Broad thermal spectrum metagenomic laccase with action for dye decolorization and fentin hydroxide treatment
Autor(a) principal: | |
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Data de Publicação: | 2022 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1186/s13568-022-01375-0 http://hdl.handle.net/11449/230673 |
Resumo: | Laccases are multicopper oxidases that act on various phenolic and non-phenolic compounds, enabling numerous applications including xenobiotic bioremediation, biofuel production, drug development, and cosmetic production, and they can be used as additives in the textile and food industries. This wide range of uses makes these enzymes extremely attractive for novel biotechnology applications. Here, we undertook the kinetic characterization of LacMeta, a predicted as homotrimeric (~ 107,93 kDa) small laccase, and demonstrated that this enzyme performs best at an acidic pH (pH 3–5) towards ABTS as substrate and has a broad thermal spectrum (10–60 °C), which can promote high plastic action potential through dynamic environmental temperature fluctuations. This enzyme showed following kinetic parameters: kcat = 6.377 s−1 ± 0.303, Km = 4.219 mM, and Vmax = 24.43 µM/min (against ABTS as substrate). LacMeta almost completely degraded malachite green (50 mg/mL) in only 2 h. Moreover, the enzyme was able to degrade seven dyes from four distinct classes and it respectively achieved 85% and 83% decolorization of methylene blue and trypan blue with ABTS as the mediator. In addition, LacMeta showed potential for the degradation of two thirds of an agricultural fungicide: fentin hydroxide, thus demonstrating its biotechnological aptitude for bioremediation. The results of this study suggest that LacMeta has potential in textile wastewater treatment and that it could help in the bioremediation of other human/environmental toxins such as pesticides and antibiotic compounds belonging to the same chemical classes as the degraded dyes. Graphical Abstract: [Figure not available: see fulltext.] |
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Broad thermal spectrum metagenomic laccase with action for dye decolorization and fentin hydroxide treatmentBioremediationDyesLaccaseMetagenomicsLaccases are multicopper oxidases that act on various phenolic and non-phenolic compounds, enabling numerous applications including xenobiotic bioremediation, biofuel production, drug development, and cosmetic production, and they can be used as additives in the textile and food industries. This wide range of uses makes these enzymes extremely attractive for novel biotechnology applications. Here, we undertook the kinetic characterization of LacMeta, a predicted as homotrimeric (~ 107,93 kDa) small laccase, and demonstrated that this enzyme performs best at an acidic pH (pH 3–5) towards ABTS as substrate and has a broad thermal spectrum (10–60 °C), which can promote high plastic action potential through dynamic environmental temperature fluctuations. This enzyme showed following kinetic parameters: kcat = 6.377 s−1 ± 0.303, Km = 4.219 mM, and Vmax = 24.43 µM/min (against ABTS as substrate). LacMeta almost completely degraded malachite green (50 mg/mL) in only 2 h. Moreover, the enzyme was able to degrade seven dyes from four distinct classes and it respectively achieved 85% and 83% decolorization of methylene blue and trypan blue with ABTS as the mediator. In addition, LacMeta showed potential for the degradation of two thirds of an agricultural fungicide: fentin hydroxide, thus demonstrating its biotechnological aptitude for bioremediation. The results of this study suggest that LacMeta has potential in textile wastewater treatment and that it could help in the bioremediation of other human/environmental toxins such as pesticides and antibiotic compounds belonging to the same chemical classes as the degraded dyes. Graphical Abstract: [Figure not available: see fulltext.]Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Department of Agricultural and Environmental Biotechnology São Paulo State University Jaboticabal Campus, São Paulo StateMolecular Biology Laboratory Institute for Research in Bioenergy (IPBEN), São Paulo StateGraduate Program in Agricultural and Livestock Microbiology School of Agricultural and Veterinarian Sciences São Paulo State University (UNESP), SPDepartment of Agricultural and Environmental Biotechnology São Paulo State University Jaboticabal Campus, São Paulo StateGraduate Program in Agricultural and Livestock Microbiology School of Agricultural and Veterinarian Sciences São Paulo State University (UNESP), SPFAPESP: 2011/10981-3Universidade Estadual Paulista (UNESP)Institute for Research in Bioenergy (IPBEN)Lima, Natália Sarmanho Monteiro [UNESP]Gomes-Pepe, Elisângela Soares [UNESP]Campanharo, João Carlos [UNESP]de Macedo Lemos, Eliana Gertrudes [UNESP]2022-04-29T08:41:27Z2022-04-29T08:41:27Z2022-12-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1186/s13568-022-01375-0AMB Express, v. 12, n. 1, 2022.2191-0855http://hdl.handle.net/11449/23067310.1186/s13568-022-01375-02-s2.0-85127520649Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengAMB Expressinfo:eu-repo/semantics/openAccess2024-06-07T15:31:34Zoai:repositorio.unesp.br:11449/230673Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T15:30:29.753804Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Broad thermal spectrum metagenomic laccase with action for dye decolorization and fentin hydroxide treatment |
