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Partial characterization of an inulinase produced by Aspergillus japonicus URM5633
Silva, Anna Carolina da; Queiroz, Alana Emilia Soares de França; Porto, Tatiana Souza; Spier, Michele Rigon; Soccol, Carlos Ricardo; Porto, Ana Lúcia Figueiredo; Souza-Motta, Cristina Maria; Moreira, Keila Aparecida.
Afiliación
  • Silva, Anna Carolina da; Universidade Federal Rural de Pernambuco. Garanhuns. BR
  • Queiroz, Alana Emilia Soares de França; Universidade Federal Rural de Pernambuco. Garanhuns. BR
  • Porto, Tatiana Souza; Universidade Federal Rural de Pernambuco. Garanhuns. BR
  • Spier, Michele Rigon; Universidade Federal do Paraná. Departamento de Engenharia de Bioprocessos. Curitiba. BR
  • Soccol, Carlos Ricardo; Universidade Federal do Paraná. Departamento de Engenharia de Bioprocessos. Curitiba. BR
  • Porto, Ana Lúcia Figueiredo; Universidade Federal Rural de Pernambuco. Garanhuns. BR
  • Souza-Motta, Cristina Maria; Universidade Federal de Pernambuco. Departamento de Micologia. Recife. BR
  • Moreira, Keila Aparecida; Universidade Federal Rural de Pernambuco. Garanhuns. BR
Braz. arch. biol. technol ; Braz. arch. biol. technol;55(5): 671-676, Sept.-Oct. 2012. ilus
Article en En | LILACS | ID: lil-651649
Biblioteca responsable: BR1.1
ABSTRACT
Enzymes obtained by fermentation processes offer a number of advantages and have been widely researched and used throughout the world. This study aimed to partially characterise an inulinase produced from palm and cassava peel. The enzyme was produced via the solid-state fermentation of Aspergillus japonicus URM5633. The optimal temperatures were 50ºC and 55ºC, and the optimal pH values were 5.2 and 3.4 for inulinase fermentatively produced from palm and cassava peel, respectively. The thermostability measurements for inulinase produced in palm showed that the relative activity remained below 100% until 30 minutes of stability for all temperatures, but reached 106.8% at a temperature of 50ºC after 60 minutes. Inulinase from the crude extract of cassava peel was pH stable and only decreased to 55% of the maximal activity over the course of the assay, suggesting that this enzyme can be used in inulinase production and can be utilized in food industries.
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Texto completo: 1 Índice: LILACS Idioma: En Revista: Braz. arch. biol. technol Asunto de la revista: BIOLOGIA Año: 2012 Tipo del documento: Article

Texto completo: 1 Índice: LILACS Idioma: En Revista: Braz. arch. biol. technol Asunto de la revista: BIOLOGIA Año: 2012 Tipo del documento: Article