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Enhancement of laccase activity by pre-incubation with organic solvents
Laccases that are tolerant to organic solvents are powerful bio-catalysts with broad applications in biotechnology. Most of these uses must be accomplished at high concentration of organic solvents, during which proteins undergo unfolding, thereby losing enzyme activity. Here we show that organic-so...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6611822/ https://www.ncbi.nlm.nih.gov/pubmed/31278318 http://dx.doi.org/10.1038/s41598-019-45118-x |
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author | Wu, Meng-Hsuan Lin, Meng-Chun Lee, Cheng-Chung Yu, Su-May Wang, Andrew H.-J. Ho, Tuan-Hua David |
author_facet | Wu, Meng-Hsuan Lin, Meng-Chun Lee, Cheng-Chung Yu, Su-May Wang, Andrew H.-J. Ho, Tuan-Hua David |
author_sort | Wu, Meng-Hsuan |
collection | PubMed |
description | Laccases that are tolerant to organic solvents are powerful bio-catalysts with broad applications in biotechnology. Most of these uses must be accomplished at high concentration of organic solvents, during which proteins undergo unfolding, thereby losing enzyme activity. Here we show that organic-solvent pre-incubation provides effective and reversible 1.5- to 4.0-fold enhancement of enzyme activity of fungal laccases. Several organic solvents, including acetone, methanol, ethanol, DMSO, and DMF had an enhancement effect among all laccases studied. The enhancement was not substrate-specific and could be observed by using both phenolic and non-phenolic substrates. Laccase preincubated with organic solvents was sensitive to high temperature but remained stable at 25 °C, for an advantage for long-term storage. The acetone-pre-incubated 3-D structure of DLac, a high-efficiency fungal laccase, was determined and confirmed that the DLac protein structure remains intact and stable at a high concentration of organic solvent. Moreover, the turnover rates of fungal laccases were improved after organic-solvent pre-incubation, with DLac showing the highest enhancement among the fungal laccases examined. Our investigation sheds light on improving fungal laccase usage under extreme conditions and extends opportunities for bioremediation, decolorization, and organic synthesis. |
format | Online Article Text |
id | pubmed-6611822 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-66118222019-07-15 Enhancement of laccase activity by pre-incubation with organic solvents Wu, Meng-Hsuan Lin, Meng-Chun Lee, Cheng-Chung Yu, Su-May Wang, Andrew H.-J. Ho, Tuan-Hua David Sci Rep Article Laccases that are tolerant to organic solvents are powerful bio-catalysts with broad applications in biotechnology. Most of these uses must be accomplished at high concentration of organic solvents, during which proteins undergo unfolding, thereby losing enzyme activity. Here we show that organic-solvent pre-incubation provides effective and reversible 1.5- to 4.0-fold enhancement of enzyme activity of fungal laccases. Several organic solvents, including acetone, methanol, ethanol, DMSO, and DMF had an enhancement effect among all laccases studied. The enhancement was not substrate-specific and could be observed by using both phenolic and non-phenolic substrates. Laccase preincubated with organic solvents was sensitive to high temperature but remained stable at 25 °C, for an advantage for long-term storage. The acetone-pre-incubated 3-D structure of DLac, a high-efficiency fungal laccase, was determined and confirmed that the DLac protein structure remains intact and stable at a high concentration of organic solvent. Moreover, the turnover rates of fungal laccases were improved after organic-solvent pre-incubation, with DLac showing the highest enhancement among the fungal laccases examined. Our investigation sheds light on improving fungal laccase usage under extreme conditions and extends opportunities for bioremediation, decolorization, and organic synthesis. Nature Publishing Group UK 2019-07-05 /pmc/articles/PMC6611822/ /pubmed/31278318 http://dx.doi.org/10.1038/s41598-019-45118-x Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Wu, Meng-Hsuan Lin, Meng-Chun Lee, Cheng-Chung Yu, Su-May Wang, Andrew H.-J. Ho, Tuan-Hua David Enhancement of laccase activity by pre-incubation with organic solvents |
title | Enhancement of laccase activity by pre-incubation with organic solvents |
title_full | Enhancement of laccase activity by pre-incubation with organic solvents |
title_fullStr | Enhancement of laccase activity by pre-incubation with organic solvents |
title_full_unstemmed | Enhancement of laccase activity by pre-incubation with organic solvents |
title_short | Enhancement of laccase activity by pre-incubation with organic solvents |
title_sort | enhancement of laccase activity by pre-incubation with organic solvents |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6611822/ https://www.ncbi.nlm.nih.gov/pubmed/31278318 http://dx.doi.org/10.1038/s41598-019-45118-x |
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