A glucuronoxylan-specific xylanase from a new Paenibacillus favisporus strain isolated from tropical soil of Brazil.

Abstract

A new xylanolytic strain, Paenibacillus favisporus CC02-N2, was isolated from sugarcane plantation fields in Brazil. The strain had a xylan-degrading system with multiple enzymes, one of which, xylanase Xyn30A, was identified and characterized. The enzyme is a single-domain xylanase belonging to family 30 of the glycosyl hydrolases (GH30). Xyn30A shows high activity on glucuronoxylans, with a Vmax of 267.2 U mg⁻¹, a Km of 4.0 mg/ml, and a kcat of 13,333 min⁻¹ on beechwood xylan, but it does not hydrolyze arabinoxylans. The three-dimensional structure of Xyn30A consists of a common (β/α)8 barrel linked to a side-chain-associated β-structure, similar to previously characterized GH30 xylanases. The hydrolysis products from glucuronoxylan were methylglucuronic-acid-substituted xylooligomers (acidic xylooligosaccharides). The enzyme bound to insoluble xylan but not to crystalline cellulose. Our results suggest a specific role for Xyn30A in xylan biodegradation in natural habitats. The enzyme is a good candidate for the production of tailored xylooligosaccharides for use in the food industry and in the biotechnological transformation of biomass.

DOI: 10.2436/20.1501.01.220

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@article{Padilha2014AGX, title={A glucuronoxylan-specific xylanase from a new Paenibacillus favisporus strain isolated from tropical soil of Brazil.}, author={It{\'a}cio Q. M. Padilha and Susana V Valenzuela and Teresa Cristina S. de Lima Grisi and Pilar Diaz and Demetrius A M de Ara{\'u}jo and F. Pastor}, journal={International microbiology : the official journal of the Spanish Society for Microbiology}, year={2014}, volume={17 3}, pages={175-84} }