Biochemical and molecular characterization of <i>Coriolopsis rigida</i> laccases involved in transformation of the solid waste from olive oil production

Two laccase isoenzymes were purified and characterized from the basidiomycete <i>Coriolopsis rigida</i> during transformation of the water-soluble fraction of “alpeorujo” (WSFA), a solid residue derived from the olive oil production containing high levels of toxic compounds. Zymogram ass...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Díaz, Rosario, Saparrat, Mario Carlos Nazareno, Jurado, Miguel, García Romera, Inmaculada, Ocampo, Juan Antonio, Martínez, María Jesús
Formato: Articulo
Lenguaje:Inglés
Publicado: 2010
Materias:
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/132709
Aporte de:
id I19-R120-10915-132709
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Naturales
Olive-mill waste
Basidiomycetes
Phenol
Gene sequence
spellingShingle Ciencias Naturales
Olive-mill waste
Basidiomycetes
Phenol
Gene sequence
Díaz, Rosario
Saparrat, Mario Carlos Nazareno
Jurado, Miguel
García Romera, Inmaculada
Ocampo, Juan Antonio
Martínez, María Jesús
Biochemical and molecular characterization of <i>Coriolopsis rigida</i> laccases involved in transformation of the solid waste from olive oil production
topic_facet Ciencias Naturales
Olive-mill waste
Basidiomycetes
Phenol
Gene sequence
description Two laccase isoenzymes were purified and characterized from the basidiomycete <i>Coriolopsis rigida</i> during transformation of the water-soluble fraction of “alpeorujo” (WSFA), a solid residue derived from the olive oil production containing high levels of toxic compounds. Zymogram assays of laccases secreted by the fungus growing on WSFA and WSFA supplemented with glucose showed two bands with isoelectric points of 3.3 and 3.4. The kinetic studies of the two purified isoenzymes showed similar affinity on 2,6-dimethoxyphenol and 2,2′-azinobis-(3-ethylbenzthiazoline-6-sulfonic acid), used as phenolic and non-phenolic model substrate, respectively. The molecular mass of both proteins was 66 kDa with 9% N-linked carbohydrate. Physico-chemical properties of the purified laccases from media containing WSFA were similar to those obtained from medium with glucose as the main carbon source. In-vitro studies performed with the purified laccases revealed a 42% phenol reduction of WSFA, as well as changes in the molecular mass distribution. These findings indicate that these laccases are involved in the process of transformation, via polymerization by the oxidation of phenolic compounds present in WSFA. A single laccase gene, containing an open reading frame of 1,488 bp, was obtained in PCR amplifications performed with cDNA extracted from mycelia grown on WSFA. The product of the gene shares 90% identity (95% similarity) with a laccase from <i>Trametes trogii</i> and 89% identity (95% similarity) with a laccase from <i>Coriolopsis gallica</i>. This is the first report on purification and molecular characterization of laccases directly involved in the transformation of olive oil residues.
format Articulo
Articulo
author Díaz, Rosario
Saparrat, Mario Carlos Nazareno
Jurado, Miguel
García Romera, Inmaculada
Ocampo, Juan Antonio
Martínez, María Jesús
author_facet Díaz, Rosario
Saparrat, Mario Carlos Nazareno
Jurado, Miguel
García Romera, Inmaculada
Ocampo, Juan Antonio
Martínez, María Jesús
author_sort Díaz, Rosario
title Biochemical and molecular characterization of <i>Coriolopsis rigida</i> laccases involved in transformation of the solid waste from olive oil production
title_short Biochemical and molecular characterization of <i>Coriolopsis rigida</i> laccases involved in transformation of the solid waste from olive oil production
title_full Biochemical and molecular characterization of <i>Coriolopsis rigida</i> laccases involved in transformation of the solid waste from olive oil production
title_fullStr Biochemical and molecular characterization of <i>Coriolopsis rigida</i> laccases involved in transformation of the solid waste from olive oil production
title_full_unstemmed Biochemical and molecular characterization of <i>Coriolopsis rigida</i> laccases involved in transformation of the solid waste from olive oil production
title_sort biochemical and molecular characterization of <i>coriolopsis rigida</i> laccases involved in transformation of the solid waste from olive oil production
publishDate 2010
url http://sedici.unlp.edu.ar/handle/10915/132709
work_keys_str_mv AT diazrosario biochemicalandmolecularcharacterizationoficoriolopsisrigidailaccasesinvolvedintransformationofthesolidwastefromoliveoilproduction
AT saparratmariocarlosnazareno biochemicalandmolecularcharacterizationoficoriolopsisrigidailaccasesinvolvedintransformationofthesolidwastefromoliveoilproduction
AT juradomiguel biochemicalandmolecularcharacterizationoficoriolopsisrigidailaccasesinvolvedintransformationofthesolidwastefromoliveoilproduction
AT garciaromerainmaculada biochemicalandmolecularcharacterizationoficoriolopsisrigidailaccasesinvolvedintransformationofthesolidwastefromoliveoilproduction
AT ocampojuanantonio biochemicalandmolecularcharacterizationoficoriolopsisrigidailaccasesinvolvedintransformationofthesolidwastefromoliveoilproduction
AT martinezmariajesus biochemicalandmolecularcharacterizationoficoriolopsisrigidailaccasesinvolvedintransformationofthesolidwastefromoliveoilproduction
bdutipo_str Repositorios
_version_ 1764820454260867072