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1

Madad, Nidal, Latifa Chebil, Celine Charbonnel, Irina Ioannou, and Mohamed Ghoul. "Enzymatic polymerization of sodium lignosulfonates: effect of catalysts, initial molecular weight, and mediators." Canadian Journal of Chemistry 91, no. 3 (2013): 220–25. http://dx.doi.org/10.1139/cjc-2012-0036.

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The aim of this study was to investigate the effect of different parameters on the enzymatic polymerization of sodium lignosulfonates (SLS) by laccase, compared with the chemical treatment by manganese III. Different initial molecular weights of SLS (commercial SLS (17 800 Da), F1 (4300 Da), F2 (2500 Da), and F3 (2300 Da)) were tested. Size exclusion chromatography (SEC-UV), Fourier transform infrared (FT-IR) and phenolic group determination showed that SLS molecular weight increases depending on the laccase origin, the enzyme, and the substrate concentrations and the initial molecular weight
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2

Backes, Emanueli, Camila Gabriel Kato, Verci Alves de Oliveira Junior, et al. "Overproduction of Laccase by Trametes versicolor and Pycnoporus sanguineus in Farnesol-Pineapple Waste Solid Fermentation." Fermentation 9, no. 2 (2023): 188. http://dx.doi.org/10.3390/fermentation9020188.

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The effect of farnesol, a sesquiterpene alcohol, on the production of laccases by Trametes versicolor and Pycnoporus sanguineus in pineapple waste solid-state fermentation was evaluated. Extracellular laccase production reached a maximum of 77.88 ± 5.62 U/g (236% above control) in farnesol-induced cultures of T. versicolor on the 17th day, whereas in a similar P. sanguineus culture, a maximal laccase activity of 130.95 ± 2.20 U/g (159% increase) was obtained on the 17th day. A single 45 KDa laccase was produced by both fungi under the influence of farnesol. These and other data allow us to con
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3

Patel, Aashka Y., Austin K. Clark, Nicholas J. Paradis, et al. "Effects of Ionic Liquids on Laccase from Trametes versicolor." Biophysica 1, no. 4 (2021): 429–44. http://dx.doi.org/10.3390/biophysica1040031.

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Interactions between ionic liquids and biomolecules are of great interest due to the intrinsic properties of ionic liquids and the flexibility allowed by mixing and matching cations and anions to create unique ionic liquids. A number of ionic liquid–biomolecule studies have focused on interactions with proteins, including industrially relevant enzymes. One of these, laccase from Trametes versicolor, is a naturally derived enzyme used in the breakdown of phenolic compounds in a wide variety of industries, especially useful in breakdown of lignocellulosic materials. Here, a combination of experi
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4

Freitag, Michael, and Jeffrey J. Morrel. "Changes in selected enzyme activities during growth of pure and mixed cultures of the white-rot decay fungus Trametes versicolor and the potential biocontrol fungus Trichoderma harzianum." Canadian Journal of Microbiology 38, no. 4 (1992): 317–23. http://dx.doi.org/10.1139/m92-053.

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Two filamentous fungi, the white-rot fungus Trametes versicolor and the soil fungus and potential biocontrol organismTrichoderma harzianum, have been grown in pure and mixed cultures on low-N (0.4 mM) and high-N (4 mM) defined synthetic media to determine the activities of selected wood-degrading enzymes such as cellobiase, cellulase, laccase,and peroxidases. Growth characteristics and enzyme activities were examined for potential correlations. Such correlations would allow the use of simple enzyme assays for measuring biomass development and would facilitate predictions about competitiveness
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5

Legerská, Barbora, Daniela Chmelová, and Miroslav Ondrejovič. "Azonaphthalene dyes decolorization and detoxification by laccase from Trametes versicolor." Nova Biotechnologica et Chimica 17, no. 2 (2018): 172–80. http://dx.doi.org/10.2478/nbec-2018-0018.

