9O5H
Crystal structure of GH30_8 xylanase from Bacillus pumilus
Summary for 9O5H
| Entry DOI | 10.2210/pdb9o5h/pdb |
| Descriptor | Xylanase, GLYCEROL, CITRIC ACID, ... (4 entities in total) |
| Functional Keywords | glycoside hydrolase, hydrolase |
| Biological source | Bacillus pumilus ATCC 7061 |
| Total number of polymer chains | 2 |
| Total formula weight | 88910.97 |
| Authors | |
| Primary citation | Vacilotto, M.M.,Pellegrini, V.O.A.,Araujo, E.A.,Liberato, M.V.,Polikarpov, I. Enzymatic Production of Prebiotic Xylooligosaccharides Using a Bacillus pumilus GH30_8 Glucuronoxylanase: Structural Basis of Glucuronoxylan Recognition and Hydrolysis. J.Agric.Food Chem., 74:5417-5430, 2026 Cited by PubMed Abstract: Transformation of agro-industrial products into value-added products, such as prebiotic oligosaccharides, is a key element of the emerging bioeconomy. Here, we characterized a new GH30_8 glucuronoxylanase from (Xyn30_8A) for its potential in producing xylooligosaccharides (XOS). Xyn30_8A showed tolerance to ethanol and NaCl and released both linear and branched XOS containing MeGlcA at the penultimate nonreducing end residue. Its X-ray structure, determined at 2.16 Å resolution, revealed high similarity to other glucuronoxylanases. Furthermore, Xyn30_8A achieved higher xylan conversion yields from corn cob and sawdust than Xyn30A. Finally, fermentation assays showed that metabolized neutral XOS to acetate and lactate, whereas acidic XOS were poorly utilized. These results highlight the potential of Xyn30_8A as a valuable enzyme for the green transformation of plant biomass into prebiotic oligosaccharides with promising applications in human and animal nutrition, health, and biotechnology. PubMed: 41632704DOI: 10.1021/acs.jafc.5c07569 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.16 Å) |
Structure validation
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