Characterization of a new bifunctional endo-1,4-β-xylanase/esterase found in the rumen metagenome

Abstract 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...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Gabriella Cavazzini Pavarina, Eliana Gertrudes de Macedo Lemos, Natália Sarmanho Monteiro Lima, João Martins Pizauro Jr.
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
Materias:
R
Q
Acceso en línea:https://doaj.org/article/748b50ccd2b34acdb6bc13804254c4e4
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:748b50ccd2b34acdb6bc13804254c4e4
record_format dspace
spelling oai:doaj.org-article:748b50ccd2b34acdb6bc13804254c4e42021-12-02T14:58:38ZCharacterization of a new bifunctional endo-1,4-β-xylanase/esterase found in the rumen metagenome10.1038/s41598-021-89916-82045-2322https://doaj.org/article/748b50ccd2b34acdb6bc13804254c4e42021-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-89916-8https://doaj.org/toc/2045-2322Abstract 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.Gabriella Cavazzini PavarinaEliana Gertrudes de Macedo LemosNatália Sarmanho Monteiro LimaJoão Martins Pizauro Jr.Nature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Gabriella Cavazzini Pavarina
Eliana Gertrudes de Macedo Lemos
Natália Sarmanho Monteiro Lima
João Martins Pizauro Jr.
Characterization of a new bifunctional endo-1,4-β-xylanase/esterase found in the rumen metagenome
description Abstract 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.
format article
author Gabriella Cavazzini Pavarina
Eliana Gertrudes de Macedo Lemos
Natália Sarmanho Monteiro Lima
João Martins Pizauro Jr.
author_facet Gabriella Cavazzini Pavarina
Eliana Gertrudes de Macedo Lemos
Natália Sarmanho Monteiro Lima
João Martins Pizauro Jr.
author_sort Gabriella Cavazzini Pavarina
title Characterization of a new bifunctional endo-1,4-β-xylanase/esterase found in the rumen metagenome
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
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/748b50ccd2b34acdb6bc13804254c4e4
work_keys_str_mv AT gabriellacavazzinipavarina characterizationofanewbifunctionalendo14bxylanaseesterasefoundintherumenmetagenome
AT elianagertrudesdemacedolemos characterizationofanewbifunctionalendo14bxylanaseesterasefoundintherumenmetagenome
AT nataliasarmanhomonteirolima characterizationofanewbifunctionalendo14bxylanaseesterasefoundintherumenmetagenome
AT joaomartinspizaurojr characterizationofanewbifunctionalendo14bxylanaseesterasefoundintherumenmetagenome
_version_ 1718389272965283840