嗜冷菌科尔韦氏菌属NJ341胞外冷活性丝氨酸蛋白酶的纯化与特性分析
Purification and characterization of an extracellular cold-active serine protease from the psychrophilic bacterium Colwellia sp. NJ341.
作者信息
Wang Quan-Fu, Miao Jin-Lai, Hou Yan-Hua, Ding Yu, Wang Guo-Dong, Li Guang-You
机构信息
College of life Sciences, Ocean University of China, 266003, Qingdao, PR China.
出版信息
Biotechnol Lett. 2005 Aug;27(16):1195-8. doi: 10.1007/s10529-005-0016-x.
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.
从南极海冰中分离出的科尔韦氏菌属NJ341分泌一种冷活性丝氨酸蛋白酶。通过SDS-PAGE和基质辅助激光解吸电离飞行时间质谱分析，纯化后的蛋白酶表观分子量为60 kDa。其在pH 5至12范围内具有活性，在35℃时活性最高（检测时间为10分钟）。在0℃时的活性接近最大活性的30%。它被苯甲基磺酰氟完全抑制。
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