Production, purification and crystallization of an alkaline protease from Aspergillus tamarii[EF661565.1]

摘要

An extracellular alkaline serine protease has been purified from a strain of Aspergillus tamarii [EF661565.1] to homogeneity, by ammonium sulphate precipitation and chromatography on CM-Cellulose. Its molecular weight estimated by SDS-PAGE was 63 kDa. Maximum protease activity was observed at pH 8-9 and 60?C temperature. The protease was strongly inhibited by PMSF. The activity of enzyme was enhanced by Zn+2 and Mg+2. A strong inhibitory effect was observed in the presence of Hg+2, Co+2and Ca+2 ion. The crystallization of purified enzyme was performed by ammonium sulphate.