Isolation and characterization of a new bacteriocin, termed enterocin M, produced by environmental isolate Enterococcus faecium AL41.
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 4628 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 (4701.25). 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.
Mareková
Mária
M
Institute of Medical Chemistry, Biochemistry and Clinical Biochemistry, Medical Faculty UPJS, Tr. SNP 1, 040 01 Kosice, Slovakia.
Lauková
Andrea
A
Skaugen
Morten
M
Nes
Ingolf
I
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000302:isolation & purification*; D001952:Bridged-Ring Compounds / Q000302:isolation & purification / Q000378:metabolism; D002845:Chromatography; D016984:Enterococcus faecium / Q000737:chemistry*; D008969:Molecular Sequence Data; D008970:Molecular Weight
D000900:Anti-Bacterial Agents; D001952:Bridged-Ring Compounds; C012306:enterocin