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Journal articles on the topic 'Enzymes. Enzymes Peniophora. Laccase'

Author: Grafiati

Published: 4 June 2021

Last updated: 4 February 2022

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1

Zhang, X., G. Eigendorf, D. W. Stebbing, S. D. Mansfield, and J. N. Saddler. "Degradation of trilinolein by laccase enzymes." Archives of Biochemistry and Biophysics 405, no. 1 (2002): 44–54. http://dx.doi.org/10.1016/s0003-9861(02)00331-4.

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2

Paredes-Juárez, Ana Karina, Elba Villegas-Villareal, Rubén Díaz-Godínez, and Gerardo Díaz-Godínez. "Applications of laccase enzymes of Pleurotus ostreatus." Mexican Journal of Biotechnology 2, no. 1 (2017): 134–44. http://dx.doi.org/10.29267/mxjb.2017.2.1.135.

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La producción de enzimas extracelulares de hongos filamentosos ha sido ampliamente desarrollada mediante el uso de fermentación sumergida. Sin embargo, la fermentación en estado sólido es una alternativa adecuada para la producción de enzimas dada las características fisiológicas y morfológicas de estos hongos. En este sentido, el uso de residuos agroindustriales como sustratos en la producción de enzimas de interés industrial es una muy buena alternativa debido a su composición, principalmente de celulosa, hemicelulosa y lignina que actúan como inductores para la síntesis de enzimas. Pocos mi

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3

Tron, T., A. M. Cusano, Y. Liu, Y. Mekmouche, E. Npetgat, and V. Robert. "Engineered laccase: artificial enzymes with new properties." Journal of Biotechnology 150 (November 2010): 77. http://dx.doi.org/10.1016/j.jbiotec.2010.08.198.

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4

Moin, Syed, and Muhammad Omar. "Laccase Enzymes: Purification, Structure to Catalysis and Tailoring." Protein & Peptide Letters 21, no. 8 (2013): 707–13. http://dx.doi.org/10.2174/09298665113209990058.

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5

Viterbo, Ada, Boris Yagen, and Alfred M. Mayer. "Cucurbitacins, ‘attack’ enzymes and laccase in Botrytis cinerea." Phytochemistry 32, no. 1 (1992): 61–65. http://dx.doi.org/10.1016/0031-9422(92)80107-p.

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6

Miele, Annalisa, Paola Giardina, Eugenio Notomista, Alessandra Piscitelli, Giovanni Sannia, and Vincenza Faraco. "A Semi-Rational Approach to Engineering Laccase Enzymes." Molecular Biotechnology 46, no. 2 (2010): 149–56. http://dx.doi.org/10.1007/s12033-010-9289-y.

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7

Alberts, J. F., W. C. A. Gelderblom, A. Botha, and W. H. van Zyl. "Degradation of aflatoxin B1 by fungal laccase enzymes." International Journal of Food Microbiology 135, no. 1 (2009): 47–52. http://dx.doi.org/10.1016/j.ijfoodmicro.2009.07.022.

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8

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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9

D’Souza, Trevor M., Carlos S. Merritt, and C. Adinarayana Reddy. "Lignin-Modifying Enzymes of the White Rot Basidiomycete Ganoderma lucidum." Applied and Environmental Microbiology 65, no. 12 (1999): 5307–13. http://dx.doi.org/10.1128/aem.65.12.5307-5313.1999.

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ABSTRACT Ganoderma lucidum, a white rot basidiomycete widely distributed worldwide, was studied for the production of the lignin-modifying enzymes laccase, manganese-dependent peroxidase (MnP), and lignin peroxidase (LiP). Laccase levels observed in high-nitrogen (HN; 24 mM N) shaken cultures were much greater than those seen in low-nitrogen (2.4 mM N), malt extract, or wood-grown cultures and those reported for most other white rot fungi to date. Laccase production was readily seen in cultures grown with pine or poplar (100-mesh-size ground wood) as the sole carbon and energy source. Cultures

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10

GÓRSKA, EWA B., URSZULA JANKIEWICZ, JAKUB DOBRZYŃSKI, et al. "Production of Ligninolytic Enzymes by Cultures of White Rot Fungi." Polish Journal of Microbiology 63, no. 4 (2014): 461–65. http://dx.doi.org/10.33073/pjm-2014-062.

