Please use this identifier to cite or link to this item: http://hdl.handle.net/1893/7219
Appears in Collections:Aquaculture Journal Articles
Peer Review Status: Refereed
Title: 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
Authors: Jamal, Mamdoh T
Morris, Peter C
Hansen, Rasmus
Jamieson, Derek
Burgess, Grant
Austin, Brian
Contact Email: brian.austin@stir.ac.uk
Keywords: antibacterial protein
Bacillus licheniformis
MRSA
VRE
Issue Date: Nov-2006
Publisher: Springer
Citation: Jamal MT, Morris PC, Hansen R, Jamieson D, Burgess G & Austin B (2006) 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, Marine Biotechnology, 8 (6), pp. 587-592.
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. licheniformi
Type: Journal Article
URI: http://hdl.handle.net/1893/7219
DOI Link: http://dx.doi.org/10.1007/s10126-005-6160-4
Rights: The publisher does not allow this work to be made publicly available in this Repository. Please use the Request a Copy feature at the foot of the Repository record to request a copy directly from the author. You can only request a copy if you wish to use this work for your own research or private study.
Affiliation: Heriot-Watt University
Heriot-Watt University
Heriot-Watt University
Heriot-Watt University
Newcastle University
Heriot-Watt University

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