%0 Journal Article %T Partial Purification and Characterization of Protease from <i>Abrus precatorius</i> Linn. (Fabaceae) from Cameroon %A Mezajoug Kenfack Laurette Blandine %A Ngangoum Eric Serge %A Tchi¨¦gang Clerg¨¦ %J Advances in Enzyme Research %P 35-43 %@ 2328-4854 %D 2016 %I Scientific Research Publishing %R 10.4236/aer.2016.42004 %X Crude enzyme extracts were prepared from leaves and stems of Linn. (Fabaceae) from Cameroon under optimized conditions. Proteolytic enzymes were precipitated with ammonium sulfate at 35% (w/v) saturation and assayed for enzyme activity. The effects of temperature, pH, incubation time and substrate specificity were studied. SDS-PAGE was used to determine molecular weight of precipitated protease. Results indicated that proteolytic activity of crude extract was 35.20 U/ml compared to 51.03 U/ml of partial purified extract. The optimum enzyme activity was found to be at 40°C, while 50% of activity was maintained at 60°C after 60 min incubation. Partial purified crude extract exhibited two optimum pH (2.75 and 9.0). The highest enzyme activity towards Bovine Serum Albumine (25.9 U/ml) was noted. SDS-PAGE gels exhibited molecular weight between 40 - 60 KDa. This result confirms that partial purified extract of A. precatorius contains proteases and could be a promising source for proteolytic enzyme extraction. %K < %K i> %K A. precatorius< %K /i> %K Cameroon %K Proteases %K Partial Purified Extract %K Proteolytic Activity %U http://www.scirp.org/journal/PaperInformation.aspx?PaperID=66829