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Some Basidiomycota were chosen for studies of key ligninases synthesis (25°C, 30 days) in modified medium (shaken or not cultures) with added wheat straw. Liquid Czapek medium with straw yielded a higher amount of laccase than peroxidase, ground straw induced enzyme worse than chopped straw. With peroxidase the reverse dependencies were observed. Laccase of Lentinus edodes synthesized two enzyme isoforms (ca 30 and 16 kDa). In T. versicolor culture active laccase protein with highest molecular mass ca 65 kDa was found. P. sajor-caju yielded three different peroxidase isoforms. Ligninase biosyn

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11

Wells, A., M. Teria, and T. Eve. "Green oxidations with laccase–mediator systems." Biochemical Society Transactions 34, no. 2 (2006): 304–8. http://dx.doi.org/10.1042/bst0340304.

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Laccases are oxidase enzymes produced by ‘white rot’ fungi as part of a complex armoury of redox enzymes used to break down lignin – part of the carbon cycle of nature. Laccases alone or in combination with redox co-catalysts have been shown to oxidize xenobiotic compounds under conditions that can be described as ‘green’. This paper describes some novel oxidations using the laccase–mediator method and some current limitations to the use of this technology.

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12

Ogunyewo, Olusola A., and Folasade M. Olajuyigbe. "Unravelling the Interactions between Hydrolytic and Oxidative Enzymes in Degradation of Lignocellulosic Biomass bySporothrix carnisunder Various Fermentation Conditions." Biochemistry Research International 2016 (2016): 1–8. http://dx.doi.org/10.1155/2016/1614370.

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The mechanism underlying the action of lignocellulolytic enzymes in biodegradation of lignocellulosic biomass remains unclear; hence, it is crucial to investigate enzymatic interactions involved in the process. In this study, degradation of corn cob bySporothrix carnisand involvement of lignocellulolytic enzymes in biodegradation were investigated over 240 h cultivation period. About 60% degradation of corn cob was achieved byS. carnisat the end of fermentation. The yields of hydrolytic enzymes, cellulase and xylanase, were higher than oxidative enzymes, laccase and peroxidase, over 144 h ferm

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13

Galindo-de-la-Rosa, J., E. Ortiz-Ortega, B. López-González, L. G. Arriaga, and J. Ledesma-García. "Microfluidic biofuel cell based on cholesterol oxidase/laccase enzymes." Journal of Physics: Conference Series 1407 (November 2019): 012096. http://dx.doi.org/10.1088/1742-6596/1407/1/012096.

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14

Valls, Cristina, and M. Blanca Roncero. "Using both xylanase and laccase enzymes for pulp bleaching." Bioresource Technology 100, no. 6 (2009): 2032–39. http://dx.doi.org/10.1016/j.biortech.2008.10.009.

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15

Praveen, K., B. Viswanath, K. Y. Usha, et al. "Lignolytic Enzymes of a Mushroom Stereum ostrea Isolated from Wood Logs." Enzyme Research 2011 (September 20, 2011): 1–6. http://dx.doi.org/10.4061/2011/749518.

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Production of lignolytic enzymes by the mushroom fungus Stereum ostrea in liquid medium under conditions of vegetative growth was examined for 10 days in comparison to the reference culture Phanerochaete chrysosporium. Though growth and secretion of extracellular protein by S. ostrea were comparable to those of P. chrysosporium, yields of laccase enzyme by S. ostrea were higher than laccase titres of P. chrysosporium by more than 2 folds on the peak production time interval (IVth day of incubation). S. ostrea yielded titres of 25 units of laccase/ml as against 8.9 units of laccase/ml on the IV

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16

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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17

Pozdnyakova, Natalia, Svetlana Nikiforova, and Olga Turkovskaya. "Influence of PAHs on ligninolytic enzymes of the fungus Pleurotus ostreatus D1." Open Life Sciences 5, no. 1 (2010): 83–94. http://dx.doi.org/10.2478/s11535-009-0075-4.

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AbstractPolycyclic aromatic hydrocarbons (PAHs), their derivatives, and their degradation products were assayed for the ability to enhance activities of ligninolytic enzymes (laccase and versatile peroxidase) of the fungus Pleurotus ostreatus D1. The activities of both laccase and versatile peroxidase were induced by the PAHs, their derivatives, and their degradation products. Laccase was produced mostly in the first 7–10 days, whereas the production of versatile peroxidase began after 5–7 days of cultivation. Non-denaturing PAGE showed the presence of additional forms of laccase and versatile

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18

Gea, Saharman, Noni Oktari, Andriayani Andriayani, Sri Rahayu, and Averroes F. Piliang. "Comparative Optimization of Cellulase and Laccase Enzymes in Deinking Process of Used Newspapers." Jurnal Kimia Sains dan Aplikasi 23, no. 10 (2020): 353–59. http://dx.doi.org/10.14710/jksa.23.10.353-359.

