M.B. Nishita, Remya Rachel Chacko, M. Anil Kumar, D. Suresh, S. Selvanaveen, M. Seenuvasan
M.B. Nishita, Remya Rachel Chacko, M. Anil Kumar, D. Suresh, S. Selvanaveen and M. Seenuvasan*
Department of Biotechnology, Madha Engineering College, Chennai 600 069, India.
Volume - 2,
Issue - 1,
Year - 2011
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.
Cite this article:
M.B. Nishita, Remya Rachel Chacko, M. Anil Kumar, D. Suresh, S. Selvanaveen , M. Seenuvasan. Comparative Studies on the Production, Purification, and Characterization of Nattokinase from Blood Fibrin of Bos taurus (Cow) and Ovis aries (Sheep) by Rhizomucor sp. Research J. Engineering and Tech. 2(1): Jan.-Mar. 2011 page 10-16.