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首页> 外文期刊>Journal of Microbiology, Biotechnology and Food Sciences >PURIFICATION AND CHARACTERIZATION OF EXTRACELLULAR PROTEASE FROM SOIL ISOLATE Stenotrophomonas maltophilia AS NOVEL TARGET FOR FIBRINOLYSIS
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PURIFICATION AND CHARACTERIZATION OF EXTRACELLULAR PROTEASE FROM SOIL ISOLATE Stenotrophomonas maltophilia AS NOVEL TARGET FOR FIBRINOLYSIS

机译：从土壤分离嗜麦芽窄食单胞菌中提纯和表征胞外蛋白酶作为纤溶蛋白的新靶标

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Fibrinolytic protease has a potential role as thrombolytic agent and useful in cardiovascular disease (CVD) treatment. In this study, a potent fibrinolytic protease-producing bacterium was isolated from casein growth medium and identified as Stenotrophomonas maltophilia by characterizing biochemical tests and 16 s rRNA sequencing. The protease production was carried out by submerged fermentation and further purified by ammonium sulphate precipitation, dialysis and ion-exchange chromatography methods. The specific activity of protease significantly increased with step by step of purification process and finally became 1.87 U/mg protein with a purification fold of 1.68 and yield of 59.52%. The sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis showed molecular weight of purified protease as ~47kDa, respectively. To the authors’ knowledge, this is the first report of ～47 kDa protease from the bacterial strain Stenotrophomonas maltophilia. The characterized enzyme exhibits maximal enzyme activity at pH 8 and temperature 40°C. The activity of enzyme is activated by cations Na+, K+, Ca++ and Mg++, whereas significant loss of activity was observed with EDTA, Zn++, Cu++ and Hg++. The Lineweaver-Burk plot analysis showed a km value of 0.303 mg/ml and Vmax as 0.00714. The present study indicates that fibrinolytic protease produced from the Stenotrophomonas maltophilia KJ801664 has an antioxidant property by 1,1-diphenyl-2-picryl-hydrazyl (DPPH) method.
机译：纤溶蛋白酶具有潜在的溶栓作用，可用于心血管疾病（CVD）治疗。在这项研究中，从酪蛋白生长培养基中分离出了一种有效的产生纤维蛋白水解蛋白酶的细菌，并通过表征生化试验和16 s rRNA测序将其鉴定为嗜麦芽窄食单胞菌。通过深层发酵进行蛋白酶生产，并通过硫酸铵沉淀，透析和离子交换色谱法进一步纯化。蛋白酶的比活性随着纯化过程的逐步提高而显着增加，最终变为1.87 U / mg蛋白，纯化倍数为1.68，产率为59.52％。十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDS-PAGE）分析显示，纯化的蛋白酶的分子量分别为〜47kDa。据作者所知，这是细菌嗜麦芽窄食单胞菌的约47 kDa蛋白酶的首次报道。表征的酶在pH 8和40°C的温度下具有最大的酶活性。酶的活性被Na +，K +，Ca ++和Mg ++阳离子激活，而使用EDTA，Zn ++，Cu ++和Hg ++时，酶的活性明显下降。 Lineweaver-Burk图分析显示km值为0.303 mg / ml，Vmax为0.00714。本研究表明，由嗜麦芽窄食单胞菌KJ801664产生的纤溶酶具有通过1，1-二苯基-2-吡啶-2-肼基（DPPH）法的抗氧化性能。

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