Mezajoug Kenfack, L.B., Ngangoum, E.S., Linder, M. and Tchiégang, C. (2014) Proteolytic Enzymes from Abrus precatorius Linn., Burnatia enneandra Micheli. And Ziziphus mauritiana Lam: Optimization of the Extraction Process by Response Surface Methodology. The Journal of Bioprocess Technology, 100, 453-451.

has been cited by the following article:

• TITLE: Partial Purification and Characterization of Protease from Abrus precatorius Linn. (Fabaceae) from Cameroon

  AUTHORS: Mezajoug Kenfack Laurette Blandine, Ngangoum Eric Serge, Tchiégang Clergé

  KEYWORDS: A. precatorius, Cameroon, Proteases, Partial Purified Extract, Proteolytic Activity

  JOURNAL NAME: Advances in Enzyme Research, Vol.4 No.2, May 27, 2016

  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.