803–9. http://dx.doi.org/10.1590/s1516-8913201402239.

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37

Lonergan, G., and W. L. Baker. "Comparative study of substrates of fungal laccase." Letters in Applied Microbiology 21, no. 1 (1995): 31–33. http://dx.doi.org/10.1111/j.1472-765x.1995.tb01000.x.

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38

Braunschmid, Verena, Sarah Fuerst, Veronika Perz, et al. "A Fungal Ascorbate Oxidase with Unexpected Laccase Activity." International Journal of Molecular Sciences 21, no. 16 (2020): 5754. http://dx.doi.org/10.3390/ijms21165754.

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Ascorbate oxidases are an enzyme group that has not been explored to a large extent. So far, mainly ascorbate oxidases from plants and only a few from fungi have been described. Although ascorbate oxidases belong to the well-studied enzyme family of multi-copper oxidases, their function is still unclear. In this study, Af_AO1, an enzyme from the fungus Aspergillus flavus, was characterized. Sequence analyses and copper content determination demonstrated Af_AO1 to belong to the multi-copper oxidase family. Biochemical characterization and 3D-modeling revealed a similarity to ascorbate oxidases,
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39

Yuan, Mengli, Qiang Wang, Jinsong Shen, Edward Smith, Rubing Bai, and Xuerong Fan. "Enzymatic coloration and finishing of wool with laccase and polyethylenimine." Textile Research Journal 88, no. 16 (2017): 1834–46. http://dx.doi.org/10.1177/0040517517712096.

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Enzymes have been widely used in textile wet processing. The precise reaction specificity of an enzyme has been utilized for specific or targeted textile finishing without causing undesirable fiber damage. Laccases are important enzymes for application in textile processing due to their great versatility and capability of catalyzing the oxidation of a broad range of substrates. The investigation of laccase-catalyzed coloration towards either wool or polyethylenimine was carried out. It is understood that amino groups from wool and polyethylenimine are involved in the formation of polymeric col
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40

Gelo-Pujic, Mirjana, Hyug-Han Kim, Nathan G. Butlin, and G. Tayhas R. Palmore. "Electrochemical Studies of a Truncated Laccase Produced in Pichia pastoris." Applied and Environmental Microbiology 65, no. 12 (1999): 5515–21. http://dx.doi.org/10.1128/aem.65.12.5515-5521.1999.

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ABSTRACT The cDNA that encodes an isoform of laccase from Trametes versicolor (LCCI), as well as a truncated version (LCCIa), was subcloned and expressed by using the yeast Pichia pastorisas the heterologous host. The amino acid sequence of LCCIa is identical to that of LCCI except that the final 11 amino acids at the C terminus of LCCI are replaced with a single cysteine residue. This modification was introduced for the purpose of improving the kinetics of electron transfer between an electrode and the copper-containing active site of laccase. The two laccases (LCCI and LCCIa) are compared in
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41

Camarero, S., I. Pardo, A. I. Cañas, et al. "Engineering Platforms for Directed Evolution of Laccase from Pycnoporus cinnabarinus." Applied and Environmental Microbiology 78, no. 5 (2011): 1370–84. http://dx.doi.org/10.1128/aem.07530-11.

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ABSTRACTWhile thePycnoporus cinnabarinuslaccase (PcL) is one of the most promising high-redox-potential enzymes for environmental biocatalysis, its practical use has to date remained limited due to the lack of directed evolution platforms with which to improve its features. Here, we describe the construction of a PcL fusion gene and the optimization of conditions to induce its functional expression inSaccharomyces cerevisiae, facilitating its directed evolution and semirational engineering. The native PcL signal peptide was replaced by the α-factor preproleader, and this construct was subjecte
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42

Pickard, Michael A., Rosa Roman, Raunel Tinoco, and Rafael Vazquez-Duhalt. "Polycyclic Aromatic Hydrocarbon Metabolism by White Rot Fungi and Oxidation by Coriolopsis gallica UAMH 8260 Laccase." Applied and Environmental Microbiology 65, no. 9 (1999): 3805–9. http://dx.doi.org/10.1128/aem.65.9.3805-3809.1999.

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ABSTRACT We studied the metabolism of polycyclic aromatic hydrocarbons (PAHs) by using white rot fungi previously identified as organisms that metabolize polychlorinated biphenyls. Bran flakes medium, which has been shown to support production of high levels of laccase and manganese peroxidase, was used as the growth medium. Ten fungi grown for 5 days in this medium in the presence of anthracene, pyrene, or phenanthrene, each at a concentration of 5 μg/ml could metabolize these PAHs. We studied the oxidation of 10 PAHs by using laccase purified from Coriolopsis gallica. The reaction mixtures c
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43

Solano, Francisco, Patricia Lucas-Elío, Eva Fernández, and Antonio Sanchez-Amat. "Marinomonas mediterranea MMB-1 Transposon Mutagenesis: Isolation of a Multipotent Polyphenol Oxidase Mutant." Journal of Bacteriology 182, no. 13 (2000): 3754–60. http://dx.doi.org/10.1128/jb.182.13.3754-3760.2000.

