Subir material

Suba sus trabajos a SEDICI, para mejorar notoriamente su visibilidad e impacto

 

Mostrar el registro sencillo del ítem

dc.date.accessioned 2020-10-23T19:52:44Z
dc.date.available 2020-10-23T19:52:44Z
dc.date.issued 2002
dc.identifier.uri http://sedici.unlp.edu.ar/handle/10915/107657
dc.description.abstract Previous work has shown that the white rot fungus Coriolopsis rigida degraded wheat straw lignin and both the aliphatic and aromatic fractions of crude oil from contaminated soils. To better understand these processes, we studied the enzymatic composition of the ligninolytic system of this fungus. Since laccase was the sole ligninolytic enzyme found, we paid attention to the oxidative capabilities of this enzyme that would allow its participation in the mentioned degradative processes. We purified two laccase isoenzymes to electrophoretic homogeneity from copper-induced cultures. Both enzymes are monomeric proteins, with the same molecular mass (66 kDa), isoelectric point (3.9), N-linked carbohydrate content (9%), pH optima of 3.0 on 2,6-dimethoxyphenol (DMP) and 2.5 on 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), absorption spectrum, and N-terminal amino acid sequence. They oxidized 4-anisidine and numerous phenolic compounds, including methoxyphenols, hydroquinones, and lignin-derived aldehydes and acids. Phenol red, an unusual substrate of laccase due to its high redox potential, was also oxidized. The highest enzyme affinity and efficiency were obtained with ABTS and, among phenolic compounds, with 2,6-dimethoxyhydroquinone (DBQH2). The presence of ABTS in the laccase reaction expanded the substrate range of C. rigida laccases to nonphenolic compounds and that of MBQH2 extended the reactions catalyzed by these enzymes to the production of H2O2, the oxidation of Mn2+, the reduction of Fe3+, and the generation of hydroxyl radicals. These results confirm the participation of laccase in the production of oxygen free radicals, suggesting novel uses of this enzyme in degradative processes. en
dc.format.extent 1534-1540 es
dc.language en es
dc.subject Coriolopsis rigida es
dc.subject laccase es
dc.title Induction, isolation, and characterization of two laccases from the white rot basidiomycete Coriolopsis rigida en
dc.type Articulo es
sedici.identifier.uri http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC123844&blobtype=pdf es
sedici.identifier.uri https://aem.asm.org/content/68/4/1534 es
sedici.identifier.other pmid:11916665 es
sedici.identifier.other pmcid:PMC123844 es
sedici.identifier.other http://dx.doi.org/10.1128/aem.68.4.1534-1540.2002 es
sedici.identifier.issn 1098-5336 es
sedici.creator.person Saparrat, Mario Carlos Nazareno es
sedici.creator.person Guillén, Francisco es
sedici.creator.person Arambarri, Angélica Margarita es
sedici.creator.person Martínez, Angel T. es
sedici.creator.person Martínez, María Jesús es
sedici.subject.materias Ciencias Naturales es
sedici.subject.materias Botánica es
sedici.description.fulltext true es
mods.originInfo.place Facultad de Ciencias Naturales y Museo es
mods.originInfo.place Instituto de Botánica "Dr. Carlos Spegazzini" es
sedici.subtype Articulo es
sedici.rights.license Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
sedici.rights.uri http://creativecommons.org/licenses/by-nc-sa/4.0/
sedici.description.peerReview peer-review es
sedici.relation.journalTitle Applied and Environmental Microbiology es
sedici.relation.journalVolumeAndIssue vol. 68, no. 4 es


Descargar archivos

Este ítem aparece en la(s) siguiente(s) colección(ones)

Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) Excepto donde se diga explícitamente, este item se publica bajo la siguiente licencia Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)