Biotechnology Letters, Vol.27, No.16, 1195-1198, 2005
Purification and characterization of an extracellular cold-active serine protease from the psychrophilic bacterium Colwellia sp NJ341
Colwellia sp. NJ341, isolated from Antarctic sea ice, secreted a cold-active serine protease. The purified protease had an apparent Mr of 60 kDa by SDS-PAGE and MALDI-TOF MS. It was active from pH 5-12 with maximum activity at 35 degrees C (assayed over 10 min). Activity at 0 degrees C was nearly 30% of the maximum activity. It was completely inhibited by phenylmethylsulfonyl fluoride.