摘要
试验以通过硫酸铵沉淀、DEAE-Sepharose FF离子交换层析、Sephadex G-75凝胶过滤等技术分离得到分子量在31ku的细菌型豆豉溶栓酶为研究对象，对其酶学性质进行了研究探讨，发现此酶的最适作用温度为60℃，pH7～8时酶活性最高，在pH6～10的范围内稳定性较强；该酶没有明显的金属离子激活剂，高浓度的Cu^2＋，Fe^3＋，Al^3＋对此酶有抑制作用；添加蛋白胨、明胶可以提高酶的活性；抑制剂PMSF对豆豉溶栓酶抑制率几乎达到100％，EDTA、β-巯基乙醇对酶活几乎无抑制作用。
Fibrinolysis enzyme which molecular weight was approximately 31 lcu. was separated and purified by ammonium sulfate of summation 75 %, by DEAE-Sepharose and by Sephadex G-75. SDS-PAGE. The properties of fibrinolysis enzyme was discussed in experimentation. The optimal reaction temperature and pH of fibrinolysis enzyme was 60 ℃ ,pH 7-8 respectively. From pH 6 - 10, fibrinolysis enzyme exhibited high stability . There were not metal ion that can activate the enzyme; but the higher concentration Cu^2＋ , Fe^3＋ , Al^3＋ had some deactivation effect. Glutin and peptone could activate the enzyme. The 0.1 mm PMSF could totally deactivate fibrinolysis enzyme. EDTA and β-thiol ethyl acid were not apparent influence.
出处
《中国调味品》
CAS
北大核心
2008年第12期45-49,共5页
China Condiment
基金
山东省自然科学基金资助项目(Y2007D76)
关键词
细菌型
豆豉
酶学性质
Bacteria-type
Douchi
properties of enzymology
