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首页> 外文期刊>Preparative biochemistry & biotechnology: An international journal for rapid communication >Detergent-compatible, organic solvent-tolerant alkaline protease from Bacillus circulans MTCC 7942: Purification and characterization
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Detergent-compatible, organic solvent-tolerant alkaline protease from Bacillus circulans MTCC 7942: Purification and characterization

机译：来自马氏杆菌芽孢杆菌MTCC 7942的与洗涤剂兼容的，耐有机溶剂的碱性蛋白酶：纯化和表征

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摘要

Proteases are now recognized as the most indispensable industrial biocatalyst owing to their diverse microbial sources and innovative applications. In the present investigation, a thermostable, organic solvent-tolerant, alkaline serine protease from Bacillus circulans MTCC 7942, was purified and characterized. The protease was purified to 37-fold by a three-step purification scheme with 39% recovery. The optimum pH and temperature for protease was 10 and 60 degrees C, respectively. The apparent molecular mass of the purified enzyme was 43kD as revealed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The K-m and V-max values using casein-substrate were 3.1mg/mL and 1.8 mu mol/min, respectively. The protease remained stable in the presence of organic solvents with higher (>3.2) log P value (cyclohexane, n-octane, n-hexadecane, n-decane, and n-dodecane), as compared to organic solvents with lower (<3.2) log P value (acetone, butanol, benzene, chloroform, toluene). Remarkably, the protease showed profound stability even in the presence of organic solvents with less log P values (glycerol, dimethyl sulfate [DMSO], p-xylene), indicating the possibility of nonaqueous enzymatic applications. Also, protease activity was improved in the presence of metal ions (Ca2+, Mg2+, Mn2+); enhanced by biosurfactants; hardly affected by bleaching agents, oxidizing agents, and chemical surfactants; and stable in commercial detergents. In addition, a protease-detergent formulation effectively washed out egg and blood stains as compared to detergent alone. The protease was suitable for various commercial applications like processing of gelatinous film and as a compatible additive to detergent formulation with its operative utility in hard water.
机译：蛋白酶由于其多种微生物来源和创新的应用，现已被认为是最不可缺少的工业生物催化剂。在本研究中，纯化并鉴定了来自环状芽孢杆菌MTCC 7942的耐高温，耐有机溶剂的碱性丝氨酸蛋白酶。通过三步纯化方案将蛋白酶纯化至37倍，回收率为39％。蛋白酶的最佳pH和温度分别为10和60摄氏度。经十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDS-PAGE）显示，纯化的酶的表观分子量为43kD。使用酪蛋白底物的K-m和V-max值分别为3.1mg / mL和1.8μmol/ min。与具有较低（<3.2）log P值的有机溶剂（环己烷，正辛烷，正十六烷，正癸烷和正十二烷）相比，该蛋白酶在存在稳定的有机溶剂的情况下仍保持稳定）log P值（丙酮，丁醇，苯，氯仿，甲苯）。值得注意的是，该蛋白酶即使在具有较小log P值的有机溶剂（甘油，硫酸二甲酯[DMSO]，对二甲苯）的存在下也显示出深远的稳定性，表明有可能进行非水酶应用。同样，在金属离子（Ca2 +，Mg2 +，Mn2 +）存在下，蛋白酶的活性也得到改善。由生物表面活性剂增强;几乎不受漂白剂，氧化剂和化学表面活性剂的影响;在商业洗涤剂中稳定。另外，与单独的洗涤剂相比，蛋白酶洗涤剂制剂可有效洗净蛋和血渍。该蛋白酶适用于各种商业应用，例如凝胶状薄膜的加工，并且作为洗涤剂配方的相容性添加剂，在硬水中具有有效的实用性。

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