Zobrazeno 1 - 10
of 236
pro vyhledávání: '"Melanocarpus albomyces"'
Autor:
Ulrich Schwaneberg, Jasmin Eidner, Gaurao V. Dhoke, Ronny Martinez, Catalina Novoa, Patrick Lorenz, Diana M. Mate, Ruth Schwerdtfeger, Mehdi D. Davari, Thomas Haarmann, Felix Jakob, Martina Schreiter
Publikováno v:
ChemBioChem. 20:1458-1466
To date, commercial laccase preparations are used in the food, textile, and paper and pulp industries (mild pH). Laccases are attractive in the synthesis of dye molecules or oxidative lignin treatment, which take place at high pH (≥8.0). So far, on
Autor:
Jesper Vind, Gerard Santiago, Sibel Kilic, Joan Gilabert, Ángel T. Martínez, Victor Guallar, Felipe de Salas, Susana Camarero, Pablo Aza, Mehmet E. Sener
Publikováno v:
Green Chemistry
Digital.CSIC. Repositorio Institucional del CSIC
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Digital.CSIC. Repositorio Institucional del CSIC
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12 p.-12 fig.-1 tab.
Fungal laccases can play an important role as biocatalysts in organic chemistry to replace chemical synthesis. In a previous work we synthesized conductive polyaniline using a high-redox potential laccase from our collection
Fungal laccases can play an important role as biocatalysts in organic chemistry to replace chemical synthesis. In a previous work we synthesized conductive polyaniline using a high-redox potential laccase from our collection
Akademický článek
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Akademický článek
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Autor:
Laura-Leena Kiiskinen, Markku Saloheimo, Anu Koivula, Kristiina Kruus, Nina Hakulinen, Arja Paananen, Juha Rouvinen
Publikováno v:
Hakulinen, N, Kiiskinen, L-L, Kruus, K, Saloheimo, M, Paananen, A, Koivula, A & Rouvinen, J 2002, ' Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site ', Nature Structural Biology, vol. 9, no. 8, pp. 601-605 . https://doi.org/10.1038/nsb823
We have crystallized the ascomycete laccase from Melanocarpus albomyces with all four coppers present and determined the crystal structure at 2.4 Å resolution. The enzyme is heavily glycosylated and consists of three cupredoxin-like domains, similar
Autor:
Stefan Willför, Annika Smeds, Liisa Viikari, Jussi Sipilä, Maija-Liisa Mattinen, Jussi Kontro, Pekka Maijala, Tarja Tamminen, Paula Nousiainen
Publikováno v:
Mattinen, M-L, Maijala, P, Nousiainen, P, Smeds, A, Kontro, J, Sipilä, J, Tamminen, T, Willför, S & Viikari, L 2011, ' Oxidation of lignans and lignin model compounds by laccase in aqueous solvent systems ', Journal of Molecular Catalysis B: Enzymatic, vol. 72, no. 3-4, pp. 122-129 . https://doi.org/10.1016/j.molcatb.2011.05.009
The stability and activity of the low redox potential Melanocarpus albomyces laccase (MaL) in various aqueous organic (acetone, ethanol, propylene glycol, diethylene glycol monomethyl ether) solvent systems was studied spectrophotometrically using 2,
Autor:
Jari Vehmaanperä, Matti Siika-aho, Kati Réczey, Marika Alapuranen, Nóra Szijártó, Liisa Viikari, Maija Tenkanen
Publikováno v:
Szijártó, N, Siika-aho, M, Tenkanen, M, Alapuranen, M, Vehmaanperä, J, Réczey, K & Viikari, L 2008, ' Hydrolysis of amorphous and crystalline cellulose by heterologously produced cellulases of Melanocarpus albomyces ', Journal of Biotechnology, vol. 136, no. 3-4, pp. 140-147 . https://doi.org/10.1016/j.jbiotec.2008.05.010
Three thermostable neutral cellulases from Melanocarpus albomyces, a 20-kDa endoglucanase (Cel45A), a 50-kDa endoglucanase (Cel7A), and a 50-kDa cellobiohydrolase (Cel7B) heterologously produced in a recombinant Trichoderma reesei were purified and s
Publikováno v:
Hakulinen, N, Andberg, M, Kallio, J, Koivula, A, Kruus, K & Rouvinen, J 2008, ' A near atomic resolution structure of a Melanocarpus albomyces laccase ', Journal of Structural Biology, vol. 162, no. 1, pp. 29-39 . https://doi.org/10.1016/j.jsb.2007.12.003
We have solved a crystal structure from Melanocarpus albomyces laccase expressed in the filamentous fungus Trichoderma reesei (rMaL) at 1.3 Å resolution by using synchrotron radiation at 100 K. At the moment, this is the highest resolution that has
Autor:
Jari Vehmaanperä, Harry Boer, Markus Linder, Juha Rouvinen, Anu Koivula, Sanni Voutilainen, Terhi Puranen
Publikováno v:
Voutilainen, S, Boer, H, Linder, M, Puranen, T, Rouvinen, J, Vehmaanperä, J & Koivula, A 2007, ' Heterologous expression of Melanocarpus albomyces cellobiohydrolase Cel7B, and random mutagenesis to improve its thermostability ', Enzyme and Microbial Technology, vol. 41, no. 3, pp. 234-243 . https://doi.org/10.1016/j.enzmictec.2007.01.015
Fungal cellobiohydrolases from the glycosyl hydrolase family 7 are key enzymes in crystalline cellulose hydrolysis. Difficulties in heterologous expression in a bacterial or yeast host have hampered engineering of these cellulases for industrial appl
Publikováno v:
Kontkanen, H, Reinikainen, T & Saloheimo, M 2006, ' Cloning and expression of a Melanocarpus albomyces steryl esterase gene in Pichia pastoris and Trichoderma reesei ', Biotechnology and Bioengineering, vol. 94, no. 3, pp. 407-415 . https://doi.org/10.1002/bit.20686
The ste1 gene encoding a steryl esterase was isolated from the thermophilic fungus Melanocarpus albomyces. The gene has one intron, and it encodes a protein consisting of 576 amino acids. The deduced amino acid sequence of the steryl esterase was sho