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Optimization of Endoglucanase Production from a Novel Bacterial Isolate, Arthrobacter sp. HPG166 and Characterization of Its Properties
Huang, Shengwei; Deng, Guanjun; Yang, Ying; Wu, Zhengyan; Wu, Lifang.
Afiliação
  • Huang, Shengwei; Chinese Academy of Sciences. Hefei Institutes of Physical Science. Bioenergy Forest Research Center of State Forestry Administration and Key Laboratory of Ion Beam Bioengineering. Hefei. CN
  • Deng, Guanjun; Chinese Academy of Sciences. Hefei Institutes of Physical Science. Bioenergy Forest Research Center of State Forestry Administration and Key Laboratory of Ion Beam Bioengineering. Hefei. CN
  • Yang, Ying; Chinese Academy of Sciences. Hefei Institutes of Physical Science. Bioenergy Forest Research Center of State Forestry Administration and Key Laboratory of Ion Beam Bioengineering. Hefei. CN
  • Wu, Zhengyan; Chinese Academy of Sciences. Hefei Institutes of Physical Science. Bioenergy Forest Research Center of State Forestry Administration and Key Laboratory of Ion Beam Bioengineering. Hefei. CN
  • Wu, Lifang; Chinese Academy of Sciences. Hefei Institutes of Physical Science. Bioenergy Forest Research Center of State Forestry Administration and Key Laboratory of Ion Beam Bioengineering. Hefei. CN
Braz. arch. biol. technol ; 58(5): 692-701, tab, graf
Artigo em Inglês | LILACS-Express | LILACS | ID: lil-764487
Biblioteca responsável: BR1.1
ABSTRACT
ABSTRACTIn this study, a potential novel cellulolytic bacteriumArthrobacter sp. HPG166 was isolated from the hindgut of root-feeding larvaeHolotrichia parallela. Optimization of fermentation factors for endoglucanase production byArthrobacter sp. HPG166 was carried out via response surface methodology. Sodium carboxymethylcellulose 1.19% (w/v) and beef extract 0.35% (w/v) were the ideal combination of carbon and nitrogen sources for enzyme production; the optimum temperature and pH for cellulase production were 34°C and pH 8.0 respectively. Under the optimized fermentation conditions, the maximum endoglucanase activity of 1.411 U mL-1 was obtained. The crude endoglucanase was thermotolerant as it retained 50.31% of its activity after incubation at 70°C for an hour. Metal profile of the enzyme indicated that Mg2+ and Na+ were strong stimulators while Mn2+ and Co+ drastically inhibited its activity. Due to its particular characteristics, this enzyme could have potential for industrial applications.

Texto completo: Disponível Coleções: Bases de dados internacionais Base de dados: LILACS Idioma: Inglês Revista: Braz. arch. biol. technol Assunto da revista: Biologia Ano de publicação: 2015 Tipo de documento: Artigo / Documento de projeto País de afiliação: China Instituição/País de afiliação: Chinese Academy of Sciences/CN

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Texto completo: Disponível Coleções: Bases de dados internacionais Base de dados: LILACS Idioma: Inglês Revista: Braz. arch. biol. technol Assunto da revista: Biologia Ano de publicação: 2015 Tipo de documento: Artigo / Documento de projeto País de afiliação: China Instituição/País de afiliação: Chinese Academy of Sciences/CN
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