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AbstractThe aim of the present study was to investigate the dye decolorization ability of laccase from Trametes versicolor. Five azonaphthalene dyes (Acid Violet 7, Acid Red 1, Allura Red AC, Orange G and Sunset Yellow FCF) were used to evaluate dye decolorization. Laccase from T. versicolor is capable of decolorizing dyes, namely Acid Violet 7 (53.7±2.3 %) and Orange G (46.0±2.2 %). The less effective ability of laccase was observed at the decolorization of other selected dyes (6.9 - 18.6 %). The presence of redox mediator (1-hydroxybenzotriazole) increased decolorization percentage for all t
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6

Al Shaikly, Ali A. Taha. "Purification And Characterization of Trametes hirsute DSMZ No.5072 Laccase." Journal of Biotechnology Research Center 3, no. 1 (2009): 46–59. http://dx.doi.org/10.24126/jobrc.2009.3.1.44.

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In this study, the Production of laccase enzyme from Trametes hirsuta strain (DSMZ No.5072) in the 2L fermenter using different culturing media had been achieved. The production of laccase was also induced by using different concentrations of Copper sulphate, 2, 5 Xylidine and Gallic acid as inducers. The maximum laccase activitiy observed during T. hirsuta growth in the presence of various inducers was 5.89 U ml -1. Laccase purification was performed by precipitated the enzymes with ammoniam sulphate, saturation 90%, followed by gel filtration chromatography using Sephadex-G25 and more purifi
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7

Fodor, Csaba, Bernadetta Gajewska, Omar Rifaie-Graham, Edward A. Apebende, Jonas Pollard, and Nico Bruns. "Laccase-catalyzed controlled radical polymerization of N-vinylimidazole." Polymer Chemistry 7, no. 43 (2016): 6617–25. http://dx.doi.org/10.1039/c6py01261b.

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8

Piccinino, Davide, Eliana Capecchi, Lorenzo Botta, et al. "Layer by layer supported laccase on lignin nanoparticles catalyzes the selective oxidation of alcohols to aldehydes." Catalysis Science & Technology 9, no. 15 (2019): 4125–34. http://dx.doi.org/10.1039/c9cy00962k.

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9

Wang, Feng, An-Zhou Ma, Chen Guo, Guo-Qiang Zhuang, and Chun-Zhao Liu. "Ultrasound-intensified laccase production from Trametes versicolor." Ultrasonics Sonochemistry 20, no. 1 (2013): 118–24. http://dx.doi.org/10.1016/j.ultsonch.2012.05.003.

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10

Adekunle, Abiodun E., Chen Guo, and Chun-Zhao Liu. "Lignin-Enhanced Laccase Production from Trametes versicolor." Waste and Biomass Valorization 8, no. 4 (2016): 1061–66. http://dx.doi.org/10.1007/s12649-016-9680-4.

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11

Galai, S., A. P. de los Ríos, F. J. Hernández-Fernández, S. Haj Kacem, and F. Tomas-Alonso. "Over-activity and stability of laccase using ionic liquids: screening and application in dye decolorization." RSC Advances 5, no. 21 (2015): 16173–89. http://dx.doi.org/10.1039/c4ra07351g.

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12

Taha, Ali A., Nahida J. Hameed, and Farah Hamed Ali. "Degradation of Anthracene by Immobilizing Laccase From Trametes Versicolor onto Chitosan Beads and Hyacinth Plant." Al-Mustansiriyah Journal of Science 31, no. 3 (2020): 14. http://dx.doi.org/10.23851/mjs.v31i3.670.