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ABSTRACT Marinomonas mediterranea is a melanogenic marine bacterium expressing a multifunctional polyphenol oxidase (PPO) able to oxidize substrates characteristic for laccases and tyrosinases, as well as produce a classical tyrosinase. A new and quick method has been developed for screening laccase activity in culture plates to detect mutants differentially affected in this PPO activity. Transposon mutagenesis has been applied for the first time to M. mediterranea by using different minitransposons loaded in R6K-based suicide delivery vectors mobilizable by conjugation. Higher frequencies of
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44

Polak, Jolanta, Kamila Wlizło, Rebecca Pogni, et al. "Structure and Bioactive Properties of Novel Textile Dyes Synthesised by Fungal Laccase." International Journal of Molecular Sciences 21, no. 6 (2020): 2052. http://dx.doi.org/10.3390/ijms21062052.

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Novel sustainable processes involving oxidative enzymatic catalysts are considered as an alternative for classical organic chemistry. The unique physicochemical and bioactive properties of novel bio-products can be obtained using fungal laccase as catalyst. Among them are textile biodyes synthesised during oxidation of substrates belonging to the amine and methoxy organic derivatives. The process of synthesis occurs in mild conditions of pH, temperature, and pressure, and without using harmful oxidants. The effect of fungal laccase activity on the substrates mixture transformation efficiency w
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45

Lonergan, Greg, Elizabeth Mew, Kirsten Schliephake, and Warren L. Baker. "Phenolic substrates for fluorometric detection of laccase activity." FEMS Microbiology Letters 153, no. 2 (2006): 485–90. http://dx.doi.org/10.1111/j.1574-6968.1997.tb12614.x.

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46

Gramss, Gerhard, and Klaus-Dieter Voigt. "Basidiospores from Wood-Decay Fungi Transform Laccase Substrates in the Absence of Glucose and Nitrogen Supplements." Journal of Fungi 6, no. 2 (2020): 62. http://dx.doi.org/10.3390/jof6020062.

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Preparations of bacterial endospores and fungal conidia are applied in biocontrols, biocatalyses, and lignocellulose fermentations. The biocatalytic abilities of basidiospores from mushrooms of the order Agaricales are unknown. To assess their potential in colonizing recalcitrant substrates solely with their inherent resources, spores of the white-rot fungi Stropharia rugoso-annulata (Stru) and Kuehneromyces mutabilis (Kmt, Strophariaceae) were analyzed for surface-bound and internal total carbohydrates, phenols, proteins, minerals, and oxidoreductases to estimate their chemistry and the preco
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47

Raghukumar, C., T. M. D’Souza, R. G. Thorn, and C. A. Reddy. "Lignin-Modifying Enzymes of Flavodon flavus, a Basidiomycete Isolated from a Coastal Marine Environment." Applied and Environmental Microbiology 65, no. 5 (1999): 2103–11. http://dx.doi.org/10.1128/aem.65.5.2103-2111.1999.

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ABSTRACT A basidiomycetous fungus Flavodon flavus (Klotzsch) Ryvarden (strain 312), isolated from decaying sea grass from a coral lagoon off the west coast of India, mineralized nearly 24% of14C-labeled synthetic lignin to14CO2 in 24 days. When grown in low-nitrogen medium (2.4 mM N) this fungus produced three major classes of extracellular lignin-modifying enzymes (LMEs): manganese-dependent peroxidase (MNP), lignin peroxidase (LIP), and laccase. Low MNP and laccase activities were seen in high-nitrogen medium (24 mM N), but no LIP activity was seen. In media containing lignocellulosic substr
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48

Ghindilis, A. "Direct electron transfer catalysed by enzymes: application for biosensor development." Biochemical Society Transactions 28, no. 2 (2000): 84–89. http://dx.doi.org/10.1042/bst0280084.

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The ability to catalyse an electrode reaction via direct (mediatorless) electron transfer has been demonstrated for a number of redox enzymes. In the case of mediatorless electron transfer, the electron is transferred directly from the electrode to the substrate molecule via the active site of the enzyme, or vice versa. The electron itself is the second substrate for the reaction. An important point characterizing bioelectrocatalysis is the catalytic removal of the reaction over-voltage. Therefore the enzyme attached to the electrode is able to catalyse electrode reaction and forms a ‘molecula
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49

Araújo, José Hilton Bernardino de, Vinicius Oliveira Uemura, Flavio Faria de Moraes, Aneli de Melo Barbosa, and Gisella Maria Zanin. "A comparative study on fungal laccases immobilized on chitosan." Brazilian Archives of Biology and Technology 48, spe (2005): 1–6. http://dx.doi.org/10.1590/s1516-89132005000400001.

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The phenoloxidase enzyme laccase from the cultures of the Pleurotus ostreatus and Botryosphaeria sp. and a commercial laccase from Aspergillus sp. were immobilized on chitosan of pharmaceutical degree by adsorption followed by crosslinking. Different immobilization conditions in relation to the granulometry of support and amount of enzymatic laccase extract used were tested, aiming at reaching high enzymatic activity with the immobilized enzyme. Two different substrates, ABTS and DMP, were used for the determination of enzymatic activity. The highest enzymatic activity was obtained when 1.0mg/
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50

Baiocco, Paola, Anna Maria Barreca, Maura Fabbrini, Carlo Galli, and Patrizia Gentili. "Promoting laccase activity towards non-phenolic substrates: a mechanistic investigation with some laccase–mediator systems." Org. Biomol. Chem. 1, no. 1 (2003): 191–97. http://dx.doi.org/10.1039/b208951c.

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