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...
Autores principales: | , , , |
---|---|
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 |