Cargando…

Purification and Characterization of Two Novel Laccases from Peniophora lycii

Although, currently, more than 100 laccases have been purified from basidiomycete fungi, the majority of these laccases were obtained from fungi of the Polyporales order, and only scarce data are available about the laccases from other fungi. In this article, laccase production by the white-rot basi...

Descripción completa

Detalles Bibliográficos
Autores principales: Glazunova, Olga A., Moiseenko, Konstantin V., Savinova, Olga S., Fedorova, Tatyana V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7762197/
https://www.ncbi.nlm.nih.gov/pubmed/33291231
http://dx.doi.org/10.3390/jof6040340
_version_ 1783627747804839936
author Glazunova, Olga A.
Moiseenko, Konstantin V.
Savinova, Olga S.
Fedorova, Tatyana V.
author_facet Glazunova, Olga A.
Moiseenko, Konstantin V.
Savinova, Olga S.
Fedorova, Tatyana V.
author_sort Glazunova, Olga A.
collection PubMed
description Although, currently, more than 100 laccases have been purified from basidiomycete fungi, the majority of these laccases were obtained from fungi of the Polyporales order, and only scarce data are available about the laccases from other fungi. In this article, laccase production by the white-rot basidiomycete fungus Peniophora lycii, belonging to the Russulales order, was investigated. It was shown that, under copper induction, this fungus secreted three different laccase isozymes. Two laccase isozymes—Lac5 and LacA—were purified and their corresponding nucleotide sequences were determined. Both purified laccases were relatively thermostable with periods of half-life at 70 °C of 10 and 8 min for Lac5 and LacA, respectively. The laccases demonstrated the highest activity toward ABTS (97 U·mg(−1) for Lac5 and 121 U·mg(−1) for LacA at pH 4.5); Lac5 demonstrated the lowest activity toward 2,6-DMP (2.5 U·mg(−1) at pH 4.5), while LacA demonstrated this towards gallic acid (1.4 U·mg(−1) at pH 4.5). Both Lac5 and LacA were able to efficiently decolorize such dyes as RBBR and Bromcresol Green. Additionally, phylogenetic relationships among laccases of Peniophora spp. were reconstructed, and groups of orthologous genes were determined. Based on these groups, all currently available data about laccases of Peniophora spp. were systematized.
format Online
Article
Text
id pubmed-7762197
institution National Center for Biotechnology Information
language English
publishDate 2020
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-77621972020-12-26 Purification and Characterization of Two Novel Laccases from Peniophora lycii Glazunova, Olga A. Moiseenko, Konstantin V. Savinova, Olga S. Fedorova, Tatyana V. J Fungi (Basel) Article Although, currently, more than 100 laccases have been purified from basidiomycete fungi, the majority of these laccases were obtained from fungi of the Polyporales order, and only scarce data are available about the laccases from other fungi. In this article, laccase production by the white-rot basidiomycete fungus Peniophora lycii, belonging to the Russulales order, was investigated. It was shown that, under copper induction, this fungus secreted three different laccase isozymes. Two laccase isozymes—Lac5 and LacA—were purified and their corresponding nucleotide sequences were determined. Both purified laccases were relatively thermostable with periods of half-life at 70 °C of 10 and 8 min for Lac5 and LacA, respectively. The laccases demonstrated the highest activity toward ABTS (97 U·mg(−1) for Lac5 and 121 U·mg(−1) for LacA at pH 4.5); Lac5 demonstrated the lowest activity toward 2,6-DMP (2.5 U·mg(−1) at pH 4.5), while LacA demonstrated this towards gallic acid (1.4 U·mg(−1) at pH 4.5). Both Lac5 and LacA were able to efficiently decolorize such dyes as RBBR and Bromcresol Green. Additionally, phylogenetic relationships among laccases of Peniophora spp. were reconstructed, and groups of orthologous genes were determined. Based on these groups, all currently available data about laccases of Peniophora spp. were systematized. MDPI 2020-12-06 /pmc/articles/PMC7762197/ /pubmed/33291231 http://dx.doi.org/10.3390/jof6040340 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Glazunova, Olga A.
Moiseenko, Konstantin V.
Savinova, Olga S.
Fedorova, Tatyana V.
Purification and Characterization of Two Novel Laccases from Peniophora lycii
title Purification and Characterization of Two Novel Laccases from Peniophora lycii
title_full Purification and Characterization of Two Novel Laccases from Peniophora lycii
title_fullStr Purification and Characterization of Two Novel Laccases from Peniophora lycii
title_full_unstemmed Purification and Characterization of Two Novel Laccases from Peniophora lycii
title_short Purification and Characterization of Two Novel Laccases from Peniophora lycii
title_sort purification and characterization of two novel laccases from peniophora lycii
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7762197/
https://www.ncbi.nlm.nih.gov/pubmed/33291231
http://dx.doi.org/10.3390/jof6040340
work_keys_str_mv AT glazunovaolgaa purificationandcharacterizationoftwonovellaccasesfrompeniophoralycii
AT moiseenkokonstantinv purificationandcharacterizationoftwonovellaccasesfrompeniophoralycii
AT savinovaolgas purificationandcharacterizationoftwonovellaccasesfrompeniophoralycii
AT fedorovatatyanav purificationandcharacterizationoftwonovellaccasesfrompeniophoralycii