摘要
本实验室从亚洲传统发酵食品——虾酱中筛选到一株产纤溶酶能力较强的芽孢杆菌(Bacillus sp.nov.SK006),发酵液经乙醇沉淀、离子交换色谱(DEAE-Sepharose CL6B)、凝胶过滤色谱(Superdex75)后分离纯化出一种电泳纯的纤溶酶SPFE-Ⅲ,分子量约为42.6kDa,酶活为7.1U/mg(以plasmin为标准)。SPFE-Ⅲ对纤维蛋白原的降解过程为最先降解α链,其次是γ链,而对β链的降解最缓慢;利用加热纤维蛋白平板法研究纤溶酶SPFE-Ⅲ,结果发现该酶对纤维蛋白有直接降解作用,而对纤维蛋白溶解酶原的敏感性较低。
A novel fibrinolytic enzyme （SPFE-Ⅲ） was produced by Bacillus sp. nov. SK006 isolated from fermented shrimp paste, and purified by a combination of ethanol precipitation, DEAE-Sepharose CL 6B ion exchange chromatography, and Superdex 75 gel filtration chromatography. The molecular weight and specific activity of the achieved SPFE-Ⅲ were 42.6 kDa and 7.1 U/mg （using plasmin as a standard）, respecively. Fibrin clots can be effectively degraded by SPFE-Ⅲ via direct fibrinolysis. The α-subunits of fibrinogen were firstly cleaved, followed by the 7-chains, while the β-chains were resistant to the enzyme digestion. SPFE-Ⅲ had potential application in the preparation of functional foods and new therapeutic agents for thrombosis.
出处
《现代食品科技》
EI
CAS
2008年第8期751-755,共5页
Modern Food Science and Technology
基金
江苏省国际技术合作计划(BZ2007036)
