AI Article Synopsis
- Researchers discovered a new enzyme, endo-1,4-β-xylanase/esterase, from the microbiota of Nellore cattle, and successfully overexpressed it in E. coli.
- This enzyme is stable in a pH range of 5 to 6.5 and temperatures from 30 to 45 °C, showing promising activity for industrial applications.
- Its synergistic properties could enhance the breakdown of complex carbohydrates, making it useful for processing lignocellulosic biomass and as a supplement in animal feed to boost xylooligosaccharide production.
Article 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 V of 30.959 ± 2.334 µmol/min/mg, K of 3.6 ± 0.6 mM and k of 2.323 ± 175 s. 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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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8128909 | PMC |
| http://dx.doi.org/10.1038/s41598-021-89916-8 | DOI Listing |
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