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Purification and Characterization of Fibrinolytic Protease From Bacillus Amyloliquefaciens MCC2606 and Analysis of Fibrin Degradation Product by MS/MS

Purification and Characterization of Fibrinolytic Protease From Bacillus Amyloliquefaciens MCC2606 and Analysis of Fibrin Degradation Product by MS/MS

Yogesh Devaraj, Savita Kumari Rajender, Prakash Motiram Halami

Prep Biochem Biotechnol. 2018 Feb 7;48(2):172-180.

PMID: 29341842

Abstract:

A serine protease with preference for fibrin protein was purified and characterized from Bacillus amyloliquefaciens MCC2606, isolated from dosa batter. The protease was purified using ammonium sulfate precipitation, ion-exchange, and gel filtration chromatography. The degradation activity of the protease toward the fibrin was significantly higher compared with other protein substrates in the study. The molecular weight of the CFR15-protease was estimated to be 32 kDa based on SDS-PAGE. The purified enzyme exhibited both fibrinolytic and fibrinogenolytic activity. The optimum pH and temperature for the activity of the enzyme was found to be 10.5 and 45°C. A significant inhibition was seen with the protease inhibitors phenyl methyl sulphonyl fluoride and ethylene diamine tetra acetic acid and the activity of the enzyme was enhanced in presence of Mn2+. There was an observed increase in vitro activated partial thromboplastin time and prothrombin time of both time and dose dependent study. Among the four chains of fibrin, the β-chain of fibrin appears to be the primary component and site susceptible for CFR15-protease in early action as indicated by MS/MS analysis of initial degradation products. These results indicated that the CFR15-protease have the potential to be an effective fibrinolytic agent.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR424813	Protease from Bacillus amyloliquefaciens			Price

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