Academic literature on the topic 'Enzymes. Enzymes Peniophora. Laccase'

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

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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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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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Enzymes. Enzymes Peniophora. Laccase"

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Jordaan, Justin. "Isolation and characterization of a novel thermostable and catalytically efficient laccase from Peniophora sp. strain UD4." Thesis, Rhodes University, 2005. http://eprints.ru.ac.za/211/.

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Luo, Wen. "Growth studies of marine and terrestrial lignicolous fungi with special reference to laccase and other lignin-modifying enzyme activities of xylariaceous fungi /." access full-text access abstract and table of contents, 2005. http://libweb.cityu.edu.hk/cgi-bin/ezdb/thesis.pl?phd-bch-b19887905a.pdf.

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Thesis (Ph.D.)--City University of Hong Kong, 2005.<br>"Submitted to Department of Biology and Chemistry in partial fulfillment of the requirements for the degree of Doctor of Philosophy" Includes bibliographical references (leaves 216-256)
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Obanda, Aston Martin. "The oxidation of simple and complex polyphenols by laccase." Thesis, Imperial College London, 1990. http://hdl.handle.net/10044/1/46476.

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Mainardi, Pedro Henrique [UNESP]. "Produção de lacases pelo fungo filamentoso de origem marinha Peniophora sp. CBMAI 1063 em biorreator de bancada." Universidade Estadual Paulista (UNESP), 2015. http://hdl.handle.net/11449/134175.

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Made available in DSpace on 2016-02-05T18:30:03Z (GMT). No. of bitstreams: 0 Previous issue date: 2015-06-18. Added 1 bitstream(s) on 2016-02-05T18:34:10Z : No. of bitstreams: 1 000857369.pdf: 1913913 bytes, checksum: 2f38669e1a503f107487f09a70af3b0c (MD5)<br>Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)<br>As lacases são enzimas que catalisam uma reação que oxida moléculas aromáticas fenólicas. Com grande potencial biotecnológico, as lacases podem ser empregadas em diversos setores industriais. Suas principais aplicações são referentes a indústria de polpa e papel, têxtil, a
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Mainardi, Pedro Henrique. "Produção de lacases pelo fungo filamentoso de origem marinha Peniophora sp. CBMAI 1063 em biorreator de bancada /." Rio Claro, 2015. http://hdl.handle.net/11449/134175.

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Orientador: Lara Durães Sette<br>Coorientador: Rafaella Bonugli Santos<br>Banca: Luiz Henrique Souza Guimarães<br>Banca: Eleonora Cano Carmona<br>Resumo: As lacases são enzimas que catalisam uma reação que oxida moléculas aromáticas fenólicas. Com grande potencial biotecnológico, as lacases podem ser empregadas em diversos setores industriais. Suas principais aplicações são referentes a indústria de polpa e papel, têxtil, alimentícia, bem como na química sintética e biorremediação. Em estudos prévios, o fungo basidiomiceto Peniophora sp. CBMAI 1063, isolado da esponja marinha Amphimedon viridi
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Zaccaria, Simone. "Concentração, formulação e caracterização de extratos enzimáticos de lacases produzidas por Pleurotus sajor-caju PS-2001 em processo submerso." reponame:Repositório Institucional da UCS, 2017. https://repositorio.ucs.br/handle/11338/3446.

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Submitted by cmquadros@ucs.br (cmquadros@ucs.br) on 2018-02-02T10:31:31Z No. of bitstreams: 1 Dissertacao Simone Zaccaria.pdf: 993465 bytes, checksum: 0a1335797da601a4322d237b9b0aee3a (MD5)<br>Made available in DSpace on 2018-02-02T10:31:31Z (GMT). No. of bitstreams: 1 Dissertacao Simone Zaccaria.pdf: 993465 bytes, checksum: 0a1335797da601a4322d237b9b0aee3a (MD5) Previous issue date: 2018-02-01<br>Coordenação de Aperfeiçoamento de Pessoal de Nível Superior, CAPES
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Haynes, Kaaren K. "Physical properties of laccase-mediator delignified pulps." Diss., Georgia Institute of Technology, 1998. http://hdl.handle.net/1853/5884.

