从鱼露中分离出的嗜盐芽孢杆菌属SR5-3的嗜盐丝氨酸蛋白酶：纯化与特性研究
A halophilic serine proteinase from Halobacillus sp. SR5-3 isolated from fish sauce: purification and characterization.
作者信息
Namwong Sirilak, Hiraga Kazumi, Takada Katsumi, Tsunemi Masahiko, Tanasupawat Somboon, Oda Kohei
机构信息
Department of Microbiology, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok.
出版信息
Biosci Biotechnol Biochem. 2006 Jun;70(6):1395-401. doi: 10.1271/bbb.50658.
A halophilic bacterium was isolated from fish sauce, classified, and named Halobacillus sp. SR5-3. A purified 43-kDa proteinase produced by this bacterium showed optimal activity at 50 degrees C and pH 9-10 in 20% NaCl. The activity of the enzyme was enhanced about 2.5-fold by the addition of 20-35% NaCl, and the enzyme was highly stabilized by NaCl. It was found to be a serine proteinase related to either chymotrypsin or subtilisin. It absolutely preferred Ile at the P(2) position of substrates. Thus, the enzyme was found to be a halophilic serine proteinase with unique substrate specificity.
从鱼露中分离出一株嗜盐细菌，对其进行分类并命名为嗜盐芽孢杆菌属SR5 - 3。该细菌产生的一种纯化的43 kDa蛋白酶在20% NaCl溶液中，50℃和pH 9 - 10条件下表现出最佳活性。添加20 - 35% NaCl可使该酶活性提高约2.5倍，且NaCl能使其高度稳定。研究发现它是一种与胰凝乳蛋白酶或枯草杆菌蛋白酶相关的丝氨酸蛋白酶。它绝对优先选择底物P(2)位置为异亮氨酸的情况。因此，该酶是一种具有独特底物特异性的嗜盐丝氨酸蛋白酶。
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