New alkaline protease from Nocardiopsis sp.: partial purification and characterization

作者: K.A. Moreira , T.S. Porto , M.F.S. Teixeira , A.L.F Porto , J.L. Lima Filho

DOI: 10.1016/S0032-9592(02)00312-6

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摘要: Abstract A new alkaline protease from Nocardiopsis sp., isolated a soil sample collected the Northeast of Brazil is reported. The crude extract (CE) was designate as partially purified (PPE) after purification with ammonium sulphate (0–20%). Optimal pH and temperature for detection activity were obtaining at 10.5 8.0, CE PPE, respectively, 50 °C both extracts. enzyme stable more than 75% retained even incubation 120 min pH's between 8.0 10.5, use specific inhibitors, made it possible to show that belongs group serine protease. Maximum achieved (50 U/mg) 10.0 PPE (1260 U/mg). partial Sephadex G-75 obtained 26-purification fold 34% yield.

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