Characterization of a new bifunctional endo-1,4-β-xylanase/esterase found in the rumen metagenome
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1038/s41598-021-89916-8 http://hdl.handle.net/11449/208696 |
Resumo: | Metagenomic data mining of the Nellore cattle rumen microbiota identified a new bifunctional enzyme, endo-1,4-β-xylanase/esterase, which was subsequently overexpressed in E. coli BL21 (DE3). This enzyme was stable at pH intervals of 5 to 6.5 and temperatures between 30 and 45 °C, and under the test conditions, it had a Vmax of 30.959 ± 2.334 µmol/min/mg, Km of 3.6 ± 0.6 mM and kcat of 2.323 ± 175 s−1. Additionally, the results showed that the enzyme is tolerant to NaCl and organic solvents and therefore is suitable for industrial environments. Xylanases are widely applicable, and the synergistic activity of endo-1,4-β-xylanase/esterase in a single molecule will improve the degradation efficiency of heteroxylans via the creation of xylanase binding sites. Therefore, this new molecule has the potential for use in lignocellulosic biomass processing and as an animal feed food additive and could improve xylooligosaccharide production efficiency. |
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Characterization of a new bifunctional endo-1,4-β-xylanase/esterase found in the rumen metagenomeMetagenomic data mining of the Nellore cattle rumen microbiota identified a new bifunctional enzyme, endo-1,4-β-xylanase/esterase, which was subsequently overexpressed in E. coli BL21 (DE3). This enzyme was stable at pH intervals of 5 to 6.5 and temperatures between 30 and 45 °C, and under the test conditions, it had a Vmax of 30.959 ± 2.334 µmol/min/mg, Km of 3.6 ± 0.6 mM and kcat of 2.323 ± 175 s−1. Additionally, the results showed that the enzyme is tolerant to NaCl and organic solvents and therefore is suitable for industrial environments. Xylanases are widely applicable, and the synergistic activity of endo-1,4-β-xylanase/esterase in a single molecule will improve the degradation efficiency of heteroxylans via the creation of xylanase binding sites. Therefore, this new molecule has the potential for use in lignocellulosic biomass processing and as an animal feed food additive and could improve xylooligosaccharide production efficiency.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Technology Department School of Agricultural and Veterinarian Sciencess Sao Paulo State University (Unesp), Via de Acesso Prof. Paulo Donato Castellane S/N, km 5Graduate Program in Agricultural and Livestock Microbiology School of Agricultural and Veterinarian Sciences Sao Paulo State University (Unesp)Molecular Biology Laboratory Bioenergy Research Institute (IPBEN)Technology Department School of Agricultural and Veterinarian Sciencess Sao Paulo State University (Unesp), Via de Acesso Prof. Paulo Donato Castellane S/N, km 5Graduate Program in Agricultural and Livestock Microbiology School of Agricultural and Veterinarian Sciences Sao Paulo State University (Unesp)FAPESP: 2018/12885-0Universidade Estadual Paulista (Unesp)Bioenergy Research Institute (IPBEN)Pavarina, Gabriella Cavazzini [UNESP]Lemos, Eliana Gertrudes de Macedo [UNESP]Lima, Natália Sarmanho Monteiro [UNESP]Pizauro Jr, João Martins [UNESP]2021-06-25T11:16:25Z2021-06-25T11:16:25Z2021-12-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1038/s41598-021-89916-8Scientific Reports, v. 11, n. 1, 2021.2045-2322http://hdl.handle.net/11449/20869610.1038/s41598-021-89916-82-s2.0-85106209437Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengScientific Reportsinfo:eu-repo/semantics/openAccess2024-06-07T15:31:34Zoai:repositorio.unesp.br:11449/208696Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T15:52:02.227962Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Characterization of a new bifunctional endo-1,4-β-xylanase/esterase found in the rumen metagenome |
title |
Characterization of a new bifunctional endo-1,4-β-xylanase/esterase found in the rumen metagenome |
spellingShingle |
Characterization of a new bifunctional endo-1,4-β-xylanase/esterase found in the rumen metagenome Pavarina, Gabriella Cavazzini [UNESP] |
title_short |
Characterization of a new bifunctional endo-1,4-β-xylanase/esterase found in the rumen metagenome |
title_full |
Characterization of a new bifunctional endo-1,4-β-xylanase/esterase found in the rumen metagenome |
title_fullStr |
Characterization of a new bifunctional endo-1,4-β-xylanase/esterase found in the rumen metagenome |
title_full_unstemmed |
Characterization of a new bifunctional endo-1,4-β-xylanase/esterase found in the rumen metagenome |
title_sort |
Characterization of a new bifunctional endo-1,4-β-xylanase/esterase found in the rumen metagenome |
author |
Pavarina, Gabriella Cavazzini [UNESP] |
author_facet |
Pavarina, Gabriella Cavazzini [UNESP] Lemos, Eliana Gertrudes de Macedo [UNESP] Lima, Natália Sarmanho Monteiro [UNESP] Pizauro Jr, João Martins [UNESP] |
author_role |
author |
author2 |
Lemos, Eliana Gertrudes de Macedo [UNESP] Lima, Natália Sarmanho Monteiro [UNESP] Pizauro Jr, João Martins [UNESP] |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) Bioenergy Research Institute (IPBEN) |
dc.contributor.author.fl_str_mv |
Pavarina, Gabriella Cavazzini [UNESP] Lemos, Eliana Gertrudes de Macedo [UNESP] Lima, Natália Sarmanho Monteiro [UNESP] Pizauro Jr, João Martins [UNESP] |
description |
Metagenomic data mining of the Nellore cattle rumen microbiota identified a new bifunctional enzyme, endo-1,4-β-xylanase/esterase, which was subsequently overexpressed in E. coli BL21 (DE3). This enzyme was stable at pH intervals of 5 to 6.5 and temperatures between 30 and 45 °C, and under the test conditions, it had a Vmax of 30.959 ± 2.334 µmol/min/mg, Km of 3.6 ± 0.6 mM and kcat of 2.323 ± 175 s−1. Additionally, the results showed that the enzyme is tolerant to NaCl and organic solvents and therefore is suitable for industrial environments. Xylanases are widely applicable, and the synergistic activity of endo-1,4-β-xylanase/esterase in a single molecule will improve the degradation efficiency of heteroxylans via the creation of xylanase binding sites. Therefore, this new molecule has the potential for use in lignocellulosic biomass processing and as an animal feed food additive and could improve xylooligosaccharide production efficiency. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-06-25T11:16:25Z 2021-06-25T11:16:25Z 2021-12-01 |
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/10.1038/s41598-021-89916-8 Scientific Reports, v. 11, n. 1, 2021. 2045-2322 http://hdl.handle.net/11449/208696 10.1038/s41598-021-89916-8 2-s2.0-85106209437 |
url |
http://dx.doi.org/10.1038/s41598-021-89916-8 http://hdl.handle.net/11449/208696 |
identifier_str_mv |
Scientific Reports, v. 11, n. 1, 2021. 2045-2322 10.1038/s41598-021-89916-8 2-s2.0-85106209437 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Scientific Reports |
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 |
|
_version_ |
1808128574877597696 |