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Bertrand, Thomas. "Etude structurale et fonctionnelle d'enzymes : la cytidine monophosphate kinase d'Escherichia coli, la laccase de Trametes versicolor, et la désoxyribose mutarotase de Salmonella typhimurium." Paris 6, 2002. http://www.theses.fr/2002PA066036.

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Lanteigne, Roch Lisa-Marie. "Utilisation des enzymes lipase et laccase pour améliorer la blancheur d'une pâte désencrée de papier journal." Thèse, Université du Québec à Trois-Rivières, 2010. http://depot-e.uqtr.ca/2005/1/030140241.pdf.

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Chakar, Fadi S. "Fundamental delignification chemistry of laccase-mediator systems on high-lignin-content kraft pulps." Diss., Georgia Institute of Technology, 2001. http://hdl.handle.net/1853/7017.

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Books on the topic "Enzymes. Enzymes Peniophora. Laccase"

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Kiiskinen, Laura-Leena. Characterization and heterologous production of a novel laccase from Melanocarpus albomyces. VTT Technical Research Centre of Finland, 2004.

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Lantto, R. Protein cross-linking with oxidative enzymes and transglutaminase: Effects in meat protein systems. VTT Technical Research Centre of Finland, 2007.

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Harris, Amanda. Laccase: Applications, Investigations and Insights. Nova Science Publishers, Incorporated, 2017.

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Book chapters on the topic "Enzymes. Enzymes Peniophora. Laccase"

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Yesilada, Ozfer, Emre Birhanli, and Hikmet Geckil. "Bioremediation and Decolorization of Textile Dyes by White Rot Fungi and Laccase Enzymes." In Fungal Biology. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-77386-5_5.

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Reinhammar, Bengt. "Laccase." In Copper Proteins and Copper Enzymes. CRC Press, 2018. http://dx.doi.org/10.1201/9781351070898-1.

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Srivastava, Neha, P. K. Mishra, and S. N. Upadhyay. "Laccase: use in removal of lignin in cellulosic biomass." In Industrial Enzymes for Biofuels Production. Elsevier, 2020. http://dx.doi.org/10.1016/b978-0-12-821010-9.00007-3.

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Forootanfar, Hamid, Shokouh Arjmand, Mina Behzadi, and Mohammad Ali Faramarzi. "Laccase-Mediated Treatment of Pharmaceutical Wastes." In Research Advancements in Pharmaceutical, Nutritional, and Industrial Enzymology. IGI Global, 2018. http://dx.doi.org/10.4018/978-1-5225-5237-6.ch010.

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Laccases are versatile multi-copper enzymes belonging to the superfamily of oxidase enzymes, which have been known since the nineteenth century. Recent discoveries have refined investigators' views of the potential of laccase as a magic tool for remarkable biotechnological purposes. A literature review of the capabilities of laccases, their assorted substrates, and their molecular mechanism of action now indicates the emergence of a new direction for laccase application as part of an arsenal in the fight against the contamination of water supplies by a number of frequently prescribed medications. This chapter provides a critical review of the literature and reveals the pivotal role of laccases in the elimination and detoxification of pharmaceutical contaminants in aquatic environments and wastewaters.
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Singh, Rajender, and Mamta Chauhan. "Effective Management of Agro-Industrial Residues as Composting in Mushroom Industry and Utilization of Spent Mushroom Substrate for Bioremediation." In Advances in Environmental Engineering and Green Technologies. IGI Global, 2016. http://dx.doi.org/10.4018/978-1-4666-9734-8.ch008.