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Polycyclic aromatic hydrocarbons (PAHs) are recognized as a toxic, mutagenic and/or carcinogenic compounds, and their pollution of soil and aquifer is of increasing environmentally risk. Laccases (E.C. 1.10.3.2) are phenoloxidases catalyze the oxidation of PAHs in the presence of a mediator compound and hyacinth plant. In this study laccase from Trametes versicolor was immobilized into chitosan, and the potential to oxidize anthracene in the presence of 1-hydroxybenzotriazole (HBT) was examined. Results indicated that the immobilization enhanced the stability of laccase against temperature, pH
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13

Jing, Debing, Peijun Li, Frank Stagnitti, and Xianzhe Xiong. "Optimization of laccase production from Trametes versicolor by solid fermentation." Canadian Journal of Microbiology 53, no. 2 (2007): 245–51. http://dx.doi.org/10.1139/w06-121.

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The regulation of culture conditions, especially the optimization of substrate constituents, is crucial for laccase production by solid fermentation. To develop an inexpensive optimized substrate formulation to produce high-activity laccase, a uniform design formulation experiment was devised. The solid fermentation of Trametes versicolor was performed with natural aeration, natural substrate pH (about 6.5), environmental humidity of 60% and two different temperature stages (at 37 °C for 3 days, and then at 30 °C for the next 17 days). From the experiment, a regression equation for laccase act
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14

Ramos-Martín, Marina, Ramón Lecuna, Luciana Cicco, et al. "A one-pot two-step synthesis of tertiary alcohols combining the biocatalytic laccase/TEMPO oxidation system with organolithium reagents in aerobic aqueous media at room temperature." Chemical Communications 57, no. 99 (2021): 13534–37. http://dx.doi.org/10.1039/d1cc06460f.

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15

Han, Mei-Ling, Lin Lin, Xiao-Xiao Guo, et al. "Comparative analysis of the laccase secretion ability of five white-rot fungi in submerged fermentation with lignocellulosic biomass." BioResources 18, no. 1 (2022): 584–98. http://dx.doi.org/10.15376/biores.18.1.584-598.

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Lignocellulosic biomass is widely used in the field of laccase production because it has the advantages of low price and easy availability. Thus, a comparative analysis was performed of the laccase secretion ability of five white-rot fungi in submerged fermentation using single or mixtures of lignocellulosic biomass. Maximum laccase activity of Trametes gibbosa An 360, Vanderbylia fraxinea An 369, Perenniporia pyricola Han 202, Coriolopsis trogii Han 474, and Trametes versicolor Han 1504 was 55.83 ± 0.28 U/L on the mixture of corncob and cottonseed hull, 77.96 ± 1.60 U/L on corncob, 443.33 ± 1
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16

Bergbauer, Matthias, and Claudia Eggert. "Degradability of chlorine-free bleachery effluent lignins by two fungi: effects on lignin subunit type and on polymer molecular weight." Canadian Journal of Microbiology 40, no. 3 (1994): 192–97. http://dx.doi.org/10.1139/m94-032.

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A bleachery effluent from a sulfite process pulp mill, which was extracted with alkali and treated with oxygen and hydrogen peroxide (EOP), was treated with two fungi, Trametes versicolor and Stagonospora gigaspora. Trametes versicolor did not cause any depolymerization or degradation of effluent lignins but increased the amount of chromophores, whereas S. gigaspora depolymerized the EOP lignins and caused a substantial reduction in aromatic compounds. For both fungal treatments, CuO oxidation caused a decrease in the yield of the aldehydes within the vanillyl and p-hydroxy phenol families, wh
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17

Martínez-Montero, Lía, Vicente Gotor, Vicente Gotor-Fernández, and Iván Lavandera. "Stereoselective amination of racemic sec-alcohols through sequential application of laccases and transaminases." Green Chemistry 19, no. 2 (2017): 474–80. http://dx.doi.org/10.1039/c6gc01981a.

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A one-pot/two-step chemoenzymatic sequential methodology has been developed for the selective amination of secondary alcohols by combining the laccase from Trametes versicolor/TEMPO catalytic system with the stereoselective action of transaminases.
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18

Martínez-Montero, Lía, Alba Díaz-Rodríguez, Vicente Gotor, Vicente Gotor-Fernández, and Iván Lavandera. "Broadening the chemical scope of laccases: selective deprotection of N-benzyl groups." Green Chemistry 17, no. 5 (2015): 2794–98. http://dx.doi.org/10.1039/c5gc00525f.

