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...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2021-05-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-021-89916-8 |
| _version_ | 1819127213158563840 |
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| 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 |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-22T08:08:21Z |
| format | Article |
| id | doaj.art-748b50ccd2b34acdb6bc13804254c4e4 |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-12-22T08:08:21Z |
| publishDate | 2021-05-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-748b50ccd2b34acdb6bc13804254c4e42022-12-21T18:33:05ZengNature PortfolioScientific Reports2045-23222021-05-0111111310.1038/s41598-021-89916-8Characterization of a new bifunctional endo-1,4-β-xylanase/esterase found in the rumen metagenomeGabriella Cavazzini Pavarina0Eliana Gertrudes de Macedo Lemos1Natália Sarmanho Monteiro Lima2João Martins Pizauro Jr.3Technology Department, School of Agricultural and Veterinarian Sciencess, Sao Paulo State University (Unesp)Technology Department, School of Agricultural and Veterinarian Sciencess, Sao Paulo State University (Unesp)Technology Department, School of Agricultural and Veterinarian Sciencess, Sao Paulo State University (Unesp)Technology Department, School of Agricultural and Veterinarian Sciencess, Sao Paulo State University (Unesp)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.https://doi.org/10.1038/s41598-021-89916-8 |
| spellingShingle | 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 Scientific Reports |
| title | 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_short | 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 |
| url | https://doi.org/10.1038/s41598-021-89916-8 |
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