期刊名称：Advance Journal of Food Science and Technology
印刷版ISSN：2042-4868
电子版ISSN：2042-4876
出版年度：2014
卷号：6
期号：12
页码：1294-1300
DOI：10.19026/ajfst.6.199
出版社：MAXWELL Science Publication
摘要：A Fibrinolytic Enzyme (BSFE) was isolated from fermented chickpeas using Bacillus subtilis . BSFE was purified with ammonium sulfate precipitation, ion exchange and gel filtration chromatography. The fibrin (ogen) olytic activity of BSFE was investigated by means of fibrinolysis plate and hydrolysis of fibrinogen. Through these steps, the purity of the enzyme increased with 74.60-fold with 6.88% recovery activity. The molecular weight of the BSFE was estimated to be 30 kDa by SDS-PAGE. The optimum pH, optimum temperature, pH stability and thermal stability of BSFE were measured, respectively as 8.0, 55°C, 6.0-8.0 and less than 45°C. The activity was inhibited by serine protease inhibitor PMSF as well as metalloprotease inhibitor EDTA, indicating that the BSFE is a serine metalloprotease. In fibrin plate assay, BSFE showed more stronger fibrinolytic activity than that of nattokinase and it specifically hydrolyzed Aα and B&beta chains followed by γ chain of fibrinogen. Therefore, this study provided a method and it for the preparation of multifunctional food of chickpeas which has strong fibrinolytic activity.
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