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The chemoselective deprotection of N-benzylated primary amines, amino esters, diamines and amino alcohols in aqueous media using molecular oxygen as a mild oxidant has been demonstrated combining laccase from Trametes versicolor and TEMPO.
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19

Odaci, Dilek, Suna Timur, Nurdan Pazarlioglu, et al. "Determination of phenolic acids using Trametes versicolor laccase." Talanta 71, no. 1 (2007): 312–17. http://dx.doi.org/10.1016/j.talanta.2006.04.032.

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20

Wang, Feng, Chen Guo, Tao Wei, Tian Zhang, and Chun-Zhao Liu. "Heat Shock Treatment Improves Trametes versicolor Laccase Production." Applied Biochemistry and Biotechnology 168, no. 2 (2012): 256–65. http://dx.doi.org/10.1007/s12010-012-9769-6.

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21

Collins, P. J., and A. Dobson. "Regulation of Laccase Gene Transcription in Trametes versicolor." Applied and environmental microbiology 63, no. 9 (1997): 3444–50. http://dx.doi.org/10.1128/aem.63.9.3444-3450.1997.

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22

Maryšková, Milena, Petra Vaňátková, Markéta Schaabová, and Jiří Maryška. "Immobilization of Laccase from T. versicolor on Nanofiber Matrix." Materials Science Forum 937 (October 2018): 123–28. http://dx.doi.org/10.4028/www.scientific.net/msf.937.123.

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Prepared nanofiber matrices based on polyamide 6 and polyamide 6/chitosan with numerous amine groups were tested on enzyme immobilization. Laccase from Trametes versicolor was immobilized on both nanofiber sheets either via glutaraldehyde and hexamethylenediamine activation, or via adsorption followed by glutaraldehyde crosslinking. Both types of the attachment were successful, however, the adsorption method provided immobilized laccase with enhanced operational stability.
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23

Chmelová, Daniela, and Miroslav Ondrejovič. "Effect Of Metal Ions On Triphenylmethane Dye Decolorization By Laccase From Trametes Versicolor." Nova Biotechnologica et Chimica 14, no. 2 (2015): 191–200. http://dx.doi.org/10.1515/nbec-2015-0026.

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Abstract The aim of this study was investigate the influence of different metal ions on laccase activity and triphenylmethane dye decolorization by laccase from white-rot fungus Trametes versicolor. Laccase activity was inhibited by monovalent ions (Li+, Na+, K+ and Ag+) but the presence of divalent ions increased laccase activity at the concentration of 10 mmol/l. The effect of metal ions on decolorization of triphenylmethane dyes with different structures namely Bromochlorophenol Blue, Bromophenol Blue, Bromocresol Blue and Phenol Red was tested. The presence of metal ions (Na+, K+, Mg2+, Ca
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24

Van Hamme, Jonathan D., Eddie T. Wong, Heather Dettman, Murray R. Gray, and Michael A. Pickard. "Dibenzyl Sulfide Metabolism by White Rot Fungi." Applied and Environmental Microbiology 69, no. 2 (2003): 1320–24. http://dx.doi.org/10.1128/aem.69.2.1320-1324.2003.

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ABSTRACT Microbial metabolism of organosulfur compounds is of interest in the petroleum industry for in-field viscosity reduction and desulfurization. Here, dibenzyl sulfide (DBS) metabolism in white rot fungi was studied. Trametes trogii UAMH 8156, Trametes hirsuta UAMH 8165, Phanerochaete chrysosporium ATCC 24725, Trametes versicolor IFO 30340 (formerly Coriolus sp.), and Tyromyces palustris IFO 30339 all oxidized DBS to dibenzyl sulfoxide prior to oxidation to dibenzyl sulfone. The cytochrome P-450 inhibitor 1-aminobenzotriazole eliminated dibenzyl sulfoxide oxidation. Laccase activity (0.1
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25

Liu, Yulong, and Xiufu Hua. "Degradation of acenaphthylene and anthracene by chemically modified laccase from Trametes versicolor." RSC Adv. 4, no. 59 (2014): 31120–22. http://dx.doi.org/10.1039/c4ra02807d.

