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Optimization and partial characterization of ca-independent α-amylase from Bacillus amyloliquefaciens BH1.
Du, Renpeng; Zhao, Fangkun; Qiao, Xiaoxiao; Song, Qiaozhi; Ye, Guangbin; Wang, Yu; Wang, Binbin; Han, Ye; Zhou, Zhijiang.
Afiliação
  • Du R; a School of Chemical Engineering and Technology , Tianjin University , Tianjin , PR China.
  • Zhao F; a School of Chemical Engineering and Technology , Tianjin University , Tianjin , PR China.
  • Qiao X; a School of Chemical Engineering and Technology , Tianjin University , Tianjin , PR China.
  • Song Q; a School of Chemical Engineering and Technology , Tianjin University , Tianjin , PR China.
  • Ye G; b YoujiangMedical University for Nationalities , Guangxi , Baise , PR China.
  • Wang Y; a School of Chemical Engineering and Technology , Tianjin University , Tianjin , PR China.
  • Wang B; a School of Chemical Engineering and Technology , Tianjin University , Tianjin , PR China.
  • Han Y; a School of Chemical Engineering and Technology , Tianjin University , Tianjin , PR China.
  • Zhou Z; a School of Chemical Engineering and Technology , Tianjin University , Tianjin , PR China.
Prep Biochem Biotechnol ; 48(8): 768-774, 2018.
Article em En | MEDLINE | ID: mdl-30303444
Strain Bacillus amyloliquefaciens BH1 was evaluated for the generation of α-amylase. Culture conditions and medium components were optimized by a statistical approach for the optimal generation of α-amylase with response surface methodology (RSM) method. The Plackett-Burman (PB) design was executed to select the fermentation variables and Central composite design (CCD) for optimizing significant factors influencing production. The optimum levels for highest generation of α-amylase activity (198.26 ± 3.54 U/mL) were measured. A 1.69-fold improve generation was acquired in comparison with the non-optimized. Partial characterization of the α-amylase indicated optimal pH and temperature at 7.0 and 40 °C, respectively. Crude α-amylase maintained a constant pH range 5.0-8.0 and 30-70 °C. The α-amylase was independent of Ca2+, and the activity was inhibited by Fe3+, Co2+, Cu2+, and Hg2+. The thermo and pH stability of the α-amylase indicate its extensive application in the food and pharmaceutical industries.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Cálcio / Alfa-Amilases / Bacillus amyloliquefaciens Idioma: En Revista: Prep Biochem Biotechnol Assunto da revista: BIOQUIMICA / BIOTECNOLOGIA Ano de publicação: 2018 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Cálcio / Alfa-Amilases / Bacillus amyloliquefaciens Idioma: En Revista: Prep Biochem Biotechnol Assunto da revista: BIOQUIMICA / BIOTECNOLOGIA Ano de publicação: 2018 Tipo de documento: Article