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Expression, Purification, and Characterization of a Well-Adapted Tyrosinase from Peatlands Identified by Partial Community Analysis
[Image: see text] In peatlands, bacterial tyrosinases (TYRs) are proposed to act as key regulators of carbon storage by removing phenolic compounds, which inhibit the degradation of organic carbon. Historically, TYR activity has been blocked by anoxia resulting from persistent waterlogging; however,...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8375020/ https://www.ncbi.nlm.nih.gov/pubmed/34156250 http://dx.doi.org/10.1021/acs.est.1c02514 |
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author | Panis, Felix Krachler, Rudolf F. Krachler, Regina Rompel, Annette |
author_facet | Panis, Felix Krachler, Rudolf F. Krachler, Regina Rompel, Annette |
author_sort | Panis, Felix |
collection | PubMed |
description | [Image: see text] In peatlands, bacterial tyrosinases (TYRs) are proposed to act as key regulators of carbon storage by removing phenolic compounds, which inhibit the degradation of organic carbon. Historically, TYR activity has been blocked by anoxia resulting from persistent waterlogging; however, recent events of prolonged summer drought have boosted TYR activity and, consequently, the release of carbon stored in the form of organic compounds from peatlands. Since 30% of the global soil carbon stock is stored in peatlands, a profound understanding of the production and activity of TYRs is essential to assess the impact of carbon dioxide emitted from peatlands on climate change. TYR partial sequences identified by degenerated primers suggest a versatile TYR enzyme community naturally present in peatlands, which is produced by a phylogenetically diverse spectrum of bacteria, including Proteobacteria and Actinobacteria. One full-length sequence of an extracellular TYR (SzTYR) identified from a soda-rich inland salt marsh has been heterologously expressed and purified. SzTYR exhibits a molecular mass of 30 891.8 Da and shows a pH optimum of 9.0. Spectroscopic studies and kinetic investigations characterized SzTYR as a tyrosinase and proved its activity toward monophenols (coumaric acid), diphenols (caffeic acid, protocatechuic acid), and triphenols (gallic acid) naturally present in peatlands. |
format | Online Article Text |
id | pubmed-8375020 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American
Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-83750202021-08-20 Expression, Purification, and Characterization of a Well-Adapted Tyrosinase from Peatlands Identified by Partial Community Analysis Panis, Felix Krachler, Rudolf F. Krachler, Regina Rompel, Annette Environ Sci Technol [Image: see text] In peatlands, bacterial tyrosinases (TYRs) are proposed to act as key regulators of carbon storage by removing phenolic compounds, which inhibit the degradation of organic carbon. Historically, TYR activity has been blocked by anoxia resulting from persistent waterlogging; however, recent events of prolonged summer drought have boosted TYR activity and, consequently, the release of carbon stored in the form of organic compounds from peatlands. Since 30% of the global soil carbon stock is stored in peatlands, a profound understanding of the production and activity of TYRs is essential to assess the impact of carbon dioxide emitted from peatlands on climate change. TYR partial sequences identified by degenerated primers suggest a versatile TYR enzyme community naturally present in peatlands, which is produced by a phylogenetically diverse spectrum of bacteria, including Proteobacteria and Actinobacteria. One full-length sequence of an extracellular TYR (SzTYR) identified from a soda-rich inland salt marsh has been heterologously expressed and purified. SzTYR exhibits a molecular mass of 30 891.8 Da and shows a pH optimum of 9.0. Spectroscopic studies and kinetic investigations characterized SzTYR as a tyrosinase and proved its activity toward monophenols (coumaric acid), diphenols (caffeic acid, protocatechuic acid), and triphenols (gallic acid) naturally present in peatlands. American Chemical Society 2021-06-22 2021-08-17 /pmc/articles/PMC8375020/ /pubmed/34156250 http://dx.doi.org/10.1021/acs.est.1c02514 Text en © 2021 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Panis, Felix Krachler, Rudolf F. Krachler, Regina Rompel, Annette Expression, Purification, and Characterization of a Well-Adapted Tyrosinase from Peatlands Identified by Partial Community Analysis |
title | Expression,
Purification, and Characterization of
a Well-Adapted Tyrosinase from Peatlands Identified by Partial Community
Analysis |
title_full | Expression,
Purification, and Characterization of
a Well-Adapted Tyrosinase from Peatlands Identified by Partial Community
Analysis |
title_fullStr | Expression,
Purification, and Characterization of
a Well-Adapted Tyrosinase from Peatlands Identified by Partial Community
Analysis |
title_full_unstemmed | Expression,
Purification, and Characterization of
a Well-Adapted Tyrosinase from Peatlands Identified by Partial Community
Analysis |
title_short | Expression,
Purification, and Characterization of
a Well-Adapted Tyrosinase from Peatlands Identified by Partial Community
Analysis |
title_sort | expression,
purification, and characterization of
a well-adapted tyrosinase from peatlands identified by partial community
analysis |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8375020/ https://www.ncbi.nlm.nih.gov/pubmed/34156250 http://dx.doi.org/10.1021/acs.est.1c02514 |
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