Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Felipe de Salas"'
Autor:
David Rodríguez-Escribano, Rocío Pliego-Magán, Felipe de Salas, Pablo Aza, Patrizia Gentili, Petri Ihalainen, Thomas Levée, Valérie Meyer, Michel Petit-Conil, Sandra Tapin-Lingua, Michael Lecourt, Susana Camarero
Publikováno v:
Biotechnology for Biofuels and Bioproducts, Vol 15, Iss 1, Pp 1-19 (2022)
Abstract Background During the kraft process to obtain cellulosic pulp from wood, most of the lignin is removed by high-temperature alkaline cooking, released in the black liquors and usually incinerated for energy. However, kraft lignins are a valua
Externí odkaz:
https://doaj.org/article/3f6fbd1d7fe04c4a84040e8e47faeaad
Autor:
David Rodríguez-Escribano, Felipe de Salas, Rocío Pliego, Gisela Marques, Thomas Levée, Anu Suonpää, Ana Gutiérrez, Ángel T. Martínez, Petri Ihalainen, Jorge Rencoret, Susana Camarero
Publikováno v:
Polymers, Vol 15, Iss 22, p 4433 (2023)
Lignins released in the black liquors of kraft pulp mills are an underutilised source of aromatics. Due to their phenol oxidase activity, laccases from ligninolytic fungi are suitable biocatalysts to depolymerise kraft lignins, which are characterise
Externí odkaz:
https://doaj.org/article/482eabc16a8a46a6b021156599966cc2
Autor:
Isabel Pardo, David Rodríguez-Escribano, Pablo Aza, Felipe de Salas, Angel T. Martínez, Susana Camarero
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-10 (2018)
Abstract The robustness of a high-redox potential laccase has been enhanced by swapping its second cupredoxin domain with that from another fungal laccase, which introduced a pool of neutral mutations in the protein sequence without affecting enzyme
Externí odkaz:
https://doaj.org/article/d95467d880f942c59297af612d813c18
Autor:
Pablo Aza, Felipe de Salas, Gonzalo Molpeceres, David Rodríguez-Escribano, Iñigo de la Fuente, Susana Camarero
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 3, p 1157 (2021)
Laccases secreted by saprotrophic basidiomycete fungi are versatile biocatalysts able to oxidize a wide range of aromatic compounds using oxygen as the sole requirement. Saccharomyces cerevisiae is a preferred host for engineering fungal laccases. To
Externí odkaz:
https://doaj.org/article/50065c23c4de4847a771e6cd53f1867c
Autor:
Felipe de Salas, Isabel Pardo, Horacio J Salavagione, Pablo Aza, Eleni Amougi, Jesper Vind, Angel T Martínez, Susana Camarero
Publikováno v:
PLoS ONE, Vol 11, Iss 10, p e0164958 (2016)
Polyaniline is a conductive polymer with distinctive optical and electrical properties. Its enzymatic synthesis is an environmentally friendly alternative to the use of harsh oxidants and extremely acidic conditions. 7D5L, a high-redox potential lacc
Externí odkaz:
https://doaj.org/article/6f5b6bc610fc42449014aab284798162
Publikováno v:
International Journal of Molecular Sciences, Vol 18, Iss 8, p 1793 (2017)
Lignin valorization is a pending issue for the integrated conversion of lignocellulose in consumer goods. Lignosulfonates (LS) are the main technical lignins commercialized today. However, their molecular weight should be enlarged to meet application
Externí odkaz:
https://doaj.org/article/dad0c9beef144ad4a8a3280c24a793c4
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
instname
Digital.CSIC. Repositorio Institucional del CSIC
instname
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
Autor:
Pablo, Aza, Felipe, de Salas, Gonzalo, Molpeceres, David, Rodríguez-Escribano, Iñigo, de la Fuente, Susana, Camarero
Publikováno v:
International Journal of Molecular Sciences
Laccases secreted by saprotrophic basidiomycete fungi are versatile biocatalysts able to oxidize a wide range of aromatic compounds using oxygen as the sole requirement. Saccharomyces cerevisiae is a preferred host for engineering fungal laccases. To
Autor:
Alicia Virseda-Jerez, Ángel T. Martínez, Felipe de Salas, Gerard Santiago, Patrizia Gentili, Jesper Vind, Rubén Cañadas, Victor Guallar, Susana Camarero, Inés G. Muñoz
Publikováno v:
International Journal of Biological Macromolecules
Digital.CSIC. Repositorio Institucional del CSIC
instname
Digital.CSIC. Repositorio Institucional del CSIC
instname
13 p.-7 fig.-2 tab
Fungal laccases have great potential as biocatalysts oxidizing a variety of aromatic compounds using oxygen as co-substrate. Here, the crystal structure of 7D5 laccase (PDB 6H5Y), developed in Saccharomyces cerevisiae and over
Fungal laccases have great potential as biocatalysts oxidizing a variety of aromatic compounds using oxygen as co-substrate. Here, the crystal structure of 7D5 laccase (PDB 6H5Y), developed in Saccharomyces cerevisiae and over
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62e40266ff9c108ec2a7f236d0166801
http://hdl.handle.net/10261/190477
http://hdl.handle.net/10261/190477
Autor:
Ángel T. Martínez, Felipe de Salas, Pablo Aza, Susana Camarero, Isabel Pardo, David Rodríguez-Escribano
Publikováno v:
Scientific Reports
Digital.CSIC. Repositorio Institucional del CSIC
instname
Scientific Reports, Vol 8, Iss 1, Pp 1-10 (2018)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Scientific Reports, Vol 8, Iss 1, Pp 1-10 (2018)
10 p.-4 fig.-3 tab.
The robustness of a high-redox potential laccase has been enhanced by swapping its second cupredoxin domain with that from another fungal laccase, which introduced a pool of neutral mutations in the protein sequence without a
The robustness of a high-redox potential laccase has been enhanced by swapping its second cupredoxin domain with that from another fungal laccase, which introduced a pool of neutral mutations in the protein sequence without a