TY - JOUR
T1 - 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
AU - Jamal, Mamdoh T.
AU - Morris, Peter C.
AU - Hansen, Rasmus
AU - Jamieson, Derek J.
AU - Burgess, J. Grant
AU - Austin, Brian
PY - 2006/12
Y1 - 2006/12
N2 - 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 a- or ß-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. © 2006 Springer Science+Business Media, Inc.
AB - 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 a- or ß-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. © 2006 Springer Science+Business Media, Inc.
KW - Antibacterial protein
KW - Bacillus licheniformis
KW - MRSA
KW - VRE
UR - http://www.scopus.com/inward/record.url?scp=33846230094&partnerID=8YFLogxK
U2 - 10.1007/s10126-005-6160-4
DO - 10.1007/s10126-005-6160-4
M3 - Article
SN - 1436-2228
VL - 8
SP - 587
EP - 592
JO - Marine Biotechnology
JF - Marine Biotechnology
IS - 6
ER -