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The use of enzymes in the bio-deinking process of newspaper waste has promising potential. However, investigations on the concentration of enzyme combinations need to be carried out to obtain the optimum ratio of cellulase and laccase enzymes for the bio-deinking process of recycled newspapers. The mixture of the two enzymes at various ratios was used to remove the ink on paper pulp from used newspapers by mechanical disintegration method treatment and followed by the bio-deinking process in an incubator shaker. The characterization of functional groups, structures, and thermal properties of b

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19

Shantaveera Swamy, H. M., and Ramalingappa. "Lignolytic Enzymes Production from Selected Mushrooms." International Journal of Applied Sciences and Biotechnology 3, no. 2 (2015): 308–13. http://dx.doi.org/10.3126/ijasbt.v3i2.12732.

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In this paper, ligninase enzymes produced by selected mushrooms have been reported. We collected mushrooms from Western Ghats, most of them were edible food. Thirty samples isolated were tested using a plate assay through direct agar plate assay by using ABTS, decolourisation containing the fifteen isolates were able to decolourise the dye, indicating a lignin-degrading ability. Spectrophotometric enzyme assays from all selected isolates were carried out to examine the production of Ligninolytic enzymes (Laccase, lignin peroxidase and manganese peroxidase). Ten selected isolates produced all t

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20

Mezzomo, Ricardo, Jéssica Mengue Rolim, Álvaro Figueredo dos Santos, et al. "Aggressiveness of Fusarium oxysporum and Fusarium solani isolates to yerba-mate and production of extracellular enzymes." Summa Phytopathologica 45, no. 2 (2019): 141–45. http://dx.doi.org/10.1590/0100-5405/198057.

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ABSTRACT The yerba-mate (Ilex paraguariensis) has great socioeconomic importance on family farming in Southerm Brazil. One of the main yerba-mate disease is root rotting, caused by Fusarium spp. Little is known about the pathogen physiology, especially regarding the aggressiveness associated with the production of extracellular enzymes. On this work, the aggressiveness of isolates of F. oxysporum and F. solani pathogenic to yerba-mate was evaluated and it was determined the activities of extracellular enzymes catalase, laccase, cellulase, caseinase, amylase, protease, lipase and pectinases pro

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21

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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22

Sudarson, Jenefar, Shenbhagaraman Ramalingam, Premalatha Kishorekumar, and Kaviyarasan Venkatesan. "Expeditious Quantification of Lignocellulolytic Enzymes from Indigenous Wood Rot and Litter Degrading Fungi from Tropical Dry Evergreen Forests of Tamil Nadu." Biotechnology Research International 2014 (February 26, 2014): 1–6. http://dx.doi.org/10.1155/2014/127848.

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In this study thirty wood rotting and litter degrading basidiomycetes were screened for the production of lignocellulolytic enzymes such as, laccase, peroxidase, and cellulase using rapid micro quantification assay. Out of the 30 indigenous isolates Trametes gibbosa was identified to be a potential lignocellulolytic enzyme producer, producing a maximum amount of cellulase (299.66±1.59 IU/L) and laccase (257.94±1.79 U/L). Moreover, it is the second leading producer of peroxidase enzyme (170.19±1.98 U/L). Tricholomopsis sp. a wood rot basidiomycete was found to be the leading lignin decomposer w

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23

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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24

Preda, Daniel, Mălina Deșliu-Avram, Bogdan Trică, Florin Oancea, and Diana Constantinescu-Aruxandei. "Optimization of Laccase Extraction from Spent Pleurotus Substrate." Proceedings 57, no. 1 (2020): 77. http://dx.doi.org/10.3390/proceedings2020057077.

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25

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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26

Vats, Anumeha, Anuj Sangam Kurade, and Srikanth Mutnuri. "Recovery of Lignocellulolytic Enzymes and Valorization of Spent Mushroom Substrate." Environment and Natural Resources Journal 20, no. 1 (2021): 1–9. http://dx.doi.org/10.32526/ennrj/20/202100099.

