Abstract
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Article Information:
A Fibrinolytic Enzyme Produced by Bacillus subtilis Using Chickpea (Cicer arietinum L.) as Substrate
Ping Xiao, Siping Yao, Rizwan-ur-rehman, Ran Kang and Yanping Wang
Corresponding Author: Yanping Wang
Submitted: May 19, 2014
Accepted: June 18, 2014
Published: December 10, 2014 |
Abstract:
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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 Bβ 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.
Key words: Bacillus subtilis, chickpea fermentation, fibrinolytic activity, Fibrinolytic Enzyme (BSFE) , , ,
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Cite this Reference:
Ping Xiao, Siping Yao, Rizwan-ur-rehman, Ran Kang and Yanping Wang, . A Fibrinolytic Enzyme Produced by Bacillus subtilis Using Chickpea (Cicer arietinum L.) as Substrate . Advance Journal of Food Science and Technology, (12): 1294-1300.
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ISSN (Online): 2042-4876
ISSN (Print): 2042-4868 |
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