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We are studying the chemically modified laccase from Trametes versicolor for use in the in vitro oxidation of two polycyclic aromatic hydrocarbons (PAHs), acenaphthylene and anthracene, in combination with 2,2′-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) as a redox mediator.
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26

Píva, G. A., and R. W. S. P. Thomas. "Biomass and laccase production by Trametes versicolor, Trametes villosa and Pycnoporus sanguineus." International Biodeterioration & Biodegradation 37, no. 1-2 (1996): 119. http://dx.doi.org/10.1016/0964-8305(96)84326-5.

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27

Uldschmid, Andreas, Renate Dombi, and Karin Marbach. "Identification and functional expression of ctaA, a P-type ATPase gene involved in copper trafficking in Trametes versicolor." Microbiology 149, no. 8 (2003): 2039–48. http://dx.doi.org/10.1099/mic.0.26177-0.

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Here the identification and characterization of a gene encoding a copper-trafficking enzyme, ctaA (copper-transporting ATPase), from the basidiomycete Trametes versicolor are described. This P-type copper ATPase gene has two alleles, differing primarily in the length of the second, unusually long intron, and encodes a 983 aa protein with 40 % sequence identity to yeast Ccc2p. Overexpression of ctaA in yeast grown in the presence of copper led to a 15-fold increase in laccase yields, while overexpression of ctaA and tahA, a previously identified copper homeostasis gene of T. versicolor, was add
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28

Wasak, Agata, Radosław Drozd, Bartłomiej Grygorcewicz, Dorota Jankowiak, and Rafał Rakoczy. "Purification and recovery of laccase produced by submerged cultures of Trametes versicolor by three-phase partitioning as a simple and highly efficient technique." Polish Journal of Chemical Technology 20, no. 4 (2018): 88–95. http://dx.doi.org/10.2478/pjct-2018-0059.

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Abstract In this work, three-phase partitioning (TPP) was used for the purification of laccase from liquid cultures of Trametes versicolor. For determining the optimal conditions of TPP process, parameters such as initial pH (6.5, 7.0, 7.5, 8.0), ammonium sulphate saturation (20%-80%) and the water phase to tert-butanol ratio (1:0.5, 1:1, 1:2), were analyzed. The best conditions with 73% recovery and 24-fold purification was obtained with the use of 50% saturation with ammonium sulphate, water phase to tert-butanol ratio of 1:1 and initial pH 7.0. The molecular mass of the purified laccase sec
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29

Iimura, Yosuke, Tomonori Sonoki, and Hiroshi Habe. "Heterologous expression of Trametes versicolor laccase in Saccharomyces cerevisiae." Protein Expression and Purification 141 (January 2018): 39–43. http://dx.doi.org/10.1016/j.pep.2017.09.004.

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30

Chen, Lei, Xiaoming Yi, Fajun Deng, et al. "A novel ethanol-tolerant laccase, Tvlac, from Trametes versicolor." Biotechnology Letters 38, no. 3 (2015): 471–76. http://dx.doi.org/10.1007/s10529-015-1994-y.

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31

Hu, Xiaoke, Peng Wang, and Huey-min Hwang. "Oxidation of anthracene by immobilized laccase from Trametes versicolor." Bioresource Technology 100, no. 21 (2009): 4963–68. http://dx.doi.org/10.1016/j.biortech.2009.03.089.

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32

Adekunle, Abiodun Emmanuel, Feng Wang, Jianhua Hu, et al. "Chitosan multiple addition enhances laccase production from Trametes versicolor." Bioprocess and Biosystems Engineering 38, no. 10 (2015): 1973–81. http://dx.doi.org/10.1007/s00449-015-1438-z.