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Spent Mushroom Substrate (SMS) comprises sugarcane bagasse, coconut coir, chicken manure, and paddy straw; inoculated with and farmed for Agaricus bisporus. At present, the waste generation at a mushroom cultivation plant in Goa is 40 tons/day (15,000 tons annually). Valorization of this waste has been explored in terms of extracting lignocellulolytic enzymes and briquette production. SMS was screened for the presence of lignocellulolytic enzymes and then was used to make briquettes. The enzymes found in SMS were cellulase and laccase, which were further concentrated via tangential flow filtra

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Janusz, Grzegorz, Anna Pawlik, Urszula Świderska-Burek, et al. "Laccase Properties, Physiological Functions, and Evolution." International Journal of Molecular Sciences 21, no. 3 (2020): 966. http://dx.doi.org/10.3390/ijms21030966.

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Discovered in 1883, laccase is one of the first enzymes ever described. Now, after almost 140 years of research, it seems that this copper-containing protein with a number of unique catalytic properties is widely distributed across all kingdoms of life. Laccase belongs to the superfamily of multicopper oxidases (MCOs)—a group of enzymes comprising many proteins with different substrate specificities and diverse biological functions. The presence of cupredoxin-like domains allows all MCOs to reduce oxygen to water without producing harmful byproducts. This review describes structural characteri

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Šrédlová, Kamila, Kateřina Šírová, Tatiana Stella, and Tomáš Cajthaml. "Degradation Products of Polychlorinated Biphenyls and Their In Vitro Transformation by Ligninolytic Fungi." Toxics 9, no. 4 (2021): 81. http://dx.doi.org/10.3390/toxics9040081.

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Metabolites of polychlorinated biphenyls (PCBs)—hydroxylated PCBs (OH-PCBs), chlorobenzyl alcohols (CB-OHs), and chlorobenzaldehydes (CB-CHOs)—were incubated in vitro with the extracellular liquid of Pleurotus ostreatus, which contains mainly laccase and low manganese-dependent peroxidase (MnP) activity. The enzymes were able to decrease the amount of most of the tested OH-PCBs by > 80% within 1 h; the removal of more recalcitrant OH-PCBs was greatly enhanced by the addition of the laccase mediator syringaldehyde. Conversely, glutathione substantially hindered the reaction, suggesting that

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29

Ayla, Sridevi, Narasimha Golla, and Suvarnalathadevi Pallipati. "Production of Ligninolytic Enzymes from Penicillium Sp. and Its Efficiency to Decolourise Textile Dyes." Open Biotechnology Journal 12, no. 1 (2018): 112–22. http://dx.doi.org/10.2174/1874070701812010112.

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Background:The present study discussed the bio decolourization of synthetic textile dyes using extracellular crude laccase from an Ascomycetes fungusPenicilliumsp. Laccase based decolourization is found to be potentially advantageous to bioremediation technologies.Methods:In this study, the production of laccase was observed for 7 days of incubation under shaking conditions. Maximum laccase production was secreted by fungal strain on the 6thday of incubation under submerged fermentation. Incubation of fungal mycelium and culture filtrate as crude enzyme obtained fromPenicilliumsp. with textile

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Rohrmann, S., and H. P. Molitoris. "Screening for wood-degrading enzymes in marine fungi." Canadian Journal of Botany 70, no. 10 (1992): 2116–23. http://dx.doi.org/10.1139/b92-263.

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Forty marine and 15 terrestrial fungi in the Ascomycetes, Basidiomycetes, and Deuteromycetes were screened for presence and relative amount of enzymes involved in wood degradation (cellulases and redox enzymes) using seawater and deionized water media. Distribution of cellulases, laccase, tyrosinase, and peroxidase among marine and terrestrial groups of fungi was investigated. β-Glucosidase (C4) and endoglucanase (C3) were the most frequent enzymes (80 – 100% of the strains) of cellulose metabolism. Acid-swollen cellulose (C1) was generally more easily degraded than microcrystalline-dyed Avice

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Pickard, M. A., H. Vandertol, R. Roman, and R. Vazquez-Duhalt. "High production of ligninolytic enzymes from white rot fungi in cereal bran liquid medium." Canadian Journal of Microbiology 45, no. 7 (1999): 627–31. http://dx.doi.org/10.1139/w98-233.

