天然产物研究与开发 ›› 2020, Vol. 32 ›› Issue (11): 1937-1942.doi: 10.16333/j.1001-6880.2020.11.018

• 开发研究 • 上一篇    下一篇

好食脉孢霉纤溶酶的纯化及体外纤溶活性研究

邓永平1,2,车鑫1,艾瑞波1,刘晓兰1,2*,郭建华1,2


  

  1. 1齐齐哈尔大学 食品与生物工程学院;2黑龙江省玉米深加工理论与技术重点实验室,齐齐哈尔 161006

  • 出版日期:2020-11-28 发布日期:2020-12-07
  • 基金资助:
    国家自然科学基金面上项目(31301414);黑龙江省省属高等学校基本科研业务费科研项目“粮头食尾”专项(LTSW201740)

Study on purification and in vitro fibrinolytic activity of fibrinolytic enzyme from Neurospora sitophila

DENG Yong-ping1,2,CHE Xin1,AI Rui-bo1,LIU Xiao-lan1,2*,GUO Jian-hua1,2#br#

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  1. 1College of Food and Biotechnology,Qiqihar University;2Key Laboratory of Corn Deep Proessing Theory and Techology,Qiqihar University,Qiqihar 161006,China

  • Online:2020-11-28 Published:2020-12-07

摘要: 从公认安全真菌好食脉孢霉(Neospora sitophila)代谢产物中纯化了一种纤溶酶,纯化倍数为86.6倍,比活力为519.59 U/mg。该酶由两个分子量分别为30.0 kDa和15.5 kDa的亚基构成,是一种丝氨酸蛋白酶,能依次水解人血纤维蛋白原的Aα、Bβ和γ链,具有直接水解纤维蛋白以及激活纤溶酶原的双重功能。该酶不水解人血清白蛋白。结果表明,好食脉孢霉纤溶酶可能在治疗血栓中具有潜在的应用价值。


关键词: 好食脉孢霉, 纤溶酶, 纯化, 体外纤溶活性

Abstract:

A fibrinolytic enzyme had been purified from the GRAS (generally eecognized as safe) fungus,Neurospora sitophila.The purification fold of fibrinolytic enzyme was 86.6,and the specific activity was 519.59 U/mg.The enzyme,a serine protease,is composed of two subunits with relative molecular weights of 30.0 kDa and 15.5 kDa respectively.It can hydrolyze the Aα,Bβ and γ chains of human fibrinogen in turn.It has the dual functions of directly hydrolyzing fibrin and activating plasminogen.The enzyme can not hydrolyze human serum albumin.These results suggest that fibrinolytic enzyme from Neurospora sitophila may have potential applications in treating thrombosis.

Key words: Neurospora sitophila, fibrinolytic enzyme, purification, in vitro , fibrinolytic activity

中图分类号:  Q814.1