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Effects of temperature, pH and additives on the activity of tannase produced by Paecilomyces variotii
Battestin, Vania; Macedo, Gabriela A.
Afiliação
  • Battestin, Vania; Campinas Statue University. Faculty of Food Engineering. Food Science Department. BR
  • Macedo, Gabriela A; Campinas Statue University. Faculty of Food Engineering. Food Science Department. BR
Electron. j. biotechnol ; 10(2): 191-199, Apr. 15, 2007. ilus, graf, tab
Artigo em Inglês | LILACS | ID: lil-499182
Biblioteca responsável: CL1.1
ABSTRACT
A biochemical characterization of the tannase from a Paecilomyces variotii strain isolated in Sao Paulo, Brazil was carried out. Paecilomyces variotii is a strain obtained from the screening of five hundred fungi that were tested for their production of tannase. The enzyme produced was partially purified using ammonium sulfate precipitation followed by ion exchange chromatography, diethylaminoethyl (DEAE)-Sepharose. Effects of temperature and pH on the activity of crude tannase crude and purified tannase was studied. Km was found to be 0.61 ‘mol and Vmax = 0.55 U/mL. Temperature of 40 to 65øC and pH 4.5 to 6.5 were optimum for tannase activity and stability; it could find potential use in the food-processing industry. The effects of different inhibitors, surfactants and chelators on the enzyme activity were also studied
Assuntos

Texto completo: Disponível Coleções: Bases de dados internacionais Base de dados: LILACS Assunto principal: Paecilomyces / Hidrolases de Éster Carboxílico Idioma: Inglês Revista: Electron. j. biotechnol Assunto da revista: Biotecnologia Ano de publicação: 2007 Tipo de documento: Artigo País de afiliação: Brasil Instituição/País de afiliação: Campinas Statue University/BR
Texto completo: Disponível Coleções: Bases de dados internacionais Base de dados: LILACS Assunto principal: Paecilomyces / Hidrolases de Éster Carboxílico Idioma: Inglês Revista: Electron. j. biotechnol Assunto da revista: Biotecnologia Ano de publicação: 2007 Tipo de documento: Artigo País de afiliação: Brasil Instituição/País de afiliação: Campinas Statue University/BR
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