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White rot fungi from the University of Alberta Mold Herbarium, identified as able to degrade aromatics from a study of PCB metabolism, were examined for production of ligninolytic enzymes. Production of lignin peroxidase, manganese peroxidase, laccase, and veratryl alcohol oxidase were monitored during growth in different media. Good growth but low enzyme production occurred in a glucose - malt extract - yeast extract medium. Media containing 2% cereal bran in 60 mM phosphate buffer supported high levels of laccase production, up to 13 000 U/L in Coriolopsis gallica UAMH 8260 and manganese per

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32

Usha, K. Y., K. Praveen, and B. Rajasekhar Reddy. "Enhanced Production of Ligninolytic Enzymes by a Mushroom Stereum ostrea." Biotechnology Research International 2014 (December 30, 2014): 1–9. http://dx.doi.org/10.1155/2014/815495.

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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

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Pérez, J., T. de la Rubia, O. Ben Hamman, and J. Martínez. "Phanerochaete flavido-alba Laccase Induction and Modification of Manganese Peroxidase Isoenzyme Pattern in Decolorized Olive Oil Mill Wastewaters." Applied and Environmental Microbiology 64, no. 7 (1998): 2726–29. http://dx.doi.org/10.1128/aem.64.7.2726-2729.1998.

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ABSTRACT Lignin-degrading enzymes were partially purified from supernatant solutions obtained from Phanerochaete flavido-alba-decolorized olive oil mill wastewaters (OMW). The dominant enzymes, manganese peroxidases, exhibited different isoform patterns in decolorized OMW-containing cultures than in residue-free samples. Laccase induction was also detected in OMW-containing cultures but not in control cultures.

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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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Unuofin, John O., Anthony I. Okoh, and Uchechukwu U. Nwodo. "Aptitude of Oxidative Enzymes for Treatment of Wastewater Pollutants: A Laccase Perspective." Molecules 24, no. 11 (2019): 2064. http://dx.doi.org/10.3390/molecules24112064.

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Natural water sources are very often contaminated by municipal wastewater discharges which contain either of xenobiotic pollutants and their sometimes more toxic degradation products, or both, which frustrates the universal millenium development goal of provision of the relatively scarce pristine freshwater to water-scarce and -stressed communities, in order to augment their socioeconomic well-being. Seeing that both regulatory measures, as regards the discharge limits of wastewater, and the query for efficient treatment methods remain unanswered, partially, the prospects of enzymatic treatmen

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Subowo, Yohanes Bernard, and Arwan Sugiharto. "The Influence of Inducers on the Coltricia cinnamomea Laccase Activity and its Ability to Degrade POME." Biosaintifika: Journal of Biology & Biology Education 13, no. 2 (2021): 243–49. http://dx.doi.org/10.15294/biosaintifika.v13i2.29660.

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Some species of Basidiomycetes, specifically white rot groups, produce three ligninolytic enzymes, namely, Lignin Peroxidase (LiP), Manganese Peroxidase (MnP) and Laccase (Lac), which have low activity in degrading Palm Oil Mill Effluent (POME). The research objective was to obtain the data on the ability of the Coltricia cinnamomea to produce LiP, MnP, and Lac enzymes to degrade POME. This research also studied the effect of sucrose, alcohol, veratryl alcohol, CuSO4 and ZnSO4,as inducers. Isolates of Coltricia cinnamomea, which were stored in a PDA media at -20℃ were obtained from the Microbi

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Quevedo-Hidalgo, Balkys, Paulo Cesar Narváez-Rincón, Aura Marina Pedroza-Rodríguez, and Mario Enrique Velásquez-Lozano. "Production of lignocellulolytic enzymes from floriculture residues using Pleurotus ostreatus." Universitas Scientiarum 20, no. 1 (2014): 117. http://dx.doi.org/10.11144/javeriana.sc20-1.eple.

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Floriculture is a vital agro-industrial sector in the Colombian economy; the export of flowers positively impacts employment and the balance of trade. However, this industry could negatively impact the environment if its waste products are not handled properly. These flower residues, rich in lignin, hemicellulose and cellulose, could be a cost-effective raw material to produce enzymes. Here, we evaluate the production of lignocellulolytic enzymes by degradation of Chrysanthemum and Rosa residues using Pleurotus ostreatus and manganese sulfate and copper sulfate as inductors. From the two resid

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Armesto, Cecilia, Fernanda Gonçalves Martins Maia, Fernando Pereira Monteiro, and Mário Sobral de Abreu. "exoenzymes as a pathogenicity factor for Colletotrichum gloeosporioides associated with coffee plants." Summa Phytopathologica 45, no. 4 (2019): 368–73. http://dx.doi.org/10.1590/0100-5405/191071.

