蜡样芽孢杆菌SRM-001分泌的纤溶酶的纯化、生化及热学性质
Purification, biochemical, and thermal properties of fibrinolytic enzyme secreted by Bacillus cereus SRM-001.
作者信息
Narasimhan Manoj Kumar, Ethiraj Selvarajan, Krishnamurthi Tamilarasan, Rajesh Mathur
机构信息
a Department of Genetic Engineering, School of Bioengineering , SRM University , Kattankulathur , Tamil Nadu , India.
b Department of Chemical Engineering , School of Bioengineering, SRM University , Kattankulathur , Tamil Nadu , India.
出版信息
Prep Biochem Biotechnol. 2018 Jan 2;48(1):34-42. doi: 10.1080/10826068.2017.1387560. Epub 2018 Jan 3.
The discovery of microbial fibrinolytic enzymes is essential to treat cardiovascular diseases. This study reports the discovery of a fibrinolytic enzyme secreted by Bacillus cereus SRM-001, a microorganism isolated from the soil of a chicken waste-dump yard. The B. cereus SRM-001 was cultured and the secreted fibrinolytic enzyme purified to show that it is a ∼28 kDa protein. The purified enzyme was characterized for its kinetics, biochemical and thermal properties to show that it possesses properties similar to plasmin. A HPLC-MS/MS analysis of trypsin digested protein indicated that the fibrinolytic enzyme shared close sequence homology with serine proteases reported for other Bacillus sp. The results show that the B. cereus SRM-001 secreted enzyme is a ∼28 kDa serine protease that possesses fibrinolytic potential.
微生物纤溶酶的发现对于治疗心血管疾病至关重要。本研究报告了从鸡粪堆肥场土壤中分离出的蜡样芽孢杆菌SRM-001所分泌的一种纤溶酶的发现。对蜡样芽孢杆菌SRM-001进行培养，并对分泌的纤溶酶进行纯化，结果表明它是一种约28 kDa的蛋白质。对纯化后的酶进行了动力学、生化和热性质表征，结果表明它具有与纤溶酶相似的性质。对胰蛋白酶消化后的蛋白质进行的HPLC-MS/MS分析表明，该纤溶酶与其他芽孢杆菌属报道的丝氨酸蛋白酶具有密切的序列同源性。结果表明，蜡样芽孢杆菌SRM-001分泌的酶是一种约28 kDa的丝氨酸蛋白酶，具有纤溶潜力。
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