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33

Bassanini, Ivan, Simone Grosso, Chiara Tognoli, Giovanni Fronza, and Sergio Riva. "Studies on the Oxidation of Aromatic Amines Catalyzed by Trametes versicolor Laccase." International Journal of Molecular Sciences 24, no. 4 (2023): 3524. http://dx.doi.org/10.3390/ijms24043524.

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The bio-oxidation of a series of aromatic amines catalyzed by T. versicolor laccase has been investigated exploiting either commercially available nitrogenous substrates [(E)-4-vinyl aniline and diphenyl amine] or ad hoc synthetized ones [(E)-4-styrylaniline, (E)-4-(prop-1-en-1-yl)aniline and (E)-4-(((4-methoxyphenyl)imino)methyl)phenol]. At variance to their phenolic equivalents, the investigated aromatic amines were not converted into the expected cyclic dimeric structures under T. versicolor catalysis. The formation of complex oligomeric/polymeric or decomposition by-products was mainly obs
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34

Cardinal-Watkins, Chantale, та Jim A. Nicell. "Enzyme-Catalyzed Oxidation of 17β-Estradiol Using Immobilized Laccase from Trametes versicolor". Enzyme Research 2011 (22 серпня 2011): 1–11. http://dx.doi.org/10.4061/2011/725172.

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Many natural and synthetic estrogens are amenable to oxidation through the catalytic action of oxidative enzymes such as the fungal laccase Trametes versicolor. This study focused on characterizing the conversion of estradiol (E2) using laccase that had been immobilized by covalent bonding onto silica beads contained in a bench-scale continuous-flow packed bed reactor. Conversion of E2 accomplished in the reactor declined when the temperature of the system was changed from room temperature to just above freezing at pH 5 as a result of a reduced rate of reaction rather than inactivation of the
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35

Alcalde, Miguel, Thomas Bulter, and Frances H. Arnold. "Colorimetric Assays for Biodegradation of Polycyclic Aromatic Hydrocarbons by Fungal Laccases." Journal of Biomolecular Screening 7, no. 6 (2002): 547–53. http://dx.doi.org/10.1177/1087057102238629.

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Polycyclic aromatic hydrocarbons (PAHs) are highly toxic organic pollutants widely distributed in terrestrial and aquatic environments. In the present work, 2 colorimetric assays for laccase-catalyzed degradation of PAHs were developed based on studies of the oxidation of 12 aromatic hydrocarbons by fungal laccases from Trametes versicolor and Myceliophthora thermophila. Using a sodium borohydride water-soluble solution, the authors could reduce the single product of laccase-catalyzed anthracene biooxidation into the orange-colored 9,10-anthrahydroquinone, which is quantifiable spectrophotomet
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36

Park, Saerom, Dahun Jung, Hyejin Do, et al. "Laccase-Mediator System Using a Natural Mediator as a Whitening Agent for the Decolorization of Melanin." Polymers 13, no. 21 (2021): 3671. http://dx.doi.org/10.3390/polym13213671.

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In this study, a laccase-mediator system (LMS) using a natural mediator was developed as a whitening agent for melanin decolorization. Seven natural mediators were used to replace synthetic mediators and successfully overcome the low redox potential of laccase and limited access of melanin to the active site of laccase. The melanin decolorization activity of laccases from Trametes versicolor (lacT) and Myceliophthora thermophila (lacM) was significantly enhanced using natural mediators including acetosyringone, syringaldehyde, and acetovanillone, which showed low cytotoxicity. The methoxy and
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37

Zhang, Sitong, Zhuofu Wu, Guang Chen, and Zhi Wang. "An Improved Method to Encapsulate Laccase from Trametes versicolor with Enhanced Stability and Catalytic Activity." Catalysts 8, no. 7 (2018): 286. http://dx.doi.org/10.3390/catal8070286.

