Enhanced Production of Fibrinolytic Enzyme from Bacillus amyloliquefaciens CGMCC 7380 Using Broad Bean ( Vicia faba L.) as Substrate

2015 
enzyme is a potent protease with the potential for thrombolytic therapy. In this research, liquid fermentation production fibrinolytic enzyme by a newly isolated Bacillus amyloliquefaciens CGMCC 7380 using broad bean ( Vicia faba L.) as substrate was investigated for the first time. With the B. amyloliquefaciens CGMCC 7380, the design of the optimum medium composition for high-level production of broad bean-fibrinolytic enzyme was attempted by using Plackett-Burman design and Central Composite Design. Maximum protease activity (4900 U/mL) was obtained when the strain was grown in medium containing (g/L): broad bean power 38.0, maltose 32.0, CaCl 2 0.2, K 2 HPO 4 2.0, KH 2 PO 4 2.0, MgCl 2 0.5. Furthermore, in vitr studies revealed that the enzyme could catalyze fibrin clot lysis effectively. And in carrageenan induced mouse tail thrombosis model, tail-thrombus of the enzyme treated group was significantly shorter than the control group indicated that the broad bean-fibrinolytic protease could be a useful thrombolytic agent. Therefore, this study provided a novel method for the preparation of functional food of broad bean and potential thrombolytic drugs.
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