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枯草芽孢杆菌纤溶酶的纯化及性质研究
引用本文:刘美艳,张健,孙楠,杨玉梅,袁静,曹露莎.枯草芽孢杆菌纤溶酶的纯化及性质研究[J].食品与发酵工业,2007,33(7):42-45.
作者姓名:刘美艳  张健  孙楠  杨玉梅  袁静  曹露莎
作者单位:1. 徐州师范大学生命科学学院,江苏徐州,221116
2. 四川大学生命科学学院,四川成都,610000
基金项目:徐州师范大学校科研和教改项目
摘    要:以从牛肉酱中筛选的1株高产纤溶酶的枯草芽孢杆菌为材料,进行发酵产酶。其发酵液经过硫酸铵盐析、Sephadex G-100凝胶过滤、C M SepharoseCL-6B离子交换层析和电泳制备,得到电泳纯的枯草芽孢杆菌纤溶酶;其分子质量为32.5ku;pI10.9~11.8;具有直接溶解纤维蛋白和激活纤溶酶原的双重作用;胰蛋白酶对此酶无降解作用,对其纤溶活性无影响;该酶在pH4.0~13.0稳定,对温度的适应范围较广。

关 键 词:枯草芽孢杆菌  分离纯化  纤溶酶
修稿时间:2007-01-09

Studies on Purification and Characteristics of a Fibrinolytic Enzyme from Bacillus sp.
Liu Meiyan, Zhang Jian, Sun Nan, Yang Yumei, Cao Lusha.Studies on Purification and Characteristics of a Fibrinolytic Enzyme from Bacillus sp.[J].Food and Fermentation Industries,2007,33(7):42-45.
Authors:Liu Meiyan  Zhang Jian  Sun Nan  Yang Yumei  Cao Lusha
Affiliation:1School of Life Science, Xuzhou Normal University, Xuzhou 221116,China;2School of Life Science, Sichuan University, Chengdu 610000, China
Abstract:Fibrinolytic enzyme were isolated and purified from Bacillus sp. The procedure of purification included ammonium sulphate precipitation, ion-exchange chromatography on CM -Sepharose CL-6B, Sephadex G-100 gel filtration and preparative PAGE electropheresis. This enzyme was proved to be homogeneous in SDS-PAGE electropheresis with molecular weights 32.5 ku and isoelectric point (pI) within 10.9~11.8. Fibrinolytic enzyne not only hydrolyzed fibrin directly, but also activated the plasminogen to plasmin. Effect of pH value, temperature and trypsin on the activities of BFE were studied. The result shows the activities of BFE were stabled within -25~45℃,pH4.0~13.0 . Trypsin had no effect on activities of the BFE.
Keywords:Bacillus sp  purification  fibrinolytic enzyme
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