A moderately halophilic protease producer, Bacillus sp. strain isolated from sea water is described. The protease is purified to homogeneity by ammonium sulphate precipitation and CM cellulose chromatography. The serine protease has a molecular mass of 29 kDa. Enzymatic characterization of protease revealed K(m) 2.22 mg mL(-1), Vmax 1111.11 U mL(-1), pH optimum 9.0, t1/2 190 min at 60°C and salt optima 1% (w/v) NaCl. The protease is remarkably stable in hydrophilic and hydrophobic solvents at high concentrations. The purified preparation is unstable at room temperature. Ca(2+) ions are required for preventing this loss of activity. Interestingly, the activity and stability are modulated differentially. Whereas, divalent cation Ca(2+) are involved in maintaining stability in solution at room temperature by preventing unfolding, monovalent Na(+) and K(+) ions participate in regulating the activity and assist in refolding of the enzyme. Application of the protease is shown in efficient removal of blood stain.

译文

中度嗜盐蛋白酶生产者,芽孢杆菌属。描述了从海水中分离的菌株。通过硫酸铵沉淀和二1212纤维素色谱法将蛋白酶纯化至均质。丝氨酸蛋白酶的分子量为29 kDa。蛋白酶的酶促表征显示K(m) 2.22 mg mL(-1),Vmax 1111.11 U mL(-1),pH最适9.0,60 °C下的t1/2 190分钟和盐最适1% (w/v) NaCl。蛋白酶在高浓度的亲水和疏水溶剂中非常稳定。纯化的制剂在室温下不稳定。需要Ca(2) 离子来防止这种活性损失。有趣的是,活性和稳定性受到不同的调节。鉴于二价阳离子Ca(2) 通过防止展开而参与在室温下维持溶液的稳定性,单价Na () 和K () 离子参与调节活性并协助酶的重折叠。蛋白酶的应用可有效去除血迹。

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