title: Purification and characterization of an extracellular cold-active serine protease from the psychrophilic bacterium Colwellia sp. NJ341.
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 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.
authors.affiliation: College of life Sciences, Ocean University of China, 266003, Qingdao, PR China.
authors.forename: Quan-Fu
authors.initials: QF
authors.lastname: Wang
authors.forename: Jin-Lai
authors.initials: JL
authors.lastname: Miao
authors.forename: Yan-Hua
authors.initials: YH
authors.lastname: Hou
authors.forename: Yu
authors.initials: Y
authors.lastname: Ding
authors.forename: Guo-Dong
authors.initials: GD
authors.lastname: Wang
authors.forename: Guang-You
authors.initials: GY
authors.lastname: Li
mesh_terms: D002384:Catalysis; D003080:Cold Temperature; D004789:Enzyme Activation; D004795:Enzyme Stability; D020563:Gammaproteobacteria / Q000145:classification* / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D012697:Serine Endopeptidases / Q000032:analysis / Q000737:chemistry* / Q000302:isolation & purification*; D013045:Species Specificity
chemical_list: D012697:Serine Endopeptidases