Your browser doesn't support javascript.
loading
A glucuronoxylan-specific xylanase from a new Paenibacillus favisporus strain isolated from tropical soil of Brazil.
Padilha, Itácio Q M; Valenzuela, Susana V; Grisi, Teresa C S L; Díaz, Pilar; de Araújo, Demetrius A M; Pastor, Francisco I Javier.
Afiliação
  • Padilha IQ; Department of Biotechnology, Biotechnology Center, Federal University of Paraíba, João Pessoa, Brazil.
  • Valenzuela SV; Department of Microbiology, Faculty of Biology. University of Barcelona, Barcelona, Spain.
  • Grisi TC; Department of Biotechnology, Biotechnology Center, Federal University of Paraíba, João Pessoa, Brazil.
  • Díaz P; Department of Microbiology, Faculty of Biology. University of Barcelona, Barcelona, Spain.
  • de Araújo DA; Department of Microbiology, Faculty of Biology. University of Barcelona, Barcelona, Spain.
  • Pastor FI; Department of Microbiology, Faculty of Biology. University of Barcelona, Barcelona, Spain.
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⁻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 (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.
Assuntos
Palavras-chave
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Microbiologia do Solo / Proteínas de Bactérias / Xilosidases / 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
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Microbiologia do Solo / Proteínas de Bactérias / Xilosidases / 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