An organic solvent-stable alkaline protease from Pseudomonas aeruginosa strain K: Enzyme purification and characterization
Raja Abdul Rahman, Raja Noor Zaliha, Lee, Poh Geok, Basri, Mahiran and Salleh, Abu Bakar (2006) An organic solvent-stable alkaline protease from Pseudomonas aeruginosa strain K: Enzyme purification and characterization. Enzyme and Microbial Technology, 39 (7). 1484-1491 . ISSN 0141-0229
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Official URL: http://dx.doi.org/10.1016/j.enzmictec.2006.03.038
The organic solvent-tolerant strain K protease was purified to homogeneity by ammonium sulphate precipitation and anion exchange chromatography with 124-fold increase in specific activity. The molecular mass of the purified enzyme as revealed by SDS-PAGE electrophoresis is 51,000 Da. The strain K protease was an alkaline metalloprotease with an optimum pH and temperature of 10 and 70 °C, respectively. The enzyme showed stability and activation in the presence of organic solvents with log Pa/w values equal or more than 4.0. After 14 days of incubation, the purified protease was activated 1.11, 1.82, 1.50, 1.75 and 1.80 times in 1-decanol, isooctane, decane, dodecane and hexadecane, respectively.
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