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ABSTRACT Phytopathogenic fungi during the penetration and colonization process are capable of secreting several enzymes, which enable infection of the host live tissue, acting on the degradation of wax, cuticle and cell walls. The ability of a pathogenic agent to produce enzymes or not can determine the severity degree of a disease. In this study, 33 isolates of Colletotrichum gloeosporioides related to anthracnose and blister spot on coffee trees were evaluated for their ability to produce hydrolytic enzymes (amylase, lipase, protease, laccase, pectinase and cellulase) and specific cell wall

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Ulyanova, Yevgenia, Sofia Babanova, Erica Pinchon, Ivana Matanovic, Sameer Singhal, and Plamen Atanassov. "Effect of enzymatic orientation through the use of syringaldazine molecules on multiple multi-copper oxidase enzymes." Phys. Chem. Chem. Phys. 16, no. 26 (2014): 13367–75. http://dx.doi.org/10.1039/c4cp01296h.

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Martin, King Dave G., Maria Fatima T. Astrero, Laurence Anthony N. Mallari, and Roland M. Hipol. "Activity of Laccase Enzyme Present in the Phenol-Contaminated Sediments of the Marilao-Meycauayan-Obando River System, Philippines." Oriental Journal Of Chemistry 37, no. 1 (2021): 162–68. http://dx.doi.org/10.13005/ojc/370122.

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Laccases are enzymes produced by different microbes like bacteria and fungi. These enzymes are members of the family of oxidases and are capable of oxidizing phenolics into non-toxic forms. Sediments were collected from the Marilao-Meycauayan-Obando River System, specifically from the sampling area connected to leather tanneries, which directly dump their effluents into the river. This study aimed to determine the presence of laccase activity of sediments of Meycauayan River where effluents of leather factories and tanneries are directly dumped. Concentration of the phenolic compounds from fiv

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Dettori, Maria Antonietta, Davide Fabbri, Alessandro Dessì, et al. "Synthesis and Studies of the Inhibitory Effect of Hydroxylated Phenylpropanoids and Biphenols Derivatives on Tyrosinase and Laccase Enzymes." Molecules 25, no. 11 (2020): 2709. http://dx.doi.org/10.3390/molecules25112709.

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The impaired activity of tyrosinase and laccase can provoke serious concerns in the life cycles of mammals, insects and microorganisms. Investigation of inhibitors of these two enzymes may lead to the discovery of whitening agents, medicinal products, anti-browning substances and compounds for controlling harmful insects and bacteria. A small collection of novel reversible tyrosinase and laccase inhibitors with a phenylpropanoid and hydroxylated biphenyl core was prepared using naturally occurring compounds and their activity was measured by spectrophotometric and electrochemical assays. Biose

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Davidi, Lital, Sarah Moraïs, Lior Artzi, et al. "Toward combined delignification and saccharification of wheat straw by a laccase-containing designer cellulosome." Proceedings of the National Academy of Sciences 113, no. 39 (2016): 10854–59. http://dx.doi.org/10.1073/pnas.1608012113.

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Efficient breakdown of lignocellulose polymers into simple molecules is a key technological bottleneck limiting the production of plant-derived biofuels and chemicals. In nature, plant biomass degradation is achieved by the action of a wide range of microbial enzymes. In aerobic microorganisms, these enzymes are secreted as discrete elements in contrast to certain anaerobic bacteria, where they are assembled into large multienzyme complexes termed cellulosomes. These complexes allow for very efficient hydrolysis of cellulose and hemicellulose due to the spatial proximity of synergistically act

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Evans, John Parker, Dominic F. Gervasio, and Barry M. Pryor. "A Hybrid Microbial–Enzymatic Fuel Cell Cathode Overcomes Enzyme Inactivation Limits in Biological Fuel Cells." Catalysts 11, no. 2 (2021): 242. http://dx.doi.org/10.3390/catal11020242.

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The construction of optimized biological fuel cells requires a cathode which combines the longevity of a microbial catalyst with the current density of an enzymatic catalyst. Laccase-secreting fungi were grown directly on the cathode of a biological fuel cell to facilitate the exchange of inactive enzymes with active enzymes, with the goal of extending the lifetime of laccase cathodes. Directly incorporating the laccase-producing fungus at the cathode extends the operational lifetime of laccase cathodes while eliminating the need for frequent replenishment of the electrolyte. The hybrid microb

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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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Wong, A. L., and H. J. Willetts. "Polyacrylamide-gel Electrophoresis of Enzymes during Morphogenesis of Sclerotia of Sclerotinia sclerotiorum." Microbiology 81, no. 1 (2000): 101–9. http://dx.doi.org/10.1099/00221287-81-1-101.

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Succinate dehydrogenase (SDH) and glucose-6-phosphate dehydrogenase (Glu-6-PDH) from Sclerotinia sclerotiorum (Lib.) de Bary were moderately active in submerged mycelium while in non-sclerotial aerial mycelium arylesterase and acid phosphatase were very active. In sclerotial initials, glyceraldehyde-3-phosphate dehydrogenase (Gly-3-PDH) and SDH were at their highest level of activity, Glu-6-PDH and phosphogluconate dehydrogenase (PGDH) were moderately active, laccase activity increased markedly, and tyrosinase was detected for the first time, its activity being moderate. In young compacting sc

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Chandra, Ram, and Pankaj Chowdhary. "Properties of bacterial laccases and their application in bioremediation of industrial wastes." Environmental Science: Processes & Impacts 17, no. 2 (2015): 326–42. http://dx.doi.org/10.1039/c4em00627e.

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Parvulescu, Viorica, Adriana Popa, Gabriela Paun, Ramona Ene, Corneliu-Mircea Davidescu, and Gheorghe Ilia. "Effect of polymer support functionalization on enzyme immobilization and catalytic activity." Pure and Applied Chemistry 86, no. 11 (2014): 1793–803. http://dx.doi.org/10.1515/pac-2014-0715.

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Abstract Two enzymes, laccase and peroxidase, were immobilized on chloromethylated styrene-divinylbenzene copolymers supports functionalized with phosphonates ((RO)2PO) or mixed ammonium and phosphonium groups (N+R3Cl–, P+Ph3Cl–). Phosphonates groups and quaternary ammonium salts were grafted on the “gel-type” copolymer by Michaelis–Becker polymer analogue reaction. Mixed polymer-supported ammonium and phosphonium salts were obtained by transquaternization of the ammonium groups to phosphonium group. The degrees of functionalization for obtained polymers were relatively high ensuring a suffici

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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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Taprab, Yaovapa, Toru Johjima, Yoshimasa Maeda, et al. "Symbiotic Fungi Produce Laccases Potentially Involved in Phenol Degradation in Fungus Combs of Fungus-Growing Termites in Thailand." Applied and Environmental Microbiology 71, no. 12 (2005): 7696–704. http://dx.doi.org/10.1128/aem.71.12.7696-7704.2005.

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ABSTRACT Fungus-growing termites efficiently decompose plant litter through their symbiotic relationship with basidiomycete fungi of the genus Termitomyces. Here, we investigated phenol-oxidizing enzymes in symbiotic fungi and fungus combs (a substrate used to cultivate symbiotic fungi) from termites belonging to the genera Macrotermes, Odontotermes, and Microtermes in Thailand, because these enzymes are potentially involved in the degradation of phenolic compounds during fungus comb aging. Laccase activity was detected in all the fungus combs examined as well as in the culture supernatants of

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Gómez-Toribio, Víctor, Ana B. García-Martín, María J. Martínez, Ángel T. Martínez, and Francisco Guillén. "Induction of Extracellular Hydroxyl Radical Production by White-Rot Fungi through Quinone Redox Cycling." Applied and Environmental Microbiology 75, no. 12 (2009): 3944–53. http://dx.doi.org/10.1128/aem.02137-08.

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ABSTRACT A simple strategy for the induction of extracellular hydroxyl radical (OH) production by white-rot fungi is presented. It involves the incubation of mycelium with quinones and Fe3+-EDTA. Succinctly, it is based on the establishment of a quinone redox cycle catalyzed by cell-bound dehydrogenase activities and the ligninolytic enzymes (laccase and peroxidases). The semiquinone intermediate produced by the ligninolytic enzymes drives OH production by a Fenton reaction (H2O2 + Fe2+ → OH + OH− + Fe3+). H2O2 production, Fe3+ reduction, and OH generation were initially demonstrated with two

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