纳豆激酶酶学性质的初步研究  

Study on the Characterization of Nattokinase

作　　者：陈晓飞[1] 杜迅[1] 刘安邦[1] 周伏忠[1] 陈国参[1] 

机构地区：[1]河南省微生物工程重点实验室,郑州450008

出　　处：《河南科学》2008年第10期1212-1214,共3页Henan Science

基　　金：河南省省属科研单位社会公益项目(0641180203)

摘　　要：通过(NH4)2SO4对NK分级盐析浓缩,发现用饱和度为65%的(NH4)2SO4盐析,浓缩10倍,NK回收率最高,可达到87.1%.对其纤溶活性研究表明,NK在40℃以下时,纤溶活性相对稳定,65℃以上时,活性迅速下降;pH<4时,显著抑制NK活性;Mg2+对其纤溶活性有显著激活作用,Zn2+,Ca2+,Fe2+和Cu2+对NK有不同的抑制作用,而Al3+则使NK活性完全丧失.The nattokinase （NK） was purified from natto through procedures of saline extraction, ammonium sulfate precipitation,we found that,when the saturation of ammonium sulfate was 65 %,the overall yield of NK was 87.1%. It＇s stable below 40 ℃, but the activity of fibrinolytic activity descend rapidly upwards 65 ℃. It＇s inactivated below pH 4. The fibrinolytic activity was strongly activated by Mg^2＋,was inhibited by Zn^2＋, Ca^2＋, Fe^2＋ and Cu^2＋ in different degree, and was depressed completely by the presence of Al^3＋.

关 键 词：纳豆激酶 纤溶活性 酶学性质 

分 类 号：TQ920.1[轻工技术与工程—发酵工程]