Recovery and Characterization of a 30.7-kDa Protein from Bacillus licheniformis Associated with Inhibitory Activity Against Methicillin-Resistant Staphylococcus aureus, Vancomycin-Resistant Enterococci, and Listeria monocytogenes |
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Authors: | Mamdoh T Jamal Peter C Morris Rasmus Hansen Derek J Jamieson J Grant Burgess Brian Austin |
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Institution: | (1) School of Life Sciences, John Muir Building, Heriot-Watt University, Riccarton, Edinburgh, EH14 4AS, Scotland, UK;(2) Present address: School of Marine Science and Technology, Armstrong Building, University of Newcastle upon Tyne, Newcastle upon Tyne, NE1 7RU, England, UK |
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Abstract: | Of 131 bacterial isolates from seaweed, a culture of Bacillus licheniformis produced a novel protein with antibacterial activity against methicillin-resistant Staphylococcus aureus, vancomycin-resistant enterococci, and Listeria monocytogenes. The antibacterial activity was maximal in cultures prepared in Columbia broth containing pieces of synthetic polyurethane
sponge and shaken at 210 to 230 rpm. Antibacterial activity was not found in cultures grown statically or with different speeds
of rotary shaking. Reduced activity was apparent in supernatants prepared from marine 2216E broth and tryptone soya broth
with or without 1% (wt/vol) sodium chloride. The antibacterial compound was sensitive to proteinase K, pronase, and trypsin,
but was not affected by Tween−20, −40, −60, or −80, or α− or β-amylase. Activity was not adversely affected by heating up
to 40°C or treatment at pH 5 to 14. The bioactive compound was determined to be associated with a protein of 30.7 kDa, which
had homology to the YbdN protein of B. licheniformis ATCC 14580. |
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Keywords: | antibacterial protein Bacillus licheniformis MRSA VRE |
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