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• W2550955145 abstract "A marine halophile, Halomonas sp. strain M3 was isolated from Straits of Johor, Malaysia and produce bacteriocin CC that acts as bacteriostatic agent. Characterisation of the bacterium showed that optimal growth and bacteriocin production is at ambient temperature, pH of 8-8.5 in nutrient broth medium supplemented with 2.9% w/v NaCI to mimic saltwater conditions. The stability studies indicated that bacteriocin CC is heat-labile (35°C-50°C) and was stable over 2 years when stored in 0.02M Tris- HCI with 30-60% glycerol at 4°C. A loss of activity was detected after proteolytic enzymes treatment, indicating the proteinaceous nature of the antimicrobial compound. The amino acid sequence of bacteriocin CC was obtained by Edman degradation and MALDI-TOF analysis, showed the characteristic sequence of a DING protein (D-I-N-G-G-G-A-T-L-P-Q-A-LY- Q) in size 38.9-kDa at pI of 6.8. These proteins constitute a conserved and widely distributed set of proteins found in all kingdoms with ligand-binding activities and hydrolytic enzyme, suggesting a possible role in cell signalling and bio mineralization in DING isolates. Intriguingly, DING proteins also have been involved as an anti-tumour agent in humans. Thus, bacteriocin CC as DING protein family members should be further studied to investigate its potential as a novel antimicrobial agent. © 2015, Malaysian Society of Analytical Sciences." @default.
• W2550955145 created "2016-11-30" @default.
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• W2550955145 date "2015-01-01" @default.
• W2550955145 modified "2023-09-28" @default.
• W2550955145 title "BACTERIOCIN ISOLATED FROM HALOMONAS SP.: A BACTERIAL DING PROTEIN?" @default.
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