, Volume 27, Issue 16, pp 1195-1198

Purification and Characterization of an Extracellular Cold-Active Serine Protease from the Psychrophilic Bacterium Colwellia sp. NJ341

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Abstract

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 °C (assayed over 10 min). Activity at 0 °C was nearly 30% of the maximum activity. It was completely inhibited by phenylmethylsulfonyl fluoride.