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Summary The success of second‐generation (2G) ethanol technology relies on the efficient transformation of hemicellulose into monosaccharides and, particularly, on the full conversion of xylans into xylose for over 18% of fermentable sugars. We sought new hemicellulases using ruminal liquid, after enrichment of microbes with industrial lignocellulosic substrates and preparation of metagenomic libraries. Among 150 000 fosmid clones tested, we identified 22 clones with endoxylanase activity and 125 with β‐xylosidase activity. These positive clones were sequenced en masse, and the analysis revealed open reading frames with a low degree of similarity with known glycosyl hydrolases families. Among them, we searched for enzymes that were thermostable (activity at > 50°C) and that operate at high rate at pH around 5. Upon a wide series of assays, the clones exhibiting the highest endoxylanase and β‐xylosidase activities were identified. The fosmids were sequenced, and the corresponding genes cloned, expressed and proteins purified. We found that the activity of the most active β‐xylosidase was at least 10‐fold higher than that in commercial enzymatic fungal cocktails. Endoxylanase activity was in the range of fungal enzymes. Fungal enzymatic cocktails supplemented with the bacterial hemicellulases exhibited enhanced release of sugars from pretreated sugar cane straw, a relevant agricultural residue.
Endo-1,4-beta Xylanases, Rumen, Bacteria, Glycoside Hydrolases, Saccharum, Open Reading Frames, Bacterial Proteins, Polysaccharides, Biofuels, Enzyme Stability, Animals, Brief Reports, Cattle, Metagenomics, Cloning, Molecular
Endo-1,4-beta Xylanases, Rumen, Bacteria, Glycoside Hydrolases, Saccharum, Open Reading Frames, Bacterial Proteins, Polysaccharides, Biofuels, Enzyme Stability, Animals, Brief Reports, Cattle, Metagenomics, Cloning, Molecular
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| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |
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