초록
<P><B>Abstract</B></P><P><I>Proteases constitute more than half of the industrial enzymes sales and among them, alkaline proteases are of high industrial impact. The strain identified as</I> Nocardiopsis <I>UTMC 1492 was isolated from the rhizosphere of</I> Salsola <I>sp. from saline soils. Growth at high concentration of salt and high protease activity introduced the</I> Nocardiopsis <I>UTMC 1492 as a valuable candidate for scale up fermentation and purification of its protease. In spite of 100% identity in 16S rRNA gene of</I> Nocardiopsis <I>sp. UTMC 1492 to</I> N. arvandica, <I>cultural and physiological differences suggest that microenvironment adaptation of a single strain can lead to the significant change in the behavior of the microorganism. Enzyme purification was carried out by two-step Q-sepharose fast protein liquid chromatography (FPLC)</I><I>with pH 11.0 and 8.0, followed by ammonium sulfate precipitation. This enzyme was ∼30 kDa. The partially purified enzyme showed optimum activity at 60°C and pH 9.0. This enzyme showed antioxidant producing peptones by hydrolyzing proteins extracted from rapeseed, which demonstrated its potential capability in food and feed industries.</I></P>