Isolation, purification and characterization of antimicrobial protein from seedlings of Bauhinia purpurea L

International Journal of Biological Macromolecules
Muthu Sakthivel, Perumal Palani

Abstract

A novel antimicrobial protein was purified from the seedlings of Bauhinia purpurea by sequential procedures entailing ammonium sulfate precipitation, cation exchange chromatography, preparative native-PAGE and a yield of 2.7% was obtained from the crude extract. The purified antimicrobial protein appeared as a single protein band on SDS-PAGE with the molecular mass of 20.9 kDa. Purified antimicrobial protein exhibited a potent antimicrobial activity against both Gram-positive and Gram-negative bacteria. Analysis of the trypsin digested peptides of purified protein using the MALDI-TOF MS/MS resulted in the identification of 174 amino acids. The purified protein had an optimum of pH of 5.5 and was stable at 35 °C for exhibiting its maximal antibacterial activity. The addition of metal ions such as Mn(2+) and Ca(2+) to the purified protein enhanced the antimicrobial activity of purified protein. The MIC of purified protein against Bacillus cereus and Escherichia coli were 13 μg/ml and 15 μg/ml, respectively. The purified protein digested the peptidoglycan layer of bacteria which was visualized by TEM analysis.

References

Sep 29, 2005·Antimicrobial Agents and Chemotherapy·M MeinckenM Rautenbach
Oct 11, 2005·Biotechnology Letters·Kris De Smet, Roland Contreras
Aug 25, 2006·Biochimica Et Biophysica Acta·Burkhard Bechinger, Karl Lohner
Oct 18, 2008·Comptes rendus biologies·Nathalie Munier-JolainChristophe Salon
Sep 3, 2013·Indian Journal of Microbiology·Bhawna Sunil NegiY K Agarwal

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