Protease from A. sisalana was partial purified by precipitation by 25-80 % ammoniumsuifete precipitation, Sephadex G-100 column and DEAE -cellulose column chromatography. The purification obtained was 25.41 fold with specific activity of 4.32 Units/mg protein and %yeild of 186.65 %. Activity stain after non- denaturing gel electrophoresis with 0.5% casein as substrate showed a single band The molecular weight of 21,800 was shown with Sephadex G-100 column chromatography. The pH optimum of this enzyme was 7.5 and the temperature optimum was 65 °C, the enzyme was stable at pH 8.3 and 20-40 °C, respectively. The kinetic study of partial purified enzyme showed Km of 0.084, 0.161 and 0.877 % by weight for casein, BSA and hemoglobin respectively. The enzyme also showed specificity towards peptide of G-terminal side of leucine. Mn2-, Cd2+ HgClr p-chloromercuricbenzoate and iodoacetamid could inhibit protease activity while Na2S2O5 , diithiothreitol and 2-mercaptoethanol, activated the enzyme. These results suggested that the enzyme from A. sisalana was sulfhydyl protease