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In this work, laccase from Trametes versicolor pretreated with copper ion solution was entrapped in copper alginate beads. The presence of laccase in copper alginate beads was verified by Fourier transform infrared (FTIR) spectroscopy. The alginate concentration used was optimized based on the specific activity and immobilization yield. After entrapment, laccase presents perfect pH stability and thermal stability with 2,2′-azinobis-(3-ethylbenzthiazoline-6-sulphonate) (ABTS) as the substrate. Moreover, laccase in copper alginate beads exhibits good reusability during continuous batch operation
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TUTAL, Tülay, Özfer YEŞİLADA, and Filiz BORAN. "Laccase Production of Newly Isolated Trametes versicolor under Batch, Repeated-Batch, and Solid-State Fermentation Processes." Commagene Journal of Biology 6, no. 2 (2022): 190–96. http://dx.doi.org/10.31594/commagene.1197055.

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In this study, the laccase production ability of the newly isolated Trametes versicolor strain was investigated in three different fermentation processes. In all three fermentation processes, the fungus was able to produce the laccase enzyme. During the solid-state fermentation process 13.21 U/mL laccase activity was detected on the 20th day in the 10 mM copper-containing medium, while this value reached to 27.30 U/mL in the medium containing 0.5 mM ABTS+10 mM copper. During the liquid batch fermentation process, laccase activity was significantly induced in the medium containing 1 mM copper a
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39

Xu, Chunyan, Deepak Singh, Kathleen M. Dorgan, Xiaoyu Zhang, and Shulin Chen. "Screening of ligninolytic fungi for biological pretreatment of lignocellulosic biomass." Canadian Journal of Microbiology 61, no. 10 (2015): 745–52. http://dx.doi.org/10.1139/cjm-2015-0156.

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To identify white rot fungi with high potential in biological pretreatment of lignocellulosic biomass, preliminary screening was carried out on plates by testing different strains for their ability to oxidize guaiacol and decolorize the dyes azure B and Poly R-478. Of the 86 strains screened, 16 were selected for secondary screening for their ligninolytic ability; however, low manganese peroxidase activity and no lignin peroxidase activity were detected. Strain BBEL0970 proved to be the most efficient in laccase production and was subsequently identified as Trametes versicolor by analysis of t
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40

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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Li, Congcong, Yuhong Lou, Yazhen Wan, Weiqiang Wang, Jilei Yao, and Bing Zhang. "Laccase immobilized onto poly(GMA-MAA) microspheres for p-benzenediol removal from wastewater." Water Science and Technology 67, no. 10 (2013): 2287–93. http://dx.doi.org/10.2166/wst.2013.095.

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Enzymes have already been extensively applied to degrade various organic pollutants in industrial wastewater, and how to improve the stability and reusability of the enzymes is critical to their practical application. In this study, poly(glycidyl methacrylate-methacrylic acid), poly(GMA-MAA), microspheres were prepared by suspension polymerization, and were used as a new support to immobilize Trametes versicolor laccase. The maximum loading capacity to immobilize enzyme reached as high as 44.78 mg protein/g support. The stability and reusability of laccase were greatly improved after immobiliz
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Reyes, Carolina, Alexandre Poulin, Gustav Nyström, Francis W. M. R. Schwarze, and Javier Ribera. "Enzyme Activities of Five White-Rot Fungi in the Presence of Nanocellulose." Journal of Fungi 7, no. 3 (2021): 222. http://dx.doi.org/10.3390/jof7030222.

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White-rot fungi can degrade all lignocellulose components due to their potent lignin and cellulose-degrading enzymes. In this study, five white-rot fungi, Trametes versicolor, Trametes pubescens, Ganoderma adspersum, Ganoderma lipsiense, and Rigidoporus vitreus were tested for endoglucanase, laccase, urease, and glucose-6-phosphate (G6P) production when grown with malt extract and nanocellulose in the form of TEMPO (2,2,6,6-tetramethylpiperidine-1-oxyl radical) oxidized cellulose nanofibrils (CNF) and cellulose nanocrystals (CNC). Results show that temperature plays a key role in controlling t
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Rancaño, Gonzalo, Miriam Lorenzo, Norma Molares, Susana Rodrı́guez Couto, and Ma̱ Ángeles Sanromán. "Production of laccase by Trametes versicolor in an airlift fermentor." Process Biochemistry 39, no. 4 (2003): 467–73. http://dx.doi.org/10.1016/s0032-9592(03)00083-9.

