对中国传统细菌型豆豉溶栓酶酶学性质的研究  

Study on the properties of fibrinolysis enzyme of conventional bacteria-type douchi from China

作　　者：张炳文[1] 庞庆芳 孙超 

机构地区：[1]济南大学食品科学与营养系,济南250002 [2]泰安复发中记食品有限公司,山东泰安271033 [3]济南市水业集团有限公司,济南250001

出　　处：《中国调味品》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)

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.

关 键 词：细菌型 豆豉 酶学性质 

分 类 号：TS201.25[轻工技术与工程—食品科学]