Purification, Characterization and in vitro Anti microbial Activity of Marine Bacterium Proteins: Pseudomonas sp

Abstract The marine water samples were collected from the Kilakarai deep sea, the bacterial colonies were isolated and the dominated colonies were picked out and their morphological characterization was studied. From the biochemical characterization the isolated colony results as Bacillus sp. The antimicrobial potential were analysed and the resulted Fraction I, Fraction II, Fraction III shows the greater effect when against with the clinical pathogens. Staphylococcus aureus, Pseudomonas sp, Fraction III shows greater zone of inhibition in various concentration of (25 µl, 50 µl, 75 µl, 100 µl). The higher concentration of 100 µl of sample shows the greater results. The high concentration of the 100 µl of the crude sample exhibit higher zone of inhibition against the Staphylococcus sp (14mm), Pseudomonas (13mm), The results suggested that the fraction-III warranted further purification in order to unveil the active components of Pseudomonas sp. From the curve of elution in DEAE Sepharose Fast Flow chromatography Three A280 nm peak fractions, named G-1, G-2, G-3 were collected respectively. The antimicrobial potential of the marine microbes the G-1, G-2, G-3 shows the greater effect when against with the clinical pathogens. Staphylococcus aureus, Pseudomonas sp. Among that G-3 shows the maximum results of 18.2 mm and 15.4mm against Staphylococcus aureus, Pseudomonas sp respectively. The present study crude extract of marine bacillus showed anticancer activity against HT‐15and HT‐29 cell line in a dose dependant manner. The crude extract of of marine Bacillus sp showed activity of 7.88 at 400µg/ml. Whereas, the purified crude of fraction I, fraction II and Fraction III showed 7.99% , 20.67% and29.30% of inhibition at the same concentration respectively against HT‐15 and the purified crude of fraction I, fraction II and Fraction III showed 8.0% , 9.12% and13.02% of inhibition at the same concentration respectively against HT‐29. The purified sample of G1, G2 and G3showed 18.63 , 15.80% and76.31% of inhibition at the same concentration respectively against HT‐15 and the purified sample of G1, G2 and G3showed 12.90% , 12.53% and69.32% of inhibition at the same concentration respectively against HT‐29. Estimation of amino acids was done using an automatic amino acid analyzer for the two fractions of FIII and G3.