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- W1495702204 abstract "In the last decade, a concern on protease as medicinal target for overcoming bacterial diseases and viral diseases has been rapidly increased because of the obvious involvement of this enzyme in the molecular of the diseases mechanism. The purpose of this research was to purification and characterize protease from patogenic bacteria Pseudomonas aeruginosa. The bacteria were grown in media containing triptone 1%, NaCl 1% and Yeast extract 0,5%. Protease of P.aeruginosa was purifed using column chromatography with Sephadex G-100 gel. There were three peaks of enzyme protein, which were detected on fractions 14, 17 and 30. The optimum pH of the extracellular proteasefrom P. aeruginosa was 8.. The optimum temperature of P. aeruginosa protease was 300C. Fe3+ (1 dan 5 mM) was strong activator and Co2+ was strong inhibitor. Study on the effect of metals ion and spesific inhibitors indicated that protease from P. aeruginosa was serin metaloprotease. The apparent moleculer weights, as determined by SDS-PAGE and zymogram technique,36 kD and 42 kD." @default.
- W1495702204 created "2016-06-24" @default.
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- W1495702204 date "2008-01-01" @default.
- W1495702204 modified "2023-09-26" @default.
- W1495702204 title "PURIFIKASI DAN KARAKTERISASI PROTEASE DARI BAKTERI PATOGEN Pseudomonas aeruginosa" @default.
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