9O5H image
Deposition Date 2025-04-10
Release Date 2026-04-29
Last Version Date 2026-04-29
Entry Detail
PDB ID:
9O5H
Keywords:
Title:
Crystal structure of GH30_8 xylanase from Bacillus pumilus
Biological Source:
Source Organism(s):
Method Details:
Experimental Method:
Resolution:
2.16 Å
R-Value Free:
0.21
R-Value Work:
0.19
R-Value Observed:
0.19
Space Group:
P 21 21 21
Macromolecular Entities
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Xylanase
Chain IDs:A, B
Chain Length:389
Number of Molecules:2
Biological Source:Bacillus pumilus ATCC 7061
Primary Citation
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)
PMID: 41632704 DOI: 10.1021/acs.jafc.5c07569

Abstact

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 Bacillus pumilus (BpXyn30_8A) for its potential in producing xylooligosaccharides (XOS). BpXyn30_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 A resolution, revealed high similarity to other glucuronoxylanases. Furthermore, BpXyn30_8A achieved higher xylan conversion yields from corn cob and Eucalyptus sawdust than Ruminococcus champanellensisRcXyn30A. Finally, fermentation assays showed that Bifidobacterium adolescentis metabolized neutral XOS to acetate and lactate, whereas acidic XOS were poorly utilized. These results highlight the potential of BpXyn30_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.

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