The Role of Laccase from Zygomycetous Fungus <i>Mortierella elasson</i> in Humic Acids Degradation

Biochemical stability of soil humus is an important factor affecting soil quality. Fungi are among the most efficient decomposers of humic matter due to presence of oxidative enzymes, including phenoloxidase laccase. Production of laccase by zygomycetes, a group of cellulolytic fungi widespread in s...

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Autores principales:	Alexander Lisov, Oksana Belova, Anna Zavarzina, Andrey Konstantinov, Alexey Leontievsky
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	soil organic matter decomposition humic substances laccase cellulolytic fungi Agriculture S
Acceso en línea:	https://doaj.org/article/7f08c698b335490da76bff01cc61fb8f
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spelling	oai:doaj.org-article:7f08c698b335490da76bff01cc61fb8f2021-11-25T16:05:01ZThe Role of Laccase from Zygomycetous Fungus <i>Mortierella elasson</i> in Humic Acids Degradation10.3390/agronomy111121692073-4395https://doaj.org/article/7f08c698b335490da76bff01cc61fb8f2021-10-01T00:00:00Zhttps://www.mdpi.com/2073-4395/11/11/2169https://doaj.org/toc/2073-4395Biochemical stability of soil humus is an important factor affecting soil quality. Fungi are among the most efficient decomposers of humic matter due to presence of oxidative enzymes, including phenoloxidase laccase. Production of laccase by zygomycetes, a group of cellulolytic fungi widespread in soil, is poorly studied. The potential role of laccase from zygomycetes in humus turnover is unknown. Here, we show for the first time that laccase of zygomycetous fungus <i>Mortierella elasson</i> can effectively depolymerize humic acids in vitro. The fungus produced laccase extracellularly in a liquid culture medium. Unlike in case of laccases in ligninolytic basidiomycetes, attempts to increase enzyme activity using inductors, changes in the source of nitrogen and carbon failed to lead to any increase in laccase production. Laccase was purified using ion exchange chromatography and gel filtration. The molecular weight of the laccase was 51.75 kDa. The laccase catalyzed the oxidation of ABTS and K<sub>4</sub>[Fe(CN)<sub>6</sub>], phenolic compounds, but not tyrosine. The laccase activity was inhibited by NaN<sub>3</sub> and NaF. The pH optimum of the laccase activity was 3.0 for ABTS and 5.0 for 2,6-dimethoxy phenol. The enzyme had moderate thermal stability and was rapidly inactivated at 70 °C. Purified laccase depolymerized humic acids from retisol, compost and peat more effectively than culture liquid containing laccase. The results of the study extend our knowledge of the role of laccases from different producers in the transformation of natural organic matter.Alexander LisovOksana BelovaAnna ZavarzinaAndrey KonstantinovAlexey LeontievskyMDPI AGarticlesoil organic matterdecompositionhumic substanceslaccasecellulolytic fungiAgricultureSENAgronomy, Vol 11, Iss 2169, p 2169 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	soil organic matter decomposition humic substances laccase cellulolytic fungi Agriculture S
spellingShingle	soil organic matter decomposition humic substances laccase cellulolytic fungi Agriculture S Alexander Lisov Oksana Belova Anna Zavarzina Andrey Konstantinov Alexey Leontievsky The Role of Laccase from Zygomycetous Fungus <i>Mortierella elasson</i> in Humic Acids Degradation
description	Biochemical stability of soil humus is an important factor affecting soil quality. Fungi are among the most efficient decomposers of humic matter due to presence of oxidative enzymes, including phenoloxidase laccase. Production of laccase by zygomycetes, a group of cellulolytic fungi widespread in soil, is poorly studied. The potential role of laccase from zygomycetes in humus turnover is unknown. Here, we show for the first time that laccase of zygomycetous fungus <i>Mortierella elasson</i> can effectively depolymerize humic acids in vitro. The fungus produced laccase extracellularly in a liquid culture medium. Unlike in case of laccases in ligninolytic basidiomycetes, attempts to increase enzyme activity using inductors, changes in the source of nitrogen and carbon failed to lead to any increase in laccase production. Laccase was purified using ion exchange chromatography and gel filtration. The molecular weight of the laccase was 51.75 kDa. The laccase catalyzed the oxidation of ABTS and K<sub>4</sub>[Fe(CN)<sub>6</sub>], phenolic compounds, but not tyrosine. The laccase activity was inhibited by NaN<sub>3</sub> and NaF. The pH optimum of the laccase activity was 3.0 for ABTS and 5.0 for 2,6-dimethoxy phenol. The enzyme had moderate thermal stability and was rapidly inactivated at 70 °C. Purified laccase depolymerized humic acids from retisol, compost and peat more effectively than culture liquid containing laccase. The results of the study extend our knowledge of the role of laccases from different producers in the transformation of natural organic matter.
format	article
author	Alexander Lisov Oksana Belova Anna Zavarzina Andrey Konstantinov Alexey Leontievsky
author_facet	Alexander Lisov Oksana Belova Anna Zavarzina Andrey Konstantinov Alexey Leontievsky
author_sort	Alexander Lisov
title	The Role of Laccase from Zygomycetous Fungus <i>Mortierella elasson</i> in Humic Acids Degradation
title_short	The Role of Laccase from Zygomycetous Fungus <i>Mortierella elasson</i> in Humic Acids Degradation
title_full	The Role of Laccase from Zygomycetous Fungus <i>Mortierella elasson</i> in Humic Acids Degradation
title_fullStr	The Role of Laccase from Zygomycetous Fungus <i>Mortierella elasson</i> in Humic Acids Degradation
title_full_unstemmed	The Role of Laccase from Zygomycetous Fungus <i>Mortierella elasson</i> in Humic Acids Degradation
title_sort	role of laccase from zygomycetous fungus <i>mortierella elasson</i> in humic acids degradation
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/7f08c698b335490da76bff01cc61fb8f
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The Role of Laccase from Zygomycetous Fungus <i>Mortierella elasson</i> in Humic Acids Degradation

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