title |
Broad thermal spectrum metagenomic laccase with action for dye decolorization and fentin hydroxide treatment |
spellingShingle |
Broad thermal spectrum metagenomic laccase with action for dye decolorization and fentin hydroxide treatment Lima, Natália Sarmanho Monteiro [UNESP] Bioremediation Dyes Laccase Metagenomics |
title_short |
Broad thermal spectrum metagenomic laccase with action for dye decolorization and fentin hydroxide treatment |
title_full |
Broad thermal spectrum metagenomic laccase with action for dye decolorization and fentin hydroxide treatment |
title_fullStr |
Broad thermal spectrum metagenomic laccase with action for dye decolorization and fentin hydroxide treatment |
title_full_unstemmed |
Broad thermal spectrum metagenomic laccase with action for dye decolorization and fentin hydroxide treatment |
title_sort |
Broad thermal spectrum metagenomic laccase with action for dye decolorization and fentin hydroxide treatment |
author |
Lima, Natália Sarmanho Monteiro [UNESP] |
author_facet |
Lima, Natália Sarmanho Monteiro [UNESP] Gomes-Pepe, Elisângela Soares [UNESP] Campanharo, João Carlos [UNESP] de Macedo Lemos, Eliana Gertrudes [UNESP] |
author_role |
author |
author2 |
Gomes-Pepe, Elisângela Soares [UNESP] Campanharo, João Carlos [UNESP] de Macedo Lemos, Eliana Gertrudes [UNESP] |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (UNESP) Institute for Research in Bioenergy (IPBEN) |
dc.contributor.author.fl_str_mv |
Lima, Natália Sarmanho Monteiro [UNESP] Gomes-Pepe, Elisângela Soares [UNESP] Campanharo, João Carlos [UNESP] de Macedo Lemos, Eliana Gertrudes [UNESP] |
dc.subject.por.fl_str_mv |
Bioremediation Dyes Laccase Metagenomics |
topic |
Bioremediation Dyes Laccase Metagenomics |
description |
Laccases are multicopper oxidases that act on various phenolic and non-phenolic compounds, enabling numerous applications including xenobiotic bioremediation, biofuel production, drug development, and cosmetic production, and they can be used as additives in the textile and food industries. This wide range of uses makes these enzymes extremely attractive for novel biotechnology applications. Here, we undertook the kinetic characterization of LacMeta, a predicted as homotrimeric (~ 107,93 kDa) small laccase, and demonstrated that this enzyme performs best at an acidic pH (pH 3–5) towards ABTS as substrate and has a broad thermal spectrum (10–60 °C), which can promote high plastic action potential through dynamic environmental temperature fluctuations. This enzyme showed following kinetic parameters: kcat = 6.377 s−1 ± 0.303, Km = 4.219 mM, and Vmax = 24.43 µM/min (against ABTS as substrate). LacMeta almost completely degraded malachite green (50 mg/mL) in only 2 h. Moreover, the enzyme was able to degrade seven dyes from four distinct classes and it respectively achieved 85% and 83% decolorization of methylene blue and trypan blue with ABTS as the mediator. In addition, LacMeta showed potential for the degradation of two thirds of an agricultural fungicide: fentin hydroxide, thus demonstrating its biotechnological aptitude for bioremediation. The results of this study suggest that LacMeta has potential in textile wastewater treatment and that it could help in the bioremediation of other human/environmental toxins such as pesticides and antibiotic compounds belonging to the same chemical classes as the degraded dyes. Graphical Abstract: [Figure not available: see fulltext.] |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-04-29T08:41:27Z 2022-04-29T08:41:27Z 2022-12-01 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1186/s13568-022-01375-0 AMB Express, v. 12, n. 1, 2022. 2191-0855 http://hdl.handle.net/11449/230673 10.1186/s13568-022-01375-0 2-s2.0-85127520649 |
url |
http://dx.doi.org/10.1186/s13568-022-01375-0 http://hdl.handle.net/11449/230673 |
identifier_str_mv |
AMB Express, v. 12, n. 1, 2022. 2191-0855 10.1186/s13568-022-01375-0 2-s2.0-85127520649 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
AMB Express |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
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1808128524325748736 |