Partial Purification and Characterization of Protease from Abrus precatorius Linn. (Fabaceae) from Cameroon
Open Access
- 1 January 2016
- journal article
- Published by Scientific Research Publishing, Inc. in Advances in Enzyme Research
- Vol. 04 (02), 35-43
- https://doi.org/10.4236/aer.2016.42004
Abstract
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.Keywords
This publication has 1 reference indexed in Scilit:
- Biodiversity in Indian Underexploited/Tribal PulsesPublished by Springer Science and Business Media LLC ,2003