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 |
Author(s): | 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 |
Date Deposited: | 7-Aug-2012 |
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. https://doi.org/10.1007/s10126-005-6160-4 |
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. |
DOI Link: | 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. |
Licence URL(s): | http://www.rioxx.net/licenses/under-embargo-all-rights-reserved |
File | Description | Size | Format | |
---|---|---|---|---|
jamaletal_marinebiotechnology_2006.pdf | Fulltext - Published Version | 384.12 kB | Adobe PDF | Under Permanent Embargo Request a copy |
Note: If any of the files in this item are currently embargoed, you can request a copy directly from the author by clicking the padlock icon above. However, this facility is dependent on the depositor still being contactable at their original email address.
This item is protected by original copyright |
Items in the Repository are protected by copyright, with all rights reserved, unless otherwise indicated.
The metadata of the records in the Repository are available under the CC0 public domain dedication: No Rights Reserved https://creativecommons.org/publicdomain/zero/1.0/
If you believe that any material held in STORRE infringes copyright, please contact library@stir.ac.uk providing details and we will remove the Work from public display in STORRE and investigate your claim.