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Different types of edible mushrooms like Agaricus, bisporus, A. bitoriqus, Pleurotus spp., Volvariella volvacea, Lentinula edodes, Calocybe indica, Flamullina, Ganoderma lucidum etc. are cultivated in industrial scale. Majority of edible fungi secretes extracellular Ligninocellulolytic enzymes like Laccase, lignin peroxidase, manganese peroxidase, cellulase etc. for effective conversion of ligninocellulolytic substrate to compositing form which led to fruiting of mushrooms. Consequently, an adequate disposal method is needed for the high quantities of spent mushroom substrate (SMS) generated in this agro-food industrial activity. On the other side, textile industry among the largest water consuming industries in the world and approximately, 10,000 different dyes and pigments are used at industrial scale. It is estimated that nearly 40% of the total dyes used in the dyeing process may find their way in wastewater. So, there is an attempt to utilize the ligninolytic enzymes rich SMS of different mushroom for efficiently biodegradation of textile wastewater &amp; polyaromatic pollutants.
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Singh, Rajender, and Mamta Chauhan. "Effective Management of Agro-Industrial Residues as Composting in Mushroom Industry and Utilization of Spent Mushroom Substrate for Bioremediation." In Waste Management. IGI Global, 2020. http://dx.doi.org/10.4018/978-1-7998-1210-4.ch055.

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Different types of edible mushrooms like Agaricus, bisporus, A. bitoriqus, Pleurotus spp., Volvariella volvacea, Lentinula edodes, Calocybe indica, Flamullina, Ganoderma lucidum etc. are cultivated in industrial scale. Majority of edible fungi secretes extracellular Ligninocellulolytic enzymes like Laccase, lignin peroxidase, manganese peroxidase, cellulase etc. for effective conversion of ligninocellulolytic substrate to compositing form which led to fruiting of mushrooms. Consequently, an adequate disposal method is needed for the high quantities of spent mushroom substrate (SMS) generated in this agro-food industrial activity. On the other side, textile industry among the largest water consuming industries in the world and approximately, 10,000 different dyes and pigments are used at industrial scale. It is estimated that nearly 40% of the total dyes used in the dyeing process may find their way in wastewater. So, there is an attempt to utilize the ligninolytic enzymes rich SMS of different mushroom for efficiently biodegradation of textile wastewater &amp; polyaromatic pollutants.
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Kushwaha, Ankita, Shweta Maurya, Ravi Kant Pathak, Sonam Agarwal, Pankaj Kumar Chaurasia, and M. P. Singh. "Laccase From White Rot Fungi Having Significant Role in Food, Pharma, and Other Industries." In Research Advancements in Pharmaceutical, Nutritional, and Industrial Enzymology. IGI Global, 2018. http://dx.doi.org/10.4018/978-1-5225-5237-6.ch011.

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Laccases (E.C. 1.10.3.2 benzenediol: oxygen oxidoreductase) are an interesting group of N glycosylated multicopper blue oxidase enzymes and the widely studied enzyme having a broad range of substrate specificity of both phenolic and non-phenolic compounds. They are widely found in fungi, bacteria plant, insects, and in lichen. They catalyze the oxidation of various phenolic and non-phenolic compounds, with the concomitant reduction of molecular oxygen to water. They could increase productivity, efficiency, and quality of products without a costly investment. This chapter depicts the applications of laccase enzyme from white rot fungi, having various industrial (such as textile dye bleaching, paper and pulp bleaching, food includes the baking, it also utilized in fruit juice industry to improve the quality and stabilization of some perishable products having plant oils), pharmaceutical (as it has potential for the synthesis of several useful drugs such anticancerous, antioxidants, synthesis of hormone derivatives because of their high value of oxidation potential) significance.
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Sasaki, Keiko, and Kojo T. Konadu. "Biotechnological Approaches to Facilitate Gold Recovery from Double Refractory Gold Ores." In Biotechnology in Mining and Metallurgical Industry [Working Title]. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.94334.

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Double refractory gold ore (DRGO) not only include ppt levels of gold grains locked in sulfide minerals but also a problematic amount of carbonaceous matter. This causes a significant recovery loss of gold during cyanidation because of the strong affinity of the Au(CN)2 − with the carbonaceous matter. Combustion decreases the carbonaceous matter content, but also emits pollutant gases like CO2, SO2 and As2O3. Therefore, environmentally-friendly solutions have been explored by using biotechnology. Due to the very small amount of the above targets in the ore, it is challenging to show evidential changes in solid-phase before and after the biomineral processing of DRGO. This chapter introduces the mineralogical and chemical changes in the various solid residues produced during a sequential biotreatment, consisting of the liberation of gold from sulfides by an iron-oxidizer and decomposition of carbonaceous matter by lignin-degrading enzymes (lignin peroxidase, manganese peroxidase, laccase) secreted from a white rot-fungus, which successfully improved of gold recovery to over 90%. In addition, further development of biotechnology in the recovery of gold from DRGO is addressed.
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Taber, Douglass F. "Developments in Flow Chemistry." In Organic Synthesis. Oxford University Press, 2017. http://dx.doi.org/10.1093/oso/9780190646165.003.0017.

