蛋白酶产生菌的化学诱变及酶学性质
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国家 “863”计划 (2006AA10A210)和国家自然科学基金项目(30500332)资助


Chemomorphosis and Enzymatic Characterization of Proteinase-Producing Bacillus subtilis
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    摘要:

    对1株产蛋白酶的枯草芽胞杆菌(Z5)进行化学诱变,筛选得到1株产较高酶活性、大分子质量蛋白酶的菌株。检测该蛋白酶对底物明胶的分解能力,发现该蛋白酶的分子质量约为100 ku,还原剂巯基乙醇对其活性的影响较大。在不同温度、不同pH值处理该蛋白酶后,用茚三酮法测定酶活性,发现该蛋白酶催化反应的最适pH为6,最适温度为50℃,并且该蛋白酶有较好的热稳定性,70 ℃处理10 min仍能保留50%左右的酶活性。由于此蛋白酶在分子质量及最适pH方面均不同于已报道过的枯草芽胞杆菌蛋白酶,推测其为一种新型的蛋白酶。

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    Bacillus subtilis mutant with improved protease activity was obtained using DES treatment.The approximate molecular weight of this protease was obtained using gelatin as a substrate,and effects of mercaptoethanol on the protease activity were detected as well.The protease was treated under different temperatures and pH conditions.The enzyme activity was examined using ninhydrin.The molecular weight of the purified enzyme was estimated to be 100 ku by SDS-PAGE.The optimum pH and temperature was 6.0,50 ℃.About 50% enzymatic activity was retained after incubation at 70 ℃ for 10 min.The enzyme activity was significantly influenced by mercaptoethanol.Based on the difference of molecular weight and optimum pH from reported protease of Bacillus subtilis,it indicated that this protease was a new-type with wide applications.

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马宏宇,李菁菁,祁高富,喻子牛,赵秀云.蛋白酶产生菌的化学诱变及酶学性质[J].华中农业大学学报,2010,29(6):737-740

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  • 收稿日期:2009-12-19
  • 最后修改日期:2010-06-24
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