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纳豆激酶酶学性质的初步研究
引用本文:陈晓飞,杜迅,刘安邦,周伏忠,陈国参. 纳豆激酶酶学性质的初步研究[J]. 河南科学, 2008, 26(10)
作者姓名:陈晓飞  杜迅  刘安邦  周伏忠  陈国参
作者单位:河南省微生物工程重点实验室,郑州,450008;河南省微生物工程重点实验室,郑州,450008;河南省微生物工程重点实验室,郑州,450008;河南省微生物工程重点实验室,郑州,450008;河南省微生物工程重点实验室,郑州,450008
基金项目:河南省省属科研单位社会公益项目
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.

关 键 词:纳豆激酶  纤溶活性  酶学性质

Study on the Characterization of Nattokinase
Chen Xiaofei,Du Xun,Liu Anbang,Zhou Fuzhong,Chen Guocan. Study on the Characterization of Nattokinase[J]. Henan Science, 2008, 26(10)
Authors:Chen Xiaofei  Du Xun  Liu Anbang  Zhou Fuzhong  Chen Guocan
Affiliation:Chen Xiaofei,Du Xun,Liu Anbang,Zhou Fuzhong,Chen Guocan (Key Laboratory of Microbial Engineering of Henan Province,Zhengzhou 450008,China)
Abstract: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 Mg2+,was inhibited by Zn2+,Ca2+,Fe2+ and Cu2+ in different degree,and was depressed completely by the presence of Al3+ .
Keywords:nattokinase  fibrinolytic activity  characterization  
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