PARTIAL CHARACTERIZATION OF PROTEASES FROM STREPTOMYCES CLAVULIGERUS USING AN INEXPENSIVE MEDIUM

• Autor(a) principal: Moreira,Keila Aparecida
• Data de Publicação: 2001
• Outros Autores: 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
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Brazilian Journal of Microbiology
• Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822001000300010
• topic: Streptomyces clavuligerus; extracellular proteases; thermal stability; pH

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 enzymes from the partially purified extract 3585 and 644 strains, respectively. The optimum temperature for the crude extract was 21ºC for both strains. However, for the partially preparation the optimum temperature was 50ºC and 40°C for S. clavuligerus NRRL 3585 and 644 strains respectively.