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- Title
Purification and partial amino acid sequence of thuricin S, a new anti-Listeria bacteriocin from Bacillus thuringiensis.
- Authors
Chehimi, Sonia; Delalande, François; Sablé, Sophie; Hajlaoui, Mohamed-Rabeh; Van Dorsselaer, Alain; Limam, Férid; Pons, Anne-Marie
- Abstract
We report the isolation and characterization of a new bacteriocin, thuricin S, produced by the Bacillus thuringiensis subsp. entomocidus HD198 strain. This antibacterial activity is sensitive to proteinase K, is heat-stable, and is stable at a variety of pH values (3–10.5). The monoisotopic mass of thuricin S purified by high perfomance liquid chromatography, as determined with mass spectrometry ESI-TOF-MS, is 3137.61 Da. Edman sequencing and NanoESI-MS/MS experiments provided the sequence of the 18 N-terminal amino acids. Interestingly, thuricin S has the same N-terminal sequence (DWTXWSXL) as bacthuricin F4 and thuricin 17, produced by B. thuringiensis strains BUPM4 and NEB17, respectively, and could therefore be classified as a new subclass IId bacteriocin.
- Subjects
AMINO acid sequence; BACTERIOCINS; PROTEINASES; BACILLUS thuringiensis; LIQUID chromatography; MASS spectrometry
- Publication
Canadian Journal of Microbiology, 2007, Vol 53, Issue 2, p284
- ISSN
0008-4166
- Publication type
Article
- DOI
10.1139/W06-116