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Isolation and characterization of a new bacteriocin, termed enterocin M, produced by environmental isolate Enterococcus faecium AL41

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Journal of Industrial Microbiology & Biotechnology

Abstract

The new bacteriocin, termed enterocin M, produced by Enterococcus faecium AL 41 showed a wide spectrum of inhibitory activity against the indicator organisms from different sources. It was purified by (NH4)2SO4 precipitation, cation-exchange chromatography and reverse phase chromatography (FPLC). The purified peptide was sequenced by N-terminal amino acid Edman degradation and a mass spectrometry analysis was performed. By combining the data obtained from amino acid sequence (39 N-terminal amino acid residues was determined) and the molecular weight (determined to be 4 628 Da) it was concluded that the purified enterocin M is a new bacteriocin, which is very similar to enterocin P. However, its molecular weight is different from enterocin P (4 701.25). Of the first 39 N-terminal residues of enterocin M, valine was found in position 20 and a lysine in position 35, while enterocin P has tryptophane residues in these positions.

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Acknowledgments

This work was supported by the project No. 2/5139/27 of the Slovak Scientific Agency VEGA and on the base of financial support of Dr. M. Mareková by Research Council of Norway during her stay in the Laboratory of Microbial Gene Technology NLH in As, Norway. We are grateful to Dr. Simonová and Dr. Szabóová for antimicrobial activity testing using rabbits isolates.

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Correspondence to Andrea Lauková.

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Mareková, M., Lauková, A., Skaugen, M. et al. Isolation and characterization of a new bacteriocin, termed enterocin M, produced by environmental isolate Enterococcus faecium AL41. J Ind Microbiol Biotechnol 34, 533–537 (2007). https://doi.org/10.1007/s10295-007-0226-4

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  • DOI: https://doi.org/10.1007/s10295-007-0226-4

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