%0 Journal Article
%T Purification and Biochemical Characterization of Fibrinolytic Enzyme Produced by Thermophilic Fungus Oidiodendron flavum
%A Nagwa A. Tharwat
%J Biotechnology
%D 2006
%I Asian Network for Scientific Information
%X Fibrinolytic enzyme isolated from thermophilic fungus Oidiodendron flavum, precipitated by ammonium sulfate (70% saturation) and subsequent purification using DEAE-Cellulose and Sephadex G-25 columns, then produce one clear band on SDS-PAGE at molecular weight 22,000 Da. The purified fibrinolytic enzyme was active over a wide range of pH (6.0-11.0) with optimum point at pH 8.0. The enzyme was most active at 45 and 55ˇăC all over the incubation time, but lost substantial activity upon incubation at more than 65ˇăC. Upon heating to 70ˇăC for 30 min, the activity completely disappeared. The enzyme activities were found to be enhanced by Mg2+ and Ca2+, but were inhibited by the Co2+, Cu2+, Zn2+ and Fe2+ ions, while Hg2+ at low concentrations strongly inhibited the enzyme activity.
%K Fibrinolytic enzyme
%K Oidiodendron flavum
%K fibrin plate method
%K purification
%K biochemical characterization
%U http://docsdrive.com/pdfs/ansinet/biotech/2006/160-165.pdf