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Pazarlıoǧlu, Nurdan Kaşıkara, Merih Sariişik, and Azmi Telefoncu. "Laccase: production by Trametes versicolor and application to denim washing." Process Biochemistry 40, no. 5 (2005): 1673–78. http://dx.doi.org/10.1016/j.procbio.2004.06.052.

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Kolb, Michaela, Volker Sieber, Manfred Amann, Martin Faulstich, and Doris Schieder. "Removal of monomer delignification products by laccase from Trametes versicolor." Bioresource Technology 104 (January 2012): 298–304. http://dx.doi.org/10.1016/j.biortech.2011.11.080.

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Ramaswamy, Umamaheswari, Ramkumar Lakshmanan, Mythili Ravichandran, Prabu Periasamy, and Shanmugam Sengodan. "Ameliorating Direct Blue Dye Degradation Using Trametes versicolor Derived Laccase Enzyme Optimized through Box–Behnken Design (BBD) via Submerged Fermentation." Journal of Experimental Biology and Agricultural Sciences 10, no. 4 (2022): 818–30. http://dx.doi.org/10.18006/2022.10(4).818.830.

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The major intend of this study was to elucidate the laccase production by Trametes versicolor under submerged fermentation using fruit waste peel as substrate. The textile dye was decolorized by the procured crude enzymatic extract using the response surface methodology. The submerged media with organic fruit peel waste extract (jackfruit, pineapple & kaffir) supplemented with gypsum, calcium carbonate, and nutrient broth were considered superior for laccase production. The produced laccase enzyme was used in dye decolorization at the optimum conditions using the Box-Behnken design. Subseq
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Saetang, J., and S. Babel. "Effect of glucose on enzyme activity and color removal by Trametes versicolor for high strength landfill leachate." Water Science and Technology 62, no. 11 (2010): 2519–26. http://dx.doi.org/10.2166/wst.2010.552.

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This research was carried out to study the treatment of landfill leachate by immobilized Trametes versicolor BCC 8725. Leachate was collected from Nonthaburi disposal site of Thailand from a pipe as discharged from landfill to the stabilization pond. Batch experiments were conducted to determine the effects of carbon source (glucose) on the biomass growth of fungi and the treatment of leachate in terms of color, Biological Oxygen Demand (BOD) and Chemical Oxygen Demand (COD) removal. Enzymes produced by Trametes versicolor BCC 8725 were also analyzed. Experimental results indicated a higher bi
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Sýs, Milan, Radovan Metelka, Arbër Frangu, Karel Vytřas, and Tahir Arbneshi. "Electrochemical Study of Trametes Versicolor Laccase Compatibility to Different Polyphenolic Substrates." Chemosensors 5, no. 1 (2017): 9. http://dx.doi.org/10.3390/chemosensors5010009.

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Gil, D. M. A., and M. J. F. Rebelo. "Gallic acid interference on polyphenolic amperometric biosensing using Trametes versicolor laccase." Journal of Molecular Catalysis B: Enzymatic 72, no. 3-4 (2011): 193–98. http://dx.doi.org/10.1016/j.molcatb.2011.06.005.

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Tišma, Marina, Polona Žnidaršič-Plazl, Đurđa Vasić-Rački, and Bruno Zelić. "Optimization of Laccase Production by Trametes versicolor Cultivated on Industrial Waste." Applied Biochemistry and Biotechnology 166, no. 1 (2011): 36–46. http://dx.doi.org/10.1007/s12010-011-9401-1.

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