NATURAL PRODUCT RESEARCH AND DEVELOPMENT ›› 2020, Vol. 32 ›› Issue (11): 1937-1942. doi: 10.16333/j.1001-6880.2020.11.018

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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

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

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