Purification and partial amino acid sequence of thuricin S, a new anti-Listeriabacteriocin from Bacillus thuringiensis

Canadian Journal of Microbiology - Tập 53 Số 2 - Trang 284-290 - 2007
Sonia Chehimi1,2,3,4, D. François1,2,3,4, Sophie Sablé1,2,3,4, Mohamed-Rabeh Hajlaoui1,2,3,4, Alain Van Dorsselaer1,2,3,4, Férid Limam1,2,3,4, Anne‐Marie Pons1,2,3,4
1Laboratoire de biotechnologies et de chimie bio-organique, Pôle Sciences, Université de La Rochelle, 17042 La Rochelle CEDEX 01, France
2Laboratoire de protection des végétaux, Institut national des recherches agronomiques de Tunisie, 2049 Ariana, Tunisie
3Laboratoire de spectrométrie de masse bio-organique, Université Louis Pasteur, 67087 Strasbourg CEDEX 2, France
4Laboratoire interactions légumineuses–microorganismes, Centre de biotechnologie, Technopôle Borj-Cédria, B.P. 95-2050 Hammam-Lif, Tunisie

Tóm tắt

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.

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Canadian Journal of Microbiology

Tập 53 Số 2

284-290

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