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Partial characterization of xylanase produced by Caldicoprobacter algeriensis, a new thermophilic anaerobic bacterium isolated from an Algerian hot spring.
Bouacem, Khelifa; Bouanane-Darenfed, Amel; Boucherba, Nawel; Joseph, Manon; Gagaoua, Mohammed; Ben Hania, Wajdi; Kecha, Mouloud; Benallaoua, Said; Hacène, Hocine; Ollivier, Bernard; Fardeau, Marie-Laure.
Afiliação
  • Bouacem K; Laboratory of Cellular and Molecular Biology (Microbiology group), Faculty of Biology, University of Science and Technology Houari Boumediene, Bab Ezzouar, Algiers, Algeria.
Appl Biochem Biotechnol ; 174(5): 1969-81, 2014 Nov.
Article em En | MEDLINE | ID: mdl-25161038
ABSTRACT
To date, xylanases have expanded their use in many processing industries, such as pulp, paper, food, and textile. This study aimed the production and partial characterization of a thermostable xylanase from a novel thermophilic anaerobic bacterium Caldicoprobacter algeriensis strain TH7C1(T) isolated from a northeast hot spring in Algeria. The obtained results showed that C. algeriensis xylanase seems not to be correlated with the biomass growth profile whereas the maximum enzyme production (140.0 U/ml) was recorded in stationary phase (18 h). The temperature and pH for optimal activities were 70 °C and 11.0, respectively. The enzyme was found to be stable at 50, 60, 70, and 80 °C, with a half-life of 10, 9, 8, and 4 h, respectively. Influence of metal ions on enzyme activity revealed that Ca(+2) enhances greatly the relative activity to 151.3 %; whereas Hg(2+) inhibited significantly the enzyme. At the best of our knowledge, this is the first report on the production of xylanase by the thermophilic bacterium C. algeriensis. This thermo- and alkaline-tolerant xylanase could be used in pulp bleaching process.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Clostridium / Endo-1,4-beta-Xilanases / Fontes Termais Idioma: En Ano de publicação: 2014 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Clostridium / Endo-1,4-beta-Xilanases / Fontes Termais Idioma: En Ano de publicação: 2014 Tipo de documento: Article