Open AccessDivergicin 750, a novel bacteriocin produced by Carnobacterium divergens 750
Author(s) -
Hoick Askild,
Axelsson Lars,
Schillinger Ulrich
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08043.x
Subject(s) - bacteriocin , edman degradation , peptide sequence , biology , peptide , amino acid , ammonium sulfate precipitation , biochemistry , listeria monocytogenes , molecular mass , enterococcus faecium , microbiology and biotechnology , bacteria , gene , size exclusion chromatography , genetics , antimicrobial , enzyme , antibiotics
Divergicin 750, a bacteriocin produced by Carnobacterium divergens 750, preferentially inhibited the growth of strains of Carnobacterium and Enterococcus . Selected strains of Listeria monocytogenes and Clostridium perfringens were also inhibited. The bacteriocin was purified to homogeneity by ammonium sulfate precipitation and sequential S‐Sepharose, hydrophobic interaction and reversed phase chromatography. The complete amino acid sequence was determined by Edman degradation. The peptide consisted of 34 amino acid residues. The calculated ifM r from the peptide sequence, 3447.7, agreed well with that obtained by mass spectrometry. Divergicin 750 did not show any sequence similarities to other known bacteriocins. The plasmid‐located structural gene encoding divergicin 750 ( dvn750 ) was cloned and sequenced. The gene encoded a primary translation product of 63 amino acids with a deduced M rmr = 6789.4 which is cleaved between amino acid residues 29 and 30 to yield the mature bacteriocin.