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Applied and Environmental Microbiology, July 2009, p. 4273-4276, Vol. 75, No. 13
0099-2240/09/$08.00+0 doi:10.1128/AEM.02772-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Laboratoire de Chimie Analytique et Sciences de l'Aliment, IPHC-DSA, Université de Strasbourg, CNRS, 67400 Illkirch,1 Aérial, Parc d'Innovation, 67412 Illkirch, France2
Received 5 December 2008/ Accepted 26 April 2009
Enterococcus faecalis WHE 96, a strain isolated from soft cheese based on its anti-Listeria activity, produced a 5,494-Da bacteriocin that was purified to homogeneity by ultrafiltration and cation-exchange and reversed-phase chromatographies. The amino acid sequence of this bacteriocin, named enterocin 96, was determined by Edman degradation, and its structural gene was sequenced, revealing a double-glycine leader peptide. After a comparison with other bacteriocins, it was shown that enterocin 96 was a new class II bacteriocin that showed very little similarity with known structures. Enterocin 96 was indeed a new bacteriocin belonging to class II bacteriocins. The activity spectrum of enterocin 96 covered a wide range of bacteria, with strong activity against most gram-positive strains but very little or no activity against gram-negative strains.
Published ahead of print on 1 May, 2009.
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