摘要
目的分离纯化枯草芽孢杆菌(Bacillus subtilis ZY-1)溶栓酶,探讨该酶的理化性质。方法枯草芽孢杆菌培养,利用(NH4)2SO4沉淀、Sephadex G-100柱层析对该酶发酵液进行分离纯化,利用四肽底物Sue-Ala-Ala-Pro-Phe-PNA作为底物,研究酶的理化性质。结果经发酵并纯化后获得的酶液其比活高达26400U/mg,酶反应最适温度45℃,最适pH8.0,且具有较好的热稳定性。结论枯草芽孢杆菌溶栓酶具有溶血栓作用。
Objective Purification of a fibrinolytic enzyme produced from Bacillus subtilis ZY-1 and investigation of its activity and characterization. Methods A high fibrinolytic enzyme was purified with （NH4）2SO4 fractionation and sephadex G-100 gelfiltration chromatography, and characterization was investigated by check the enzymatic activities in different conditions. Results The specific activity of enzyme was 26 400 U/rag, and its optimal temperature and pH was 45 ℃ and 8.0, respectively. The enzyme had fine thermal heat stability. Conclusion The enzyme had potential commercial value.
出处
《福建医科大学学报》
2008年第2期143-146,共4页
Journal of Fujian Medical University
基金
福建省卫生厅青年基金资助项目(2006-2-7)
福建中医学院校管基金资助项目(X2005002)
