Partial Purification and Characterization of Protease from Abrus precatorius Linn. (Fabaceae) from Cameroon - Advances in Enzyme Research

AER > Vol.4 No.2, June 2016

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

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DOI: 10.4236/aer.2016.42004 2,335 Downloads 4,404 Views Citations

Author(s)

Mezajoug Kenfack Laurette Blandine^*, Ngangoum Eric Serge, Tchiégang Clergé

Affiliation(s)

Bioprocess Laboratory, Unit of Food Sciences and nutrition, University Institute of Technology, University of Ngaoundere, Ngaoundere, Cameroon.

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

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

Share and Cite:

Blandine, M. , Serge, N. and Clergé, T. (2016) Partial Purification and Characterization of Protease from Abrus precatorius Linn. (Fabaceae) from Cameroon. Advances in Enzyme Research, 4, 35-43. doi: 10.4236/aer.2016.42004.

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