The partial, purification and characterization of antimicrobial peptide (AMP) from the hemolymph of cockroach, Periplaneta americana was studied. Hemolymph was drawn from cockroach and the antimicrobial peptide was purified on sephadex G-75 gel filtration column. The gel filtration showed 2 peaks, I and II and only peak II showed five active fractions viz. 12, 13, 14, 15 and 16 of antimicrobial activity, and fraction 13 showed the highest Microbial Inhibition concentration (MIC), and showed a single protein band on SDS-PAGE with the molecular mass of 60.2kDa. Purified antimicrobial protein exhibited a highest antimicrobial activity against E. coli at temperature 30˚C, pH 6.0, and at 5mM calcium ion. The antimicrobial peptide, showed a higher activity of MIC against Lipopolysaccharides(LPS) and β- 1,3 glucan at 5h of exposure. The study concludes that the antimicrobial peptide from hemolymph, was effective against microbes or able to recognize the pattern molecular of microorganisms.
Key words: Purification, characterization, Antimicrobial activity, Periplaneta americana.
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