PURIFICATION AND BIOCHEMICAL CHARACTERIZATION OF NOVEL FIBRINOLYTIC PROTEASE PRODUCED BY MESOPHILIC BACILLUS CIRCULANS GD25
AbstractA novel fibrinolytic protease from Bacillus circulansGD25 was isolated and characterized for the fibrinolytic activity. The fibrinolytic protease was purified by ammonium sulphate fractionation (70%) and subjected to chromatographic methods like Sephadex G-50, DEAE –Sephadex A-50 columns. The purified enzyme has an approximately 38 kDa in size by SDS-PAGE and gel filtration. Optimum activity was at 35ºC and the enzyme was highly active over a wide range of pH from 7.0-9.0 with an optimum at pH 8.0. It exhibited stronger fibrinolytic protease activity. The activity was slightly enhanced by Ca2+ and Mg2+ whereas Zn2+, Cu2+, Co2+ and Fe2+ suppressed the activity. The fibrinolytic protease activity was totally lost in the presence of PMSF, suggesting that the purified enzyme is a serine metallo-protease with potential application in thrombolytic therapy
Article Information
10
4559-4566
536KB
1299
English
IJPSR
E. Venkata Naga Raju* and Divakar Goli
Department of Biotechnology & Microbiology, Acharya & B.M. Reddy College of Pharmacy, Soldevanahalli, Hesaraghatta, Bengaluru-560107, Karnataka, India
venkatanagarajue@gmail.com
07 July, 2013
26 August, 2013
23 November, 2013
http://dx.doi.org/10.13040/IJPSR.0975-8232.4(12).4559-66
01 December 2013
Download