Yang Chengye, Wang Fang, Hao Jianhua, Zhang Kai, Yuan Na, Sun Mi
Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao, Shandong Province, China.
Biosci Biotechnol Biochem. 2010;74(6):1220-5. doi: 10.1271/bbb.100011. Epub 2010 Jun 7.
A psychrophilic protease-producing bacterium, HW08, was isolated from sediment of the Yellow Sea in eastern China. On the basis of 16S rDNA sequence analysis and physiological properties, the isolate was identified as Pseudomonas lundensis. The secreted protease, named Ps5, was purified from the culture supernatant as a monomer with an apparent molecular mass of 46 kDa on SDS-PAGE. As a metalloprotease (inhibited by EDTA), the enzyme showed maximum activity at 30 degrees C at pH 10.4. It had no activity loss exposed at 4 degrees C for 60 d or under repeated freezing and thawing. Broad temperature (25-40 degrees C) and pH (7.0-11.0) stability was observed in the presence of 5 mm Ca(2+). Furthermore, the enzyme was resistant to detergent additives such as non-ionic surfactants and bleaches. It showed considerable potential for industry that requires alkaline-protease.
从中国东部黄海沉积物中分离出一株嗜冷产蛋白酶细菌HW08。基于16S rDNA序列分析和生理特性，该菌株被鉴定为伦登假单胞菌。从培养上清液中纯化出分泌的蛋白酶，命名为Ps5，在SDS-PAGE上显示为表观分子量46 kDa的单体。作为一种金属蛋白酶（受EDTA抑制），该酶在30℃、pH 10.4时表现出最大活性。在4℃下暴露60天或反复冻融后，其活性没有损失。在5 mM Ca(2+)存在下，观察到该酶具有较宽的温度（25-40℃）和pH（7.0-11.0）稳定性。此外，该酶对非离子表面活性剂和漂白剂等洗涤剂添加剂具有抗性。它在需要碱性蛋白酶的工业领域显示出相当大的潜力。
