Partial characterization of proteases from Spretomyces clavuligerus using an inexpensive medium

Moreira, Keila AparecidaCavalcanti, Maria Taciana HolandaDuarte, Helena SimõesTambourgi, Elias BasileMelo, Eduardo Henrique Magalhäes deSilva, Valdinete LinsPorto, Ana Lúcia FigueiredoLima 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 per cent of their initial activities at pH 8.0 after 2 h incubation at 25§C. Enzyme half-life at pH 8.0 and 60§C 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 21§C for both strains. However, for the partially preparation the optimum temperature was 50§C and 40ºC for S. clavuligerus NRRL 3585 and 644 strains respectively.