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| Sales,Marilia Ribeiro; Cavalcanti,Maria Taciana Holanda; Lima Filho,José Luiz de; Motta,Cristina Maria de Souza; Porto,Ana Lúcia Figueiredo. |
| O objetivo deste trabalho foi estudar a produção de queratinase por Aspergillus carbonarius URM 1546, tendo-se como substrato penas de galinha, por meio de planejamento fatorial completo 2³. Todos os parâmetros estudados e as interações de segunda ordem foram estatisticamente significativos. A maior atividade queratinolítica (48,9 U mL-1) foi obtida com 120 rpm, 0,5% (p/v) de penas de galinha e sete dias de cultivo. |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Enzimas queratinolíticas; Fungos filamentosos; Queratina. |
| Ano: 2008 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-204X2008000200020 |
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| Duarte,Ana Rodrigues; Duarte,Débora Maria Rodrigues; Moreira,Keila Aparecida; Cavalcanti,Maria Taciana Holanda; Lima-Filho,José Luiz de; Porto,Ana Lúcia Figueiredo. |
| The partial characterization and purification of milk clotting enzyme obtained from the (root latex) of Jacaratia corumbensis O. kuntze was studied, by fractional precipitation with ammonium sulphate and ion exchange chromatography. The ammonium sulphate precipitate showed five fractions (AS1- 0-20%; AS2 - 20-40%; AS3 - 40-60%; AS4 - 60-80%; AS5 - 80-100%) and among the fractions obtained, the 40-60% fraction (AS3) showed the highest milk clotting activity with a purification factor of 1.2 fold in relation to the crude extract. This fraction when applied on Mono Q column yielded two protein peaks (p1 and p2), but p1 pool showed the best milk-clotting activity. The optimal pH for the crude and partially purified extract was 6.5 and 7.0, respectively. The... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Jacaratia corumbensis O. kuntze; Milk clotting enzyme; Characterization; Purification; Vegetable enzyme. |
| Ano: 2009 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132009000100001 |
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| Moreira,Keila Aparecida; Cavalcanti,Maria Taciana Holanda; Duarte,Helena Simões; Tambourgi,Elias Basile; Melo,Eduardo Henrique Magalhães de; Silva,Valdinete Lins; Porto,Ana Lúcia Figueiredo; Lima Filho,José Luiz de. |
| The partial characterization of extracellular proteases from Streptomyces clavuligerus NRRL 3585 and 644 mutant was investigated. The enzyme production was carried out in batch fermentation using soy bean filtrate as nitrogen source. Maximum activity was obtained after 96h of fermentation with an initial pH of 7.0. The enzyme was partially purified by ammonium sulphate precipitation. Enzymes from the two strains retained 37% of their initial activities at pH 8.0 after 2 h incubation at 25ºC. Enzyme half-life at pH 8.0 and 60ºC was 40.30 and 53.32 min, respectively for both strains (partially purified extract). The optimum pH was obtained at pH 7.0-8.0 and 8.4 for enzymes produced for 3585 and 644 strains (crude extract), respectively, and 8.4 and 8.0 for... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Streptomyces clavuligerus; Extracellular proteases; Thermal stability; PH. |
| Ano: 2001 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822001000300010 |
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