A glucuronoxylan-specific xylanase from a new Paenibacillus favisporus strain isolated from tropical soil of Brazil.
Int Microbiol
; 17(3): 175-84, 2014 Sep.
Article
em En
| MEDLINE
| ID: mdl-26419457
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⻹, a Km of 4.0 mg/ml, and a kcat of 13,333 min⻹ on beechwood xylan, but it does not hydrolyze arabinoxylans. The three-dimensional structure of Xyn30A consists of a common (ß/α)8 barrel linked to a side-chain-associated ß-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.
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1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Microbiologia do Solo
/
Proteínas de Bactérias
/
Xilosidases
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Paenibacillus
País/Região como assunto:
America do sul
/
Brasil
Idioma:
En
Revista:
Int Microbiol
Assunto da revista:
MICROBIOLOGIA
Ano de publicação:
2014
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Suíça