摘要
以产纤溶酶的根霉菌8B进行发酵,发酵液通过蒸发浓缩、(NH_4)_2SO_4分级沉淀、透析除盐、DEAE阴离子交换纤维素层析、Sephadex G—75凝胶过滤层析对该酶进行纯化,纯化浓缩后酶液活力达到3 978.5U/ mL。结果表明,该纤溶酶在-18～37℃,pH 5～7时性质稳定。该酶即能直接分解纤维蛋白,又能激活血纤维蛋白溶酶原,间接分解纤维蛋白。对家兔血栓的溶解实验表明,8B纤溶酶6h对血栓的溶解率达到52.4%,并且对兔血细胞没有明显损伤,在体外是安全有效的。
In this research, the fibrinolytic enzyme was produced from the strain of Rhizopus 8B. The enzyme was purified by circumrotate evaporation, ammonium sulfate precipitation, dialysis, freezing dehydrate, centrifuge deposit, DEAE-cellulose ion exchange and Sephadex G-75 gel filtration. The activity of the enzyme reaches 3 978.5U/ml. Under the conditions of temperature ranged -18-37℃ and pH 5-7, the enzyme showed very good stability. According to the results, the enzyme might contain both a fibrinolytic enzyme which degraded fibrin directly and a plasminogen activator which degraded fibrin by activating plasminogen. 52.4% of the rabbit gore could be dissolved by the concentrated fibrinolytic enzyme in 6h and the blood corpuscle can＇t be destroyed. The enzyme is safe and effective in vitro.
出处
《食品与发酵工业》
CAS
CSCD
北大核心
2007年第10期99-102,共4页
Food and Fermentation Industries
关键词
纤溶酶
纯化
根霉菌
fibrinolytic enzyme, purification, Rhizopus
