Research on Purification and Fibrinolytic Activity Assay of Nattokinase from Natto

Abstract

Abstract: The nattokinase was purified from natto through procedures of saline extraction, ammonium sulfate precipitation, and SephadexG-100 gel chromatograph purification with a fold of 15.6 and overall yield of 10.2%. The purified enzyme contained two protein components with molecular weight about 29kD by SDS-PAGE. Properties of fibrinolytic activity showed nattokinase. Its optimum pH was 8, stable within pH 6～10 and below 40℃, but inactivated completely below pH5. Under simulating acid environment of stomach, the fibrinolytic activity of crude extract of nattokinase lost completely while 25% of the saline extract of natto retained. The SDS-PAGE results showed that the nattokinase could not be hydrolyzed by trypsin. Nattokinase could hydrolyze fibrin directly rather than by activating plasminogen in vitro.

Key words: nattokinase, purification, fibrinolytic activity

WANG Ping, CHEN Jun, YANG Xiao-Ming, BAO Yan-Xia. Research on Purification and Fibrinolytic Activity Assay of Nattokinase from Natto[J]. FOOD SCIENCE, 2005, 26(2): 59-63.

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Research on Purification and Fibrinolytic Activity Assay of Nattokinase from Natto

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