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.
Wang
Quan-Fu
QF
College of life Sciences, Ocean University of China, 266003, Qingdao, PR China.
Miao
Jin-Lai
JL
Hou
Yan-Hua
YH
Ding
Yu
Y
Wang
Guo-Dong
GD
Li
Guang-You
GY
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
D012697:Serine Endopeptidases