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Klavs S. Jensen of MIT showed (Angew. Chem. Int. Ed. 2014, 53, 470) that “batch” kinetics could be developed in flow by online IR analysis and continuous control. Professor Jensen also demonstrated (Org. Process Res. Dev. 2014, 18, 402) the contin­uous flow production of an active pharmaceutical product, the direct renin inhibitor aliskiren, over two steps and two crystallizations, starting from two advanced interme­diates. Michael Werner and Rainer E. Martin of Hoffmann-La Roche AG Basel com­bined (Angew. Chem. Int. Ed. 2014, 53, 1704) flow synthesis with a flow-based bioassay to develop structure–activity relationships for a series of β-secretase inhibitors. Carlos Mateos of Lilly S. A. and C. Oliver Kappe of the University of Graz used (J. Org. Chem. 2014, 79, 223) flow photolysis to promote the bromination of 1 to 2. Alessandro Palmieri of the University of Camerino and Stefano Protti of the University of Pavia added (Adv. Synth. Catal. 2014, 356, 753) the aldehyde 3 to the acceptor 4 to give, after in-flow reduction, the lactone 5. Peter H. Seeberger of the Max Planck Institute Mühlenberg showed (Org. Lett. 2014, 16, 1794) that the tum­bling action of flow photolysis made the production of 7 by the unlinking of 6 from the polymer bead particularly efficient. Enzymes can also be used under flow conditions. Jörg Pietruszka of the Heinrich-Heine-Universität Düsseldorf employed (Adv. Synth. Catal. 2014, 356, 1007) com­mercial laccase to prepare 10 by coupling 8 with 9. Gas–liquid mixing under flow conditions can also be effective. Núria López of ICIQ Catalonia and Javier Pérez-Ramírez of ETH Zurich developed (Chem. Eur J. 2014, 20, 5926) conditions for the selective hydrogenation of an alkyne 11 to the cis alkene 12. Jun-ichi Yoshida of Kyoto University trapped (Chem. Eur J. 2014, 20, 7931) the inter­mediate organolithium from 13 with CO₂ to give a carboxylate that was carried on to the purifiable O-Su ester 14, ready for further coupling. Timothy F. Jamison, also of MIT, prepared (Angew. Chem. Int. Ed. 2014, 53, 3353) the amino phenol 17 by add­ing the chloromagnesium amide from 16 to the intermediate benzyne from 15, then oxidizing the product with air.
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Conference papers on the topic "Enzymes. Enzymes Peniophora. Laccase"

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Long-ho Chau, Ken C. F. Leung, and Wen J. Li. "Investigation of GDH/ laccase enzymes for bio-energy generation systems." In 2009 International Conference on Mechatronics and Automation (ICMA). IEEE, 2009. http://dx.doi.org/10.1109/icma.2009.5245001.

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Kupryashina, M. A., T. E. Pylaev, and V. E. Nikitina. "The influence of malachite green on the level of transcriptional expression of the laccase and DyP-peroxidase genes of the Azospirillum brasilense." In 2nd International Scientific Conference "Plants and Microbes: the Future of Biotechnology". PLAMIC2020 Organizing committee, 2020. http://dx.doi.org/10.28983/plamic2020.142.

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Malachite green (MG), a widely-used and recalcitrant dye, has been confirmed to be carcinogenic and mutagenic against many organisms. Herein, we were aimed at the investigation of the hypothetic role of ligninolytic bacterial enzymes similar to fungal ones in the degradation of synthetic dyes. A multiple increase in the laccases and DyP-peroxidases genes expression level was recorded by RT-qPCR for bacteria of the genus Azospirillum in the presence of MG.
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