食品科学 ›› 2012, Vol. 33 ›› Issue (15): 231-234.

• 生物工程 • 上一篇    下一篇

枯草芽孢杆菌纳豆激酶分离纯化及酶学性质

王  刚1,郭明珠2,陈 光1,*   

  1. 1.吉林农业大学生命科学学院 2.长春职业技术学院
  • 收稿日期:2011-06-29 修回日期:2012-05-16 出版日期:2012-08-15 发布日期:2012-09-07
  • 通讯作者: 陈光 E-mail:chg61@163.com
  • 基金资助:

    重组类人胶原蛋白多肽的生物制备及活性研究;纳豆激酶液体发酵条件的优化

Purification and Characterization of Bacillus subtilis Nattokinase

,Guang CHEN   

  • Received:2011-06-29 Revised:2012-05-16 Online:2012-08-15 Published:2012-09-07
  • Contact: Guang CHEN E-mail:chg61@163.com

摘要: 利用30%~70%饱和度的硫酸铵沉淀,Sephadex G-50凝胶过滤层析对浅盘发酵纳豆激酶进行分离纯化并对其酶学性质进行初步研究。以纤维平板法测定纳豆激酶活力,SDS-PAGE检验纯化效果。结果表明:纯化后纳豆激酶为电泳纯,分子质量约27.518kD,纯化倍数和酶活回收率分别为19和42.1%,纳豆激酶最适温度为50℃,最适宜pH值为8.0。

关键词: 纳豆激酶, 枯草芽孢杆菌, 纯化, 酶学特性

Abstract: In this study, nattokinase produced by Bacillus subtilis NK-1 after shallow tray fermentation was separated and purified by 30%-70% saturation ammonium sulfate precipitation and Sephadex G-50 column chromatography and enzymatically characterized. Nattokinase activity was measured by fibrin plate method, and SDS-PAGE was used to analyze its purity. Electrophoresis-pure nattokinase was obtained, with a molecular weight of about 27.518kD. The purification factor and activity recovery were 19 and 42.1%, respectively. The optimal reaction temperature and pH of this enzyme were 50 ℃ and 8.0, respectively.

Key words: nattokinase, Bacillus subtilis, purification, characterization

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