[1]满丽莉,向殿军.来源于豆豉的枯草芽孢杆菌MX-6所产纳豆激酶的稳定性研究[J].中国调味品,2019,(07):25-28.
　1,2*[J].CHINA CONDIMENT,2019,(07):25-28.
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来源于豆豉的枯草芽孢杆菌MX-6所产纳豆激酶的稳定性研究()
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《中国调味品》[ISSN:1000-9973/CN:23-1299/TS]

卷:
期数:
2019年07期
页码:
25-28
栏目:
出版日期:
2019-07-20

文章信息/Info

Title:
1,2*
作者:
满丽莉; 向殿军
文献标志码:
A
摘要:
以中国豆豉中筛选到的一株纤溶酶高产菌株-枯草芽孢杆菌MX-6为研究对象，应用聚合酶链式反应（PCR）成功扩增到1473 bp的纤溶酶编码基因aprN，系统进化树结果显示该纤溶酶为纳豆激酶。研究了纳豆激酶对热、pH、金属离子、化学物质及抑制剂和变性剂的稳定性及传代稳定性。结果表明纳豆激酶在-20、4、30～50 ℃的热稳定性较好，pH在3～11之间酶活性相对稳定，Mg2+、Ca2+对纳豆激酶具有显著的激活作用，K+、Fe2+对纳豆激酶的稳定性基本无影响，而Mn2+、Zn2+、Cu2+、Al3+、Ba2+有显著的抑制作用，Hg2+导致纳豆激酶完全失活，牛血清蛋白、明胶、蛋白胨能够显著提高纳豆激酶的稳定性，丙二醇、海藻酸钠对纳豆激酶的稳定性基本无影响，而乙醇显著降低纳豆激酶的稳定性。PMSF导致纳豆激酶活性的完全丧失，EDAT和DTT对纳豆激酶的活性基本无影响，10 mM的SDS显著降低纳豆激酶的稳定性，说明此纳豆激酶是一种丝氨酸蛋白酶，不是金属酶，不含二硫键，且具有良好的传代稳定性。结果显示该酶的稳定性较好，具有开发为溶栓药物的应用价值，有利于纳豆激酶的工业化应用。
Abstract:
high plasmin-productive strain isolated from chinese douchi, was used as the research subject, and 1473 bp of the gene encoding plasmin in B. subtilis MX-6 was amplified by polymerase chain reaction (PCR). The results of phylogenetic tree showed that the plasminase was nattokinase. The stability of nattokinase to heat, pH, metal ions, chemicals, inhibitors and denaturants, and generation were studied. The thermal stability of nattokinase was better at -20, 4, 30～50 ℃, and the activity of nattokinase was relatively stable in the range of 3～11. Mg2+, Ca2+ have significant activation effect on nattokinase activity, K+, Fe2+ have no effect on the stability of nattokinase, while Mn2+, Zn2+, Cu2+, Al3+, and Ba2+ have significant inhibitory effect, Hg2+ leads to complete inactivation of nattokinase activity. Bovine serum protein, gelatin and peptone could significantly increase the stability of nattokinase, propanediol and sodium alginate had no effect on the stability of nattokinase, while ethanol significantly decreased the stability of nattokinase. PMSF caused the complete loss of nattokinase activity, EDAT and DTT had no effect on the activity of nattokinase, the SDS of 10 mM significantly reduced the stability of nattokinase, indicating that the nattokinase is a serine protease, not a metalloenzyme, and does not contain disulfide bonds. And it has good generation stability. The results show that the enzyme has good stability and the value of application as thrombolytic drugs, which is beneficial to the industrial application of nattokinase.
更新日期/Last Update: 2020-06-22