Research Journal of Engineering and Technology

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Comparative Studies on the Production, Purification, and Characterization of Nattokinase from Blood Fibrin of Bos taurus (Cow) and Ovis aries (Sheep) by Rhizomucor sp


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1 Department of Biotechnology, Madha Engineering College, Chennai 600 069, India
     

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A novel fibrinolytic enzyme from two different blood fibrin Bos taurus and Ovis aries as an added ingredient by Rhizomucor sp. which was purified by ammonium sulphate precipitation, dialysis and ion exchange chromatography. The purification protocol resulted in 1.373 and 1.737 -fold purification of the enzyme. The apparent molecular weight of the enzyme was found to be 30.0kDa, determined by sodium dodecylsulphate poly acrylamide gel electrophoresis. Optimal temperature and pH of the nattokinase were to be at 37°C and 8.0 respectively. Upon the addition of zinc chloride the enzyme activity was increased while EDTA and PMSF inhibited the activity of the enzyme, indicating the presence of metalloproteases. The produced enzyme showcases the blood clot-busting activity.

Keywords

Nattokinase, Bos taurus, Ovis aries, Rhizomucor sp.
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  • Comparative Studies on the Production, Purification, and Characterization of Nattokinase from Blood Fibrin of Bos taurus (Cow) and Ovis aries (Sheep) by Rhizomucor sp

Abstract Views: 249  |  PDF Views: 1

Authors

M. B. Nishita
Department of Biotechnology, Madha Engineering College, Chennai 600 069, India
Remya Rachel Chacko
Department of Biotechnology, Madha Engineering College, Chennai 600 069, India
M. Anil Kumar
Department of Biotechnology, Madha Engineering College, Chennai 600 069, India
D. Suresh
Department of Biotechnology, Madha Engineering College, Chennai 600 069, India
S. Selvanaveen
Department of Biotechnology, Madha Engineering College, Chennai 600 069, India
M. Seenuvasan
Department of Biotechnology, Madha Engineering College, Chennai 600 069, India

Abstract


A novel fibrinolytic enzyme from two different blood fibrin Bos taurus and Ovis aries as an added ingredient by Rhizomucor sp. which was purified by ammonium sulphate precipitation, dialysis and ion exchange chromatography. The purification protocol resulted in 1.373 and 1.737 -fold purification of the enzyme. The apparent molecular weight of the enzyme was found to be 30.0kDa, determined by sodium dodecylsulphate poly acrylamide gel electrophoresis. Optimal temperature and pH of the nattokinase were to be at 37°C and 8.0 respectively. Upon the addition of zinc chloride the enzyme activity was increased while EDTA and PMSF inhibited the activity of the enzyme, indicating the presence of metalloproteases. The produced enzyme showcases the blood clot-busting activity.

Keywords


Nattokinase, Bos taurus, Ovis aries, Rhizomucor sp.