【摘要】 目的对以豆渣为原料,接种纳豆菌的发酵物分离纯化和酶学性质研究。方法采用生理盐水浸提、(NH4)2SO4分级沉淀、Sephadex G-100凝胶层析等纯化步骤,得到层析纯的食源性溶栓酶-纳豆激酶,结果经聚丙烯酰胺凝胶电泳显示为二个组分。酶学性质研究表明,以酪蛋白为底物时,最适反应温度为60℃,最适反应pH为8.0,在pH7~9溶液中,37℃以下基本稳定。体外溶栓作用表明,纳豆激酶溶解纤维蛋白的方式主要是直接溶解,而不是纤溶酶原激活剂。更多还原

【Abstract】 To study properties of nattokinase,a kind of food fibrinolytic enzyme was made by solid fermentation from soybean residue.It was extracted and purified by ammonium sulfate precipitation followed by Sephadex G-100 chromatography.The purified enzyme contained two stainable subunits on the gel of SDS-PAGE.The optimum temperature and pH for hydrolysis of casein were 60℃ and 8.0,respectively.The enzyme was stable up to 37℃,within the pH range of 7-9.The fibrinolysis activity was performed by degrading the fibrous protein directly,according